diff --git a/00-preface.Rmd b/00-preface.Rmd index d5f0f16cc68dbc8f93ce36df30e4204a2d142e7a..8049997a455f3ec3ceafc30950f2d18cfb2ca783 100644 --- a/00-preface.Rmd +++ b/00-preface.Rmd @@ -1,7 +1,7 @@ \phantomsection \pdfbookmark[0]{Title Page}{title} <!-- Title, name and date --> - \title{\LARGE {\bf Investigation of the selective toxicity of neonicotinoids using the nematode worm Caenorhabditis elegans}\\ + \title{\LARGE \textbf {Investigation of the selective toxicity of neonicotinoids using the nematode worm \textit {\textbf {Caenorhabditis elegans}}}\\ \vspace*{6mm}} \author{Monika Kudelska} \maketitle diff --git a/01-intro.Rmd b/01-intro.Rmd index 2f479cc1e396719d40069eb8c408102709723de7..658576553782eb5cefdcbdda7f74abc53b845857 100644 --- a/01-intro.Rmd +++ b/01-intro.Rmd @@ -41,7 +41,7 @@ library(kableExtra) In 1970s, the scientists of Shell Development Company Biological Research Centre in California identified alpha- DBPN (2-(dibromonitromethyl)-3-(methylpyridine)), first synthesised by Prof. Henry Feuer [@feuer1986]. This lead compound showed low insecticidal activity against aphid and house fly [@tomizawa2003; @tomizawa2005]. Structural alterations of DBPN resulted in production of nithiazine (Figure \@ref(fig:neonics-structure-label)). Nithiazine showed improved insecticidal activity and was particularly effective as a new housefly repellent [@kollmeyer1999]. Further replacement of the thiazine ring by chloropyridinylmethyl (CPM) group, addition of the imidazolidine or its acyclic counterpart, and retention of the nitromethylene group resulted in generation of more potent compounds, one of which, nitenpyram, exhibited particularly high efficacy. Regrettably, both nithiazine and nitenpyram are not useful in fields, as they are unstable in light. The latter however is successfully used in veterinary medicine as an external parasite treatment for cats and dogs. -To solve the issue of photo-instability, nitromethylene group (CCHNO2) was replaced by nitroguanidine (CNNO2) and cyanoamidine (CNCN) (Figure \@ref(neonics-structure-label) and @kagabu1995). These chemical moieties have absorbance spectra at much shorter wavelengths hence do not degrade upon exposure to sunlight. Further alterations, such as replacement of imidazolidine by thiazolidine or oxadiazinane, and/or chloropyridinylmethyl by chlorothiazole or tetrahydrofuran (THF) did not hinder insecticidal activity [@yamamoto1999]. As a result of these modifications, all 6 currently used neonicotinoids were synthesised. They are grouped according to their pharmacophore into N-nitroguanidines, nitromethylenes and N-cyanoamidines (Figure \@ref(fig:neonics-structure-label)). Generally compounds with acyclic- guanidine or amidine and with nitromethylene are more efficacious against moth- and butterfly- pests than those with cyclic counterparts or nitroimine respectively [@ihara2006], nevertheless all are commonly used in agriculture. Imidacloprid, currently the most widely used neonicotinoid, was synthesised in 1970 in Bayer Agrochemical Japan and introduced to the EU market in 1991. Its trade names include Confidor, Admire and Advantage. Together with thiacloprid (Calypso), imidacloprid is marketed by Bayer CropScience. Thiamethoxam (Actara) is produced by Syngenta, Clothianidin (Poncho, Dantosu, Dantop) and Nitenpyram (Capstar) by Sumitomo Chemical, acetamiprid (Mospilan) by Certis, whereas dinotefuran (Starkle) by Mitsui Chemicals company. Last neonicotinoid (dinotefuran) was launched in the EU in 2008. +To solve the issue of photo-instability, nitromethylene group (CCHNO2) was replaced by nitroguanidine (CNNO2) and cyanoamidine (CNCN) (Figure \@ref(fig:neonics-structure-label) and @kagabu1995). These chemical moieties have absorbance spectra at much shorter wavelengths hence do not degrade upon exposure to sunlight. Further alterations, such as replacement of imidazolidine by thiazolidine or oxadiazinane, and/or chloropyridinylmethyl by chlorothiazole or tetrahydrofuran (THF) did not hinder insecticidal activity [@yamamoto1999]. As a result of these modifications, all 6 currently used neonicotinoids were synthesised. They are grouped according to their pharmacophore into N-nitroguanidines, nitromethylenes and N-cyanoamidines (Figure \@ref(fig:neonics-structure-label)). Generally compounds with acyclic- guanidine or amidine and with nitromethylene are more efficacious against moth- and butterfly- pests than those with cyclic counterparts or nitroimine respectively [@ihara2006], nevertheless all are commonly used in agriculture. Imidacloprid, currently the most widely used neonicotinoid, was synthesised in 1970 in Bayer Agrochemical Japan and introduced to the EU market in 1991. Its trade names include Confidor, Admire and Advantage. Together with thiacloprid (Calypso), imidacloprid is marketed by Bayer CropScience. Thiamethoxam (Actara) is produced by Syngenta, Clothianidin (Poncho, Dantosu, Dantop) and Nitenpyram (Capstar) by Sumitomo Chemical, acetamiprid (Mospilan) by Certis, whereas dinotefuran (Starkle) by Mitsui Chemicals company. Last neonicotinoid (dinotefuran) was launched in the EU in 2008. Research into novel neonicotinoids continues [@shao2013]. In the last decade, several novel insecticides have been characterised and approved for use in the EU. Sulfoxafrol [@zhu2011; @eu2019a] and flupyradifurone [@nauen2015; @eu2019b] have been classified as representatives of new chemical classes, namely sulfoximines and butenolides. However, due to their mode of action and similar biochemical properties, some argue that they are in fact neonicotinoids, whereas their mis-classification has been deliberate to avoid association with neonicotinoids [@pan2019]. @@ -348,7 +348,7 @@ The effects of neonicotinoids on the neuronal transmission was investigated on i @sone1994 investigated the effects of imidacloprid on the neuronal activity at the thoracic ganglia of male adult American cockroaches, *Periplaneta americana* using extracurricular recordings. This method allows for a record of changes in spontaneous neuronal activity in response to mechanical or pharmacological interventions. At a very low concentration of 1 nM, imidacloprid induced a sustained for over 2 minutes increase in the rate of neuronal firing. At concentrations ranging from 10 nM to 100 $\mu$M, the following sequence of events was noted: an increase of the rate of spontaneous action potentials of neurons followed by a gradual decline, leading to a complete block of neuronal activity [@sone1994]. Imidacloprid had the same effect on various insect preparations including thoracic ganglion of the Leptinotarsa decemlineata [@tan2008] and on the abdominal ganglion of *Periplaneta americana* [@buckingham1997]. The same observations were made for other neonicotinoids [@thany2009; @schroeder1984]. This provided evidence that neonicotinoids stimulate the nervous system of insects. This conclusion was supported by the behavioural observation, whereby the neonicotinoid intoxication mirrors intoxication seen with cholinergic agents (Section . In response to imidacloprid, insects become hyper excited as evident by excessive pacing. They then collapse and exhibit diminishing uncoordinated leg and abdomen movement until eventual death [@sone1994; @elbart1997; @suchail2001]. Sub-lethal doses (i.e. < 4 nM) have distinct effect, such as an inhibition of feeding leading to starvation [@nauen1995; @elbart1997]. -@sattelle1989 used isolated cocroach neuronal preparation to record post-synaptic intracellular currents in response to neonicotinoid prototype 2(nitromethylene) tetrahydro-1, 3-thiazine (NMTHT). NMTHT depolarised the post-synaptic unpaired median neurons and the cell body of motor neurons of the abdominal ganglion. Agriculturally relevant neonicotinoids had the same effect on the post-synaptic membrane of the isolated cocroach thoracic ganglia [@tan2007; @thany2009] potato beetle isolated neurons [@tan2008], and on cultured cocroach [@ihara2006], honeybee [@palmer2013] and fruit fly [@brown2006] neurons. These data provide evidence that neonicotinoids act directly on the post-synaptic neuron in both target and non-target insects. +@sattelle1989 used isolated cocroach neuronal preparation to record post-synaptic intracellular currents in response to neonicotinoid prototype 2(nitromethylene) tetrahydro-1, 3-thiazine (NMTHT). NMTHT depolarised the post-synaptic unpaired median neurons and the cell body of motor neurons of the abdominal ganglion. Agriculturally relevant neonicotinoids had the same effect on the post-synaptic membranes in the isolated cocroach thoracic ganglia [@tan2007; @thany2009] potato beetle isolated thoracic ganglion [@tan2008], terminal abdominal ganglion of the americal cocroach [@ihara2006] and in the honeybee [@palmer2013] and fruit fly [@brown2006] neurons. Pharmacological characterisation of neonicotinoids-induced currents provided further evidence for their mode of action. The inward current elicited by neonicotinoids were dose-dependent, whereby the higher the concentration, the grater the depolarisation. EC50 values (concentrations at which the half of the maximum current was observed) are in the region of 1 - 5 $\mu$M [@thany2009; @tan2007]. Such low values indicate highly potent action of neonicotinoids on insects, in agreement with toxicological data (Section \@ref(potentpests)). Neonicotinoid-induced currents were reminiscent of those induced by acetylcholine and nicotine, and were prevented by the application of nAChRs antagonists ($\alpha$-bungarotoxin, methyllycaconitine, mecamylamine or d-tubocurarine) not by muscarinic receptor antagonists (atropine, pirenzepine), suggesting neonicotinoid-induced currents are due to the activation of nicotinic receptors. @@ -586,7 +586,7 @@ Recombinant insect nAChR are notoriously difficult to express. Several intervent ## General biology ##{#genbiology} -*C. elegans* exists as a male and hermaphrodite, with the latter sex being the more prevalent one. In the lab, 99.9 % of worms are hermaphrodites, which self-fertilize their eggs. *C. elegans* has a fast life-cycle (www.wormbook.org), which is temperature-dependent. At 15^o^C, it takes 5.5 days from egg-fertilization to the development of a worm into an adult. This process is shortened to 3.5 and 2.5 days at 20 and 25 deg;C, respectively (Figure \@ref(fig:life-cycle-label)). At 20 degrees, hermaphrodite lay eggs 2.5 hours after the fertilisation. 8 hours later the embryo hatches as a larvae in the first stage of its development (L1). In the presence of food, larvae develops into an adult through three further developmental stages, namely L2, L3 and L4. The transition between each larval stage is marked by a process of maulting, during which the old cuticle is shed and replaced by a new one. In the absence of food, developing L2 and L3 worms enter the dauer stage. The worms can remain arrested at this low metabolic activity state for up to several weeks, and will develop into adults, should the food re-appear. Hermaphrodites remain fertile for the first three days of their adulthood. Their eggs can be fertilised internally with the sperm produced by the hermaphrodite, or, if there are males available, by mating. Unmated worm can lay up to 350 eggs, whereas mated over a 1000 eggs. Figure \@ref(fig:life-cycle-label) illustrated the full *C. elegans* life cycle. +*C. elegans* exists as a male and hermaphrodite, with the latter sex being the more prevalent one. In the lab, 99.9 % of worms are hermaphrodites, which self-fertilize their eggs. *C. elegans* has a fast life-cycle (www.wormbook.org), which is temperature-dependent. At 15^o^C, it takes 5.5 days from egg-fertilization to the development of a worm into an adult. This process is shortened to 3.5 and 2.5 days at 20 and 25 $^\circ$C, respectively (Figure \@ref(fig:life-cycle-label)). At 20 degrees, hermaphrodite lay eggs 2.5 hours after the fertilisation. 8 hours later the embryo hatches as a larvae in the first stage of its development (L1). In the presence of food, larvae develops into an adult through three further developmental stages, namely L2, L3 and L4. The transition between each larval stage is marked by a process of maulting, during which the old cuticle is shed and replaced by a new one. In the absence of food, developing L2 and L3 worms enter the dauer stage. The worms can remain arrested at this low metabolic activity state for up to several weeks, and will develop into adults, should the food re-appear. Hermaphrodites remain fertile for the first three days of their adulthood. Their eggs can be fertilised internally with the sperm produced by the hermaphrodite, or, if there are males available, by mating. Unmated worm can lay up to 350 eggs, whereas mated over a 1000 eggs. Figure \@ref(fig:life-cycle-label) illustrated the full *C. elegans* life cycle. (ref:life-cycle) **The life cycle of *C. elegans*.** *C. elegans* develops into an adult through 4 larval stages L1- L4. These stages are separated by molts associated with shedding of an old and exposure of a new cuticle. Adults emerge can lay over a 1000 eggs a day which hatch within several hours. Dauer stage is a metabolic compromised worm stage entered in the absence of food. Upon re-appearance of food, worms develop into L4 and adults normally. Figure taken from www.wormatlas.org. diff --git a/01-intro_2.Rmd b/01-intro_2.Rmd index 7e42fc2117f71f9720598842387d1dc16c40a4bb..afef511df31bb6440bd5f28cfdeec658cc23093c 100644 --- a/01-intro_2.Rmd +++ b/01-intro_2.Rmd @@ -196,7 +196,6 @@ Clothianidin and thiacloprid at concentrations $\ge$ than 1.2 $\mu$M and the EC5 ##### Soil nematodes #####{soilnematodesneonicstoxicity} Neonicotinoids also induce a sublethal effect on the the free-living nematode *C. elegans*. Thiacloprid and imidacloprid have an effect on the reproduction of *C. elegans* with EC50 of 1.14 nM and 2.09 mM, respectively [@gomez-eyles2009]. Thiacloprid at 37 nM has an effect on chemosensing, whereas at 18 $\mu$M it impairs motility of this free living nematode [@hopewell2017]. Impaired motility of *C. elegans* in response to $\ge$ 120 $\mu$M imidacloprid was also recorded [@mugova2018]. Taken together, neonicotinoids have sublethal effects on earth worms and soil nematodes at concentrations as low as nM. - Most of the doses effective against worms are higher than the average doses of neonicotinoids in the field. However, the presence of clothianidin, imidacloprid and thiamethoxam has been detected at lower than average levels, such as 80.10 nM for imidacloprid, 23.01 nM for imidacloprid and 68.56 nM for thiamethoxam [@jones2014]. This suggests that the environmentally relevant concentrations of neonicotinoids may negatively impact on the the well-being of soil dwellers. <!-- Data regarding toxicity of neonicotinoids on soil worms and nematodes focuses on earthworm *Eisenia fetida* (*E. fetida*, redworm). The toxicity is assessed either following treatment in solution or in the artificial soils. In solution, the LC50 of imidacloprid after 24 hour exposure is 62.08 $\mu$M [@luo1999]. This increases to 24.24 $\mu$M after 48 hour exposure [@luo1999]. Clothianidin is less potent; its LC50 after 14 days is 24.27 $\mu$M [@decant2010]. --> @@ -301,30 +300,41 @@ Genetic studies identified other amino acids with a potential importance in conf Loop B, D and G originate from the complementary site, but the principal site may also play a role. Studies on Drosophila/chicken $\alpha2\beta2$ hybrid and chicken $\alpha2\beta4$ receptors showed that the presence of nonpolar proline in YXCC motif of loop C enhances affinity, whereas mutation of proline to glutamate markedly reduces affinity of neonicotinoids to these receptors [@shimomura2005]. The importance of C-loop regions was also demonstrated by @meng2015 who showed that chimera receptors are deferentially sensitive to imidacloprid at least partly due to the difference in loop C region, equivalent to Ls184-191. -### Cholinergic neurotransmission +### Cholinergic system in insects + +#### Enzymes at the cholinergic synapse <!-- Upon arrival of an electrical signal at the presynpatic terminal, acetylcholine is released into the synaptic cleft. It then binds to nicotinic acetylcholine receptors (nAChRs) expressed at the post-synpatic membrane. Binding of acetylcholine results in depolarisation and excitation of the post-synaptic neurons, or muscle contraction at the neuromusclular junction (NMJ) [@hille1978]. Acetylcholine can also act on other class of receptors, the metabotropic cholinergic G-protein coupled receptor, which are involved in the modulatation of neurotransmission release. The acetylcholine-evoked signal is terminated mainly by synaptic enzyme cholinesterase which hydrolyses acetylcholine to choline and acetate [@fukuto1990], but also by choline uptake to the presynaptic cell by Na^+^-choline transporter. --> -Cholinergic neurotransmission is the process of signal propagation between neurons as well as neurons and muscle cells mediated by a neurotransmitter acetylcholine (ACh) (Figure \@ref(fig:cholineric-synapse-label)) [@williamson2009]. +nAChRs mediate fast synaptic transmission at the cholinergic synapse. Cholinergic neurotransmission is the process of signal propagation between neurons as well as neurons and muscle cells mediated by a neurotransmitter acetylcholine (ACh) [@williamson2009]. Cholinergic synapse is characterised by the presence of several proteins which mediate the breakdown, the synthesis and processing of the neurotransmitter (Figure \@ref(fig:cholineric-synapse-label)). + +##### Choline acetyltransferase + +Choline acetyltransferase (ChAT) is an enzyme synthesising ACh [@greenspan1980b], by a transfer of acetyl-choA onto choline. There are at least two isoforms in Drosophila, which are produced by alternative splicing from the ChAT gene [@slemmon1982]. One is membrane bound, whereas the other is soluble, both of which are 75 kDa [@pahud1998]. The soluble isoform performs the mojority of enzymatic activity. A 65 kDa soluble isoform of ChAT was also isolated from the Locust *Schistocerca gregaria* [@lutz1988] + +##### Vesicular acetylcholine transferase + +Vesicular acetylcholine transferase (VAChT) mediates ATP-dependent transport [@varoqui1996], which packs ACh into the synaptic vesicles for release [@song1997]. In Drosophila, a single VAChT gene was identified. It is embeddded within the ChAT gene [@kitamoto1998]. + +##### Acetylcholinesterase -The function and properties of these receptors were studied using mammalian and amphibian muscle preparations. +Acetylcholinesterase (ACE) is a soluble enzyme that catalyses breakdown of ACh [@chao1980; @hsiao2004]. In Drosophila, it is encoded by the Ace locus [@hall1976]. Acetylcholinesterase is a homodimer covalently bonded by the disulphide bridge [@chao1980; @hsiao2004]. Each monomeric subunits is ~67 kDa, folded into 4-helix bundle [@harel2000]. -In 1930s, @brown1936; @bacq1937 demonstrated that the application of acetylcholine, as well as nicotine and choline to the isolated mammalian muscle leads to sustained contraction, as showed by the increase in the muscle tension. The muscle contraction was associated with an increase in the frequency of the action potential firings [@brown1936] and the depolarisation of the end-plate [@katz1957]. Acetylcholine-evoked responses could be inhibited by pre-incubation with several compounds, including snake venom proteins, $\alpha$-bungarotoxin [@chang1963]. +<!-- The function and properties of these receptors were studied using mammalian and amphibian muscle preparations. --> -Prolonged exposure to high concentration of agonist has a secondary effects on the muscle: desensitisation [@katz1957]. Desensitisation is a post-contraction period, after the removal of the agonist, at which the muscle is relaxed and a subsequent contraction cannot be elicited [@thesleft1955]. Recovery from desensitisation typically lasts few seconds after the agonist removal [@bouzat2008], however the duration varies depending on the receptor, the compound [@briggs1998] and its concentration [@gerzanich1994]. Full recovery may not occur or may be slower if the receptor are exposed to the large doses of agonist for a prolonged time [@katz1957]. +<!-- In 1930s, @brown1936; @bacq1937 demonstrated that the application of acetylcholine, as well as nicotine and choline to the isolated mammalian muscle leads to sustained contraction, as showed by the increase in the muscle tension. The muscle contraction was associated with an increase in the frequency of the action potential firings [@brown1936] and the depolarisation of the end-plate [@katz1957]. Acetylcholine-evoked responses could be inhibited by pre-incubation with several compounds, including snake venom proteins, $\alpha$-bungarotoxin [@chang1963]. --> -Biochemical, electrophysiological, genetic and pharmacological approaches were utilised to identify the role of nAChRs in neurotransmission. nAChRs were solubilised and purified from the electric organ of the *Torpedo* and reconstituted into liposomes [@anholt1982]. In the presence of acetylcholine and other agonists, the ionic current was elicited, confirming nAChR is an ion channel [@anholt1982]. Acetylcholine evoked activation ans desensitisation of nAChRs, which correspond to the effects in the muscle, provided evidence that nAChRs mediate fast synaptic transmission at the cholinergic synapse. +<!-- Prolonged exposure to high concentration of agonist has a secondary effects on the muscle: desensitisation [@katz1957]. Desensitisation is a post-contraction period, after the removal of the agonist, at which the muscle is relaxed and a subsequent contraction cannot be elicited [@thesleft1955]. Recovery from desensitisation typically lasts few seconds after the agonist removal [@bouzat2008], however the duration varies depending on the receptor, the compound [@briggs1998] and its concentration [@gerzanich1994]. Full recovery may not occur or may be slower if the receptor are exposed to the large doses of agonist for a prolonged time [@katz1957]. --> -Kinetic properties of nAChRs were studies with the patch clamp technique. Patch clamp is a technique which enables for the resolution of agonist-evoked responses at a single receptor level [@colquhoun1981; @colquhoun1985]. In response to acetylcholine the channel switches between active and inactive form, with the active form interrupted by the short-lived channel closing bursts. Temporal characterisation revealed the average duration of each event. The receptor remains opened for 1.4 ms; this is interrupted by channel closing bursts of 20 $\mu$s which occur at a frequency of 1.9 closures/opening burst. The mean period between the successive channel openings is 342 ms. Further experiments provided the showed that channel opening is not an all or nothing event. Instead, a channel exhibits multiple conductance states, one on which it is fully opened, named a full conductance state (i.e. the active form), and one in which the channel is partially opened, named the sub-conductance state [@colquhoun1985]. The fine structure of full conductance states (or opening bursts) and sub-conductance states varies depending on the agonist used and a receptor protein [@colquhoun1985; @nagata1996; @nagata1998]. +<!-- Biochemical, electrophysiological, genetic and pharmacological approaches were utilised to identify the role of nAChRs in neurotransmission. nAChRs were solubilised and purified from the electric organ of the *Torpedo* and reconstituted into liposomes [@anholt1982]. In the presence of acetylcholine and other agonists, the ionic current was elicited, confirming nAChR is an ion channel [@anholt1982]. Acetylcholine evoked activation ans desensitisation of nAChRs, which correspond to the effects in the muscle, provided evidence that nAChRs mediate fast synaptic transmission at the cholinergic synapse. --> -(ref:cholineric-synapse) **Chemical transmission at the cholinergic synapse.** Upon excitation of the presynaptic neuron (1), synaptic vesicles fuse with the membrane, releasing neurotransmitter (2). Neurotransmitter binds to the ligand-gated ion channel (LGIC) expressed on the post-synaptic membrane (3) leading to opening of ion channels and a flux of ions down their electrochemical gradient (4). This leads to either excitation or inhibition of the post-synaptic neuron (5). The signal is terminated by the action of cholinesterase which cleaves the ACh into choline and acetic acid. Choline is then transported back into the synapse and used to make more ACh. +<!-- Kinetic properties of nAChRs were studies with the patch clamp technique. Patch clamp is a technique which enables for the resolution of agonist-evoked responses at a single receptor level [@colquhoun1981; @colquhoun1985]. In response to acetylcholine the channel switches between active and inactive form, with the active form interrupted by the short-lived channel closing bursts. Temporal characterisation revealed the average duration of each event. The receptor remains opened for 1.4 ms; this is interrupted by channel closing bursts of 20 $\mu$s which occur at a frequency of 1.9 closures/opening burst. The mean period between the successive channel openings is 342 ms. Further experiments provided the showed that channel opening is not an all or nothing event. Instead, a channel exhibits multiple conductance states, one on which it is fully opened, named a full conductance state (i.e. the active form), and one in which the channel is partially opened, named the sub-conductance state [@colquhoun1985]. The fine structure of full conductance states (or opening bursts) and sub-conductance states varies depending on the agonist used and a receptor protein [@colquhoun1985; @nagata1996; @nagata1998]. --> + +(ref:cholineric-synapse) **Enzymes and transporters at the cholinergic synapse.** Upon release into the synaptic cleft, acetylcholine is broken down to choline and acetate by acetylcholinesterase (AChE). Choline is taken up to the pre-synapse by a choline transporter (ChT). The acetyl group in transferred onto choline to product acetylcholine; a reaction catalysed by choline transferase (ChAT). Generated acetylcholine is pumped back into the synaptic vesicle by the vesicular acetylcholine transporter (AChT) for re-cycling. ```{r cholineric-synapse-label, fig.cap="(ref:cholineric-synapse)", echo=FALSE, fig.scap= 'Chemical transmission at the cholinergic synapse.', fig.align='center', out.height = '60%', echo=FALSE} -knitr::include_graphics("fig/general_intro/png/synapse_general_2.png") +knitr::include_graphics("fig/general_intro/png/synapse_with_enzymes.png") ``` - <!-- This phenomenon is due to the distinct conformation of nAChRs, at in which they are not capable of ion conduction [@nemecz2016]. --> - -<!-- In the continual presence of agonist, the membrane potential gradually repolarises until it reaches the resting state, hovewer the next depolarisation will not occur, until the agonist are washed off and the receptor recovers from desensitisation [@katz1957]. --> <!-- Development of molecular cloning technique enabled for expression and kinetic characterisation of nAChRs. In 1985, @mishina1984 generated DNA constructs containing cDNA sequences encoding for the muscle type nAChR. These sequences were injected into the *Xenopus oocytes* [@mishina1984]. Upon application of acetylcholine, a current was recorded, suggesting successful cell surface expression. Single channel recordings revealed that in the presence of agonist, nAChR channel switches between active and inactive form. The active form comprises short-lived channel closing and opening [@mishina1986] and longer pauses in-between the receptor twitching. In addition, channel opening does not seem to be an all or nothing event. Instead, a channel exhibits multiple conductance states, one on which it is fully opened, named a full conductance state, and on in which the channel is partially opened, names sub-conductance state [@nagata1996; @nagata1998]. --> @@ -332,89 +342,213 @@ knitr::include_graphics("fig/general_intro/png/synapse_general_2.png") <!-- $\alpha$-bungarotoxin ($\alpha$-bgtx), is a 74-amino acid long, 8 kDa proteins isolated from the venom of a snake *Bungarus multicinctus*. It binds with high affinity to the NMJ post-synaptic membranes [@lee1967] and blocks synaptic responses evoked by acetylcholine and other agonists [@chang1963] by blocking the access of an agoinist to the nAChR binging site [@@mishina1984]. --> -## Biological relevance of the cholinergic neurotransmission ##{#insectachtransmission} +<!-- Behavioural analysis of Drosophila mutants in which cholinegic neurotransmission is diminished, provides evidence for the role of cholinergic neurotransmission in insects. Drosophila Ace null mutants are lethal: flies dye in the early development [@hall1976; @greenspan1980]. CAT mutants Lethal null mutation of drosophila choline acetyltransferase lethal flies dye during embryogenesis. some homozygus are viable but only at 18 deg c (temp sensitive) - some are temperature sensitive: viable at 18 deg due to the sufficient enzyme activity which is dimonished when flies placed in 30 deg. Upon sfift to high temp: characterisitc behaviour: loss of coordinated movement leading to paralysis and evenual death [@greenspan1980b] and disrupted cotrtnership behaviour. REDUCED MOTILITY IN vesicular acetylcholine transporter gene (Vacht) mutant [@kitamoto2000]. --> + +<!-- It is effective against plant insect pests [], and used in organic farming in form of tobacco tea [@isman2006] --> + +<!-- Exposure of insects to lethal dose of nicotine results in symptoms characteristic for the nervous system intoxication [@chadwick1947] and include increased locomotory activity, followed by convulsions, twitching and eventual death [@mcindoo1943]. --> + + +#### Localisation of cholinergic neurons in insects + +Enzymes present at the cholinergic synapse have been used as markers for detection of cholinerguic neurons in insects. (1) Immunocytochemistry with monoclonal antibodies specific to ChAt and ACE, (2) in-situ hybridization using using sequences complementary to the ChAT mRNA (3) colorimetric technique for detection of AChE activity [@karnovsky1964] (4) and reporter gene fused to the ChaT gene regulatory elements outlined the presence of cholinergic pathways in Drosophila [@buchner1986; @gorczyca1987; @barber1989; @yasuyama1999], honeybee [@kreissl1989] and locust *Locusta migratoria* [@lutz1987; @geffard1985]. Based on these data, cholinergic neurons are in almost all regions of the brain, in the peripheral nervous system, viz. visual system and the antenna. They are also present in the thoracic, abdominal and terminal abdominal ganglia involved in the regulation of movement of wings, abdomen and legs, as well as the regulation of the anal and reproductive muscles [@smarandache-wellmann2016]. + +<!-- . In particular, the muchroom bodies associated with learning, formation of memory and the sensory processing [@heisenberg1998], dorsal lobe where mechanosensory and gustatory neurons project into from the anteanna --> + +<!-- In peripheral nervous tissue, cholinergic neurons are the --> +Cholinergic neurons have been also mapped by using radiolabelled ligand, specific for nAChRs. $\alpha$-bungarotoxin ($\alpha$-bgtx), is a 74-amino acid long, 8 kDa proteins isolated from the venom of a snake *Bungarus multicinctus*. It binds with high affinity to nAChR [@lee1967] and blocks synaptic responses evoked by acetylcholine and other agonists [@chang1963] by blocking the access of an agoinist to the nAChR binging site [@mishina1984]. $\alpha$-bgtx staining mapped to brain regions identified by other methods. In the honeybee, it was found in the optic lobes, antennal lobes, ocellar system and muchroom bodies [@scheidler1990]. This correlated with the $\alpha$-bgtx staining distribution in the central nervous system of Drosophila [@schmidt-nielsen1977], moth *Manduca sexta* [@hildebrand1979] and cocroach [@orr1990]. Incubation of $\alpha$-bgtx with the ganglia of the american cocroach [@sattelle1983] and cricket *Acheta domesticus* [@meyer1985] identified further regions with high affinity to this protein. Staining was evident in the abdominal ganglion in the region rich in interneurons which make synaptic connections with the sensory afferent neurons [@daley1988] in the abdominal ganglia of the cocroach and in the thoracic ganglia [@sattelle1981]. Presence of nAChRs at the insect ganglia was confirmed using electrophysiological approaches [@sattelle1981; @bai1992] + +### Role of nAChRs in insects + +Based on the distribution of cholinergic-synapse markers and the quantitative analysis of acetylcholine in the brain [@florey1963], it was concluded that acetylcholine is a major neurotransmitter in the nervous system of insects. In contrast to vertebrates and *C. elegans*, acetylcholine in insects does not mediate signal transduction at the NMJ, insteed it is mainly involved in the sensory pathways and central information processing. The action of acetylcholine is mediated by nAChRs. + +<!-- Lerning: [@kerkut1970] acetylcholinesterase inhibitor facilitated the ability of cocroach to learn to raise its leg out of the solution in response to electrical stimuli. Drugs: neostigmine and physostigmine which inhibit acetylcholinesterase [@carlyle1963]. --> + +The biological role of nAChRs in insects was investigated in response to nAChR agonists. Lethal doses of neonicotinoid imidacloprid induces complex symptoms in American cocroach and in honeybee [@sone1994; @elbart1997; @suchail2001]. The following order of events was noted: hyperexcitation as evident by excessive pacing, collapse and diminishing uncoordinated leg and abdomen movement followed by paralysis and eventual death. Lethal dose of insecticide nicotine [@david1953], a naturally occurring alkaloid found in the *Solanaceae* family of plants, including tobacco [@steppuhn2004] induce similar effects on bees [@mcindoo1943]. Distinct behavioural alterations can be induced by nAChR agonists at sub-lethal doses. +Imidacloprid at < 4 nM inhibits feeding of *Myzus persicae*, which leads to their starvation [@nauen1995; @elbart1997]. In non-target species, such as honeybees and bumblebees neonicotinoids impair on learning and memory, as well as reproduction (Section \@ref(sublethalbees)). + +### Electrohysiological properties of insect nAChRs + +Role of nAChRs in insect cholinergic neurotransmission electrophysiological recordings : electrophysiological recordings from the insect ganglia where sensory neuron makes synpatic connections to an interneuor. Robust preparation, easy to dissect and relatively large. + +extracellular recordings from the cricket terminal abdominal ganglion recording of the interneuron activity nicotine - cholienrgic and evidence of nAChr expression from the biochem studies. In response to Iontophoretic nicotine, increase in the the rate of neuronal firing, blocked by bgtx [@meyer1985] evidence that nachr agonist lead to excitation. + +In cocroach, cell bodies of the dorsal unpaired median (DUM) neurons in the thoracic ganglion depolarised in the presence of nicotine and was blocked by selective antagonist mecamylamine [@bai1992]. + +In the abdominal ganglia of the cocroach [@sattelle1981]. + +Inward, depolarising current in isolated + +Intracellular recordings have shown that these compounds depolarise and excite the post synaptic neuron of the terminal abdominal ganglia [@kerkut1969]. However, high concentrations 1 mM - 10 mM were needed, potentially due to the high concentration of acetylcholinesterase which rapidly breaks down ACh. + +In cultured cells from honeybee antenal lobe whole patch clamp technique: nicotine depolarising inward current inhibited by bgtx [@barbara2005] cultured cells of mushroom bodies of the honey bee [@goldberg1999; @palmer2013] also inhibited by bgtx. Also cultured CNS neurons of Drosophila [@brown2006]. + +DESENSITISATION + +Exposure to high concentrations of agonist had a secondary effects : in the presence of agonist, the depolarising current slowly decreases until it is abolished due to desensitisation [@goldberg1999]. The time constant for desensitisation varied beteween compounds 390 and 420 ms for nicotine [@goldberg1999] up to 23 s in the cocroach neurons [@salgado2004] + +Desensitisation is a period after agonist removal, whereby subsequent depolarisation cannot be elicited by agonist [@goldberg1999]. Recovery is reverseble from desenstisiation is dependes on the compounds -, neuronal preparation and concentration. In cultured cells of the honey bee lasts up to 3 minutes after application of Ach/nicotine [@goldberg1999]. in the isolated thoracic neurons up to 30 s [@salgado2004]. Althout recovery is typically reversable, this does not always happen Full recovery may not occur or may be slower if the receptor are exposed to the large doses of agonist for a prolonged time [@katz1957]. + +isolated thoracic ganglia of the americal cocroach - desensitising in under a second in the presence of ACh and nicotine + +CONDUCTANCE +cultured muschroom bodies of the honey bee. Cationic conductance, mainly sodium and potassium but also calcium [@goldberg1999]. + +cocroach terminal abdominal ganglion extracellular post synaptic potentials in response to acetylcholine. In the presence of acetylcholinenesterase inhibitor acetylcholine at much lower doses 1 uM - 1 mM elicited Rapid and concentration dependent depolarisation excitation of the post-synapse and the gradual decline of the EPSP leading to their block [@callec1973; @sattelle1976]. + +SINGLE CHANNEL RECORDING + +Complex channel kinetics resembling those found in veretbrates [@colquhoun1985; @nagata1996; @nagata1998]. + + +from cholinergic neurons of the larva Drosphila CNS [@albert1993; @brown2006], Musca domestica cultured CNS neurons [@albert1993] + + +Single channel recordings + +In response to acetylcholine the channel switches between active and inactive form, with the active form interrupted by the short-lived channel closing bursts. Temporal characterisation of these events revelaved that the frequency of channel opening and the duration of opening differs depending on the agonist applied and the neuronal preparation. However, typically receptor remains opened for ~ 1.5 ms; this is interrupted by channel closing bursts of ~ 20 $\mu$s which occur at a frequency of 1-2 closures/opening burst [@albert1993]. + +Channel opening is not an all or nothing event. Instead, a channel typically exhibits two conductance states, one on which it is fully opened, named a full conductance state (i.e. the active form), and one in which the channel is partially opened, named the sub-conductance state. Although the conductance rate between channels from various preparations is similar, the ratio between the two as well as their fine structure varies depending on the concentration, the agonist used and and neuronal preparation. + +<!-- Immunocytochemistry using monoclonal antibodies specifie --> +<!-- In the brain, cholinergic neurons can be found in almost all parts of the brain and the optical lobe. In particular, mushroom bodies, --> + +<!-- thoracic ganglia : afferent sensory neurons --> + +<!-- In the peripheral primary sensory nerouns of the compound eye and the anntena. --> + +<!-- Afferent sensory neurons --> + + +<!-- interneurones of the thoracic ganglia --> + -Large quantities of achetylcholine isolated from the insect brain [@florey1963]. Further biochemical studies in which various molecules of the cholinergic synapse have been identified brain regions with the cholinergic input. -Choline acetyltransferase biosynthesis of acetylcholine, and it is thought to be a marker of cholinergic neurons. -immonocytochemistry: binding of choline acetyltransferase (ChAT) monoclonal antibodies : +<!-- Cholinergic neurons in the cortical regions of almost all regions of the insect brain --> -in the brain of locust *Locusta migratoria* [@geffard1985]. +<!-- Immunocytochemistry --> -also "immunoreactivity first, in -regions of neuropile previously shown by backfilling -with cobalt to contain terminals from sensory neurones. Some roots of peripheral nerves also bind the antibody. Secondly, a small number of neurone cell bodies in the brain and thoracic ganglia are immunoreactive and we assume these belong to interneurones" and " first, there are relatively few immunoreactive cell bodies in the CNS; and second, sensory neuropiles, such as the -ventral association centre and the ventral VAC (vVAC), the anterior ring tract, the tritocerebrum and the antennal lobe, are immunoreactive. That ChAT is contained in sensory neurones is suggested by immunoreactivity found in peripheral neurone cell bodies" [@lutz1987]. +<!-- Biochemical techniques using monoclonal antibodies specific agains --> -immunoreactivity in almost all brain regions of *D. melanogaster* " apart from -the lobes and the peduncle of the mushroom body and -most of the first visual neuropile (lamina)" [@buchner1986]. +<!-- Large quantities of achetylcholine isolated from the insect brain preparations --> -in-situ hybridization: [@barber1989] "Substantial amounts of cRNA probe for ChAT mRNA -were observed associated with cells of all cortical regions of -the optic lobe and brain. Neuropil regions of the -brain displayed insignificant amounts of hybridization with -the experimental probe and specimens incubated with the control probe did not exhibit significant -hybridization in either cortical or neuropil areas . -In peripheral nervous tissue, there was substantial labeling over primary sensory neurons in the antenna, and significant amounts of probe were associated with the -retinular cell layer of the compound eye ". the compound eye is the visual system of the fly. +<!-- also "immunoreactivity first, in --> +<!-- regions of neuropile previously shown by backfilling --> +<!-- with cobalt to contain terminals from sensory neurones. Some roots of peripheral nerves also bind the antibody. Secondly, a small number of neurone cell bodies in the brain and thoracic ganglia are immunoreactive and we assume these belong to interneurones" and " first, there are relatively few immunoreactive cell bodies in the CNS; and second, sensory neuropiles, such as the --> +<!-- ventral association centre and the ventral VAC (vVAC), the anterior ring tract, the tritocerebrum and the antennal lobe, are immunoreactive. That ChAT is contained in sensory neurones is suggested by immunoreactivity found in peripheral neurone cell bodies" [@lutz1987]. --> -AND " histochemical detection of reporter gene expression " using x-gal : [@yasuyama1999]. +<!-- immunoreactivity in almost all brain regions of *D. melanogaster* " apart from --> +<!-- the lobes and the peduncle of the mushroom body and --> +<!-- most of the first visual neuropile (lamina)" [@buchner1986]. --> +<!-- in-situ hybridization: [@barber1989] "Substantial amounts of cRNA probe for ChAT mRNA --> +<!-- were observed associated with cells of all cortical regions of --> +<!-- the optic lobe and brain. Neuropil regions of the --> +<!-- brain displayed insignificant amounts of hybridization with --> +<!-- the experimental probe and specimens incubated with the control probe did not exhibit significant --> +<!-- hybridization in either cortical or neuropil areas . --> +<!-- In peripheral nervous tissue, there was substantial labeling over primary sensory neurons in the antenna, and significant amounts of probe were associated with the --> +<!-- retinular cell layer of the compound eye ". the compound eye is the visual system of the fly. --> +<!-- AND " histochemical detection of reporter gene expression " using x-gal : [@yasuyama1999]. --> -" cholinergic primary sensory neurons in the Drosophila antennal system" -aceti-cholinesterase : colorimetric determination of acetylcholinesterase activity with -Histochemistry of AChE with colorimetric assay using isothiocholine: -"the optic lobes, fibers connecting the two brain hemispheres, and fiber tracts -as well as soma clusters within the protocerebrum. The calycal input regions of -the mushroom bodies were labelled, whereas the intrinsic Kenyon cells -showed no staining. Although the antennal afferents projecting into the dorsal -lobe showed strong AChE activity, projections into the antennal lobe showed -rather weak staining." [@kreissl1989] the same paper shows a-bungarotoxin (a-BTX) binding sites and AChR monoclonal antibodies with a good overlap in "d immunoreactivity -in neuropiles, tracts, somata, and the antennal nerve. The immunoreactivity -of the optic lobes coincided with the banding pattern of the AChE staining. A -particularly striking overlap of AChR immunoreactivity and AChE staining -was found in the lip neuropile of the mushroom bodies" all in the honeybee +<!-- " cholinergic primary sensory neurons in the Drosophila antennal system" --> +<!-- aceti-cholinesterase : colorimetric determination of acetylcholinesterase activity with --> +<!-- Histochemistry of AChE with colorimetric assay using isothiocholine: --> +<!-- "the optic lobes, fibers connecting the two brain hemispheres, and fiber tracts --> +<!-- as well as soma clusters within the protocerebrum. The calycal input regions of --> +<!-- the mushroom bodies were labelled, whereas the intrinsic Kenyon cells --> +<!-- showed no staining. Although the antennal afferents projecting into the dorsal --> +<!-- lobe showed strong AChE activity, projections into the antennal lobe showed --> +<!-- rather weak staining." [@kreissl1989] the same paper shows a-bungarotoxin (a-BTX) binding sites and AChR monoclonal antibodies with a good overlap in "d immunoreactivity --> +<!-- in neuropiles, tracts, somata, and the antennal nerve. The immunoreactivity --> +<!-- of the optic lobes coincided with the banding pattern of the AChE staining. A --> +<!-- particularly striking overlap of AChR immunoreactivity and AChE staining --> +<!-- was found in the lip neuropile of the mushroom bodies" all in the honeybee --> -check this paper to see evidence for cholinergic neurons "between the -sensory neurons and interneurons of the cockroach cercal sensory system " paper: " The pharmacology of an insect ganglion: actions of carbamylcholine and acetylcholine" -Its action is mediated predominately by nAChRs, which are the main cholinergic receptor type in their central nervous system [@breer1987]. The presence of nAChR in various brain regions has been detected using biochemical and electrophysiological techniques on neuronal preparations extracted from the Fruit fly *Drosophila melanogaster*, honey bee *Apis mellifera* and American cocroach *Periplaneia americana*. nAChRs have been found to be expressed in the regions associated with learning, formation of memory and the sensory processing [@heisenberg1998], namely the muschroom bodies [@kreissl1989; @gu2006; @oleskevich1999]. They are also present in the insect ganglia, which connects the brain to the peripheral nervous system. In particular, they were identified in the abdominal, thoracic and the terminal ganglia [@sattelle1981; @bai1992], which are involved in the movement of wings, abdomen and legs, as well as the regulation of the anal and reproductive muscles [@smarandache-wellmann2016]. In contrast to mammals and invertebrates (Table \@ref(tab:chlinergic-nts)), insects do not express nAChRs at the neuromuscular junction. +<!-- check this paper to see evidence for cholinergic neurons "between the --> +<!-- sensory neurons and interneurons of the cockroach cercal sensory system " paper: " The pharmacology of an insect ganglion: actions of carbamylcholine and acetylcholine" --> -### Biological role of nAChRs in insects -Insect nAChRs are widely expressed in the insect nervous system, where they mediate fast synaptic transmission. Their involvement in the regulation of diverse biological processes is evident from toxicity studies during which insects were exposed to nAChR agonists. +<!-- Its action is mediated predominately by nAChRs, which are the main cholinergic receptor type in their central nervous system [@breer1987]. --> -Nicotine is a naturally occurring alkaloid found in the *Solanaceae* family of plants, including tobacco [@steppuhn2004]. It is effective against plant insect pests [@david1953], and used in organic farming in form of tobacco tea [@isman2006]. Exposure of insects to lethal dose of nicotine results in symptoms characteristic for the nervous system intoxication [@chadwick1947] and include increased locomotory activity, followed by convulsions, twitching and eventual death [@carlile2006]. +<!-- The presence of nAChR in various brain regions has been detected using biochemical and electrophysiological techniques on neuronal preparations extracted from the Fruit fly *Drosophila melanogaster*, honey bee *Apis mellifera* and . --> + + +<!-- nAChRs have been found to be expressed in the regions --> + +<!-- , namely the muschroom bodies [@kreissl1989; @gu2006; @oleskevich1999]. --> + + + +<!-- In contrast to mammals and invertebrates (Table \@ref(tab:chlinergic-nts)), insects do not express nAChRs at the neuromuscular junction. --> + +<!-- ##### Electrophysiology --> +<!-- Evidence from the application of nAChR: --> + +<!-- nicotine: --> +### Kinetic properties of nAChRs + +Nicotinic acetylcholine receptors have three basic conformation states: the closed, the open and the disensitised state [@katz1957; @monod1965]. The question is: how does agonist binding lead to these conformational changes? Diffuculties in crystallising muscle nAChR restricted studies of receptor structure in multiple states. Whereas AChBP lack transmembrane domains therefore is not suitable for such studies. +Evidence comes from a crystal structure of structuraly related, bacterial pentameric ligand gated ion channels. These channels are not members of the cys-loop family because they lack N-termial disulphide bond. They also do not contain a large cytoplasmic loop between M3-M4 TM helices. They do however share common topology of 5 subunits, each comprising of 4 TM helices. The comparison of the crystal structure of *Erwinia* LGIC (ELGIC) and *Gloebacter* LGIC (GLGIC). They are both cation selective. GLIC is gated by protons, whereas ELIC by amines [@] +ELIC with no agonist bound - hence closed confirmation [@] +Aromatic residues in C loop form a cap above the bound agonist and by doing so they decrease the on/off rates of receptor binding [@hilf2008] this was compared to the crystal structure of the agonist-bound GLIC [@hilf2009]. + +Ligand binding leads to movement of the C-loop amino acids which fold over the agonist binding site, burrying it inside the protein and reducing the dissociation on/off rates of the bound agonist. + +Also loop A moves towards the loop B. In complementary subunit loop F moves in, towards the agonist. This propagates further structural changes. The beta sheets rearrange. Inner beta sheet remains in the exact position, but the inner one rotates towards the centre of the pentamer. +These structural changes propagate to the level of the channel, leading to its opening. + +2 possible ways in which channel opens: + +Hirozontal movement of pore lining helices. +Based on the Cryo EM of the mammalian muscle nAChR in closed and open state, a hypothesis of the dynamics has been derived [@unwin1995], binding of agonist leads to rotation of 5 M2 helices. Proposed that as they move, the distance between them increases, and so the ion conductivity pathway becomes wide for the ion passage. Additionaly, this results in movement of hydrophobic residues which proclude the channel entry in the closed state of the receptor. More recently, it has been proposed that the M2 helices do not move in the unified way. Some rotate, whereas others tilt or bend [@unwin2012]. + +@hilf2009 - ELIC in closed state and compared to the open state - bending of felices. + +More reccently, structures of representatives of Cys-loop receptors, glutamate gated chloride channel [@althoff2014] and glycine receptors [@du2015]. + +DESENSITISATION state is a state in which agonist affinity in higher in comparison to the resting or activated state. but ion conductance probability if lower in comparison to the resting state [@monod1965]. State in which agonist binds but there is no ion conductance [@monod1965]. Crystal structure of the human $\alpha4$/$\beta2$ receptor in desensitised state [@morales-perez2016] comparison to the structures of glycine receptors [@du2015] and GluCl channel [@althoff2014], gabaA [@miller2014] in the open state revealed difference at the interface of ECD-TM and extracellular domain loop C rotation regions of the protein and the extracellular domain which leads to occlusion of the ion channel and stabilising of the receptor in desensitising state, thereby contributing to the high affinity of the agonist to the desensitised receptor. ### Neonicotinoids target nAChRs ### {#neonicstarget} -#### Electrophysiological evidence ####{#electrophysevidence} +#### Mutations in nAChRs give rise to neonicotinoid-resistance ####{#resgenevidence} + +Resistance to neonicotinoids arises from mutations in nAChR subunits. Field isolates of peach aphid *Myzus persicae* [@bass2011], the cotton aphid *Aphis gossypii* [@hirata2015; @hirata2017] and the Colorado potato beetle *Leptinotarsa decemlineata* [@szendrei2012], as well as lab-isolates of brown planthopper, *Nilaparvata lugens* [@liu2005], fruit fly *Drosophila melanogaster* [@perry2008] with decreased sensitivity to neonicotinoids have been identified. Behavioral analysis shows that their sensitivity is up to 1500-fold lower in comparison to the reference strains, as shown by the shift in LD50. Analysis of the coding genome of the resistant strains identified mutations in nAChR subunit coding sequence [@bass2011; @perry2008; @hirata2015]. + +#### Neonicotinoids evoke nAChR-like current in insect neuronal preparations ####{#electrophysevidence} The effects of neonicotinoids on the neuronal transmission was investigated on insect neuronal preparations which express high levels of nAChRs. -@sone1994 investigated the effects of imidacloprid on the neuronal activity at the thoracic ganglia of male adult American cockroaches, *Periplaneta americana* using extracurricular recordings. This method allows for a record of changes in spontaneous neuronal activity in response to mechanical or pharmacological interventions. At a very low concentration of 1 nM, imidacloprid induced a sustained for over 2 minutes increase in the rate of neuronal firing. At concentrations ranging from 10 nM to 100 $\mu$M, the following sequence of events was noted: an increase of the rate of spontaneous action potentials of neurons followed by a gradual decline, leading to a complete block of neuronal activity [@sone1994]. Imidacloprid had the same effect on various insect preparations including thoracic ganglion of the Leptinotarsa decemlineata [@tan2008] and on the abdominal ganglion of *Periplaneta americana* [@buckingham1997]. The same observations were made for other neonicotinoids [@thany2009; @schroeder1984]. This provided evidence that neonicotinoids stimulate the nervous system of insects. This conclusion was supported by the behavioural observation, whereby the neonicotinoid intoxication mirrors intoxication seen with cholinergic agents (Section . In response to imidacloprid, insects become hyper excited as evident by excessive pacing. They then collapse and exhibit diminishing uncoordinated leg and abdomen movement until eventual death [@sone1994; @elbart1997; @suchail2001]. Sub-lethal doses (i.e. < 4 nM) have distinct effect, such as an inhibition of feeding leading to starvation [@nauen1995; @elbart1997]. +@sone1994 investigated the effects of imidacloprid on the neuronal activity at the thoracic ganglia of male adult American cockroaches, *Periplaneta americana* using extracurricular recordings. This method allows for a record of changes in spontaneous neuronal activity in response to mechanical or pharmacological interventions. At a very low concentration of 1 nM, imidacloprid induced a sustained for over 2 minutes increase in the rate of neuronal firing. At concentrations ranging from 10 nM to 100 $\mu$M, the following sequence of events was noted: an increase of the rate of spontaneous action potentials of neurons followed by a gradual decline, leading to a complete block of neuronal activity [@sone1994]. Imidacloprid had the same effect on various insect preparations including thoracic ganglion of the Leptinotarsa decemlineata [@tan2008] and on the abdominal ganglion of *Periplaneta americana* [@buckingham1997]. The same observations were made for other neonicotinoids [@thany2009; @schroeder1984]. This provided evidence that neonicotinoids stimulate the nervous system of insects. -@sattelle1989 used isolated cocroach neuronal preparation to record post-synaptic intracellular currents in response to neonicotinoid prototype 2(nitromethylene) tetrahydro-1, 3-thiazine (NMTHT). NMTHT depolarised the post-synaptic unpaired median neurons and the cell body of motor neurons of the abdominal ganglion. Agriculturally relevant neonicotinoids had the same effect on the post-synaptic membrane of the isolated cocroach thoracic ganglia [@tan2007; @thany2009] potato beetle isolated neurons [@tan2008], and on cultured cocroach [@ihara2006], honeybee [@palmer2013] and fruit fly [@brown2006] neurons. These data provide evidence that neonicotinoids act directly on the post-synaptic neuron in both target and non-target insects. + <!-- This phenomenon is due to the distinct conformation of nAChRs, at in which they are not capable of ion conduction [@nemecz2016]. --> + +<!-- In the continual presence of agonist, the membrane potential gradually repolarises until it reaches the resting state, hovewer the next depolarisation will not occur, until the agonist are washed off and the receptor recovers from desensitisation [@katz1957]. --> + +@sattelle1989 used isolated cocroach neuronal preparation to record post-synaptic intracellular currents in response to neonicotinoid prototype 2(nitromethylene) tetrahydro-1, 3-thiazine (NMTHT). NMTHT depolarised the post-synaptic unpaired median neurons and the cell body of motor neurons of the abdominal ganglion. Agriculturally relevant neonicotinoids had the same effect on the post-synaptic membrane of the isolated cocroach thoracic ganglia [@tan2007; @thany2009] potato beetle isolated neurons [@tan2008], and on cultured cocroach [@ihara2006], honeybee [@palmer2013] and fruit fly [@brown2006] neurons. Pharmacological characterisation of neonicotinoids-induced currents provided further evidence for their mode of action. The inward current elicited by neonicotinoids were dose-dependent, whereby the higher the concentration, the grater the depolarisation. EC50 values (concentrations at which the half of the maximum current was observed) are in the region of 1 - 5 $\mu$M [@thany2009; @tan2007]. Such low values indicate highly potent action of neonicotinoids on insects, in agreement with toxicological data (Section \@ref(potentpests)). Neonicotinoid-induced currents were reminiscent of those induced by acetylcholine and nicotine, and were prevented by the application of nAChRs antagonists ($\alpha$-bungarotoxin, methyllycaconitine, mecamylamine or d-tubocurarine) not by muscarinic receptor antagonists (atropine, pirenzepine), suggesting neonicotinoid-induced currents are due to the activation of nicotinic receptors. -#### Biochemical evidence +### Mode of action of neonicotinoids ###{#moaneonicsinsects} + +Neonicotinoids can have diverse mode of action. The currents produced by neonicotinoids and ACh on cultured or isolated insect neuronal preparation were compared. Neonicotinoids evoking current lower than that evoked by ACh were classed as partial agonists, those eliciting similar response were classed as true agonists, whereas those more efficacious than ACh, super-agonists. Thiacloprid and imidacloprid are partial agonists, nitenpyram, clothianidin, acetamiprid and dinotefuran are true agonists, whereas thiamethoxam has no effect on the isolated American cockroach thoracic ganglion neurons [@tan2007]. This differs from the mode of action of neonicotinoids on cultured terminal abdominal ganglion neurons of this insect. Currents produced by all neonicotinoids tested was lower than that evoked by ACh [@ihara2006], suggesting they are all partial agonists on these cells. The mode of action of neonicotinoids on the fruit fly [@brown2006] and honey bee neurons [@palmer2013] differs still, implying the presence of distinct nAChRs in different insect species and neuronal preparations. -@tomizawa1996 developed neonicotinoid agarose affinity column to isolate proteins with high binding affinity to neonicotinoids. Using Drosophila and Musca head membrane preparations, he identified three nAChR subunits as potential neonicotinoid-targets. -##### Ligand binding studies #####{#ligbinding} +#### Neonicotinoids bind with high affinity to insect nAChRs ####{#ligbinding} + +<!-- @tomizawa1996 developed neonicotinoid agarose affinity column to isolate proteins with high binding affinity to neonicotinoids. Using Drosophila and Musca head membrane preparations, he identified three nAChR subunits as potential neonicotinoid-targets. --> The binding affinity of imidacloprid to nAChRs expressed in insect membrane homogenates was assessed in the saturation ligand binding studies. -In the saturation binding experiment, various concentration of the labelled ligand is added to the preparation and the concentration of the ligand at the equilibrium is determined. This is then used to derive the binding constant (as a measure of dissociation constant, Kd). Here, it was used to define the binding strength of neonicoinoids to insect nAChRs (Table \@ref(tab:bindignrecombinant)). +<!-- In the saturation binding experiment, various concentration of the labelled ligand is added to the preparation and the concentration of the ligand at the equilibrium is determined. This is then used to derive the binding constant (as a measure of dissociation constant, Kd). Here, it was used to define the binding strength of neonicoinoids to insect nAChRs (Table \@ref(tab:bindignrecombinant)). --> Imidacloprid and thiamethoxam bind with high affinity to proteins in the whole membrane preparations of the domestic fly and aphids with the Kd in the low nM range [@liu1993; @wellmann2004; @liu2005]. Interestingly, two binding affinities have been derived from the imidacloprid study in the brown planthopper and pea aphid [@wellmann2004; @taillebois2014] suggesting there are two binding sites in these animals. @@ -441,17 +575,78 @@ library(kableExtra) threeparttable = T) ``` -In addition to the saturation studies, the competitive ligand binding studies were carried out. In the the competitive ligand binding studies, biological preparation is incubated with radiolabelled ligand. The ability of various concentrations of unlabeled ligand is measured to define its equilibrium inhibition constant (Ki). This method informs both on the affinity and on the interactions between ligands. +In addition to the saturation studies, the competitive ligand binding studies were carried out. + +<!-- In the the competitive ligand binding studies, biological preparation is incubated with radiolabelled ligand. The ability of various concentrations of unlabeled ligand is measured to define its equilibrium inhibition constant (Ki). This method informs both on the affinity and on the interactions between ligands. --> Various concentrations of neonicotinoid prototype isothiaocynate were incubated with the homogenate of fruit fly *Drosophila melanogaster* and a homogenate of the abdominal nerve cords of *Periplaneta americana* before the exposure to radiolabelled nAChR antagonist $\alpha$-bgtx [@gepner1978]. Isothiaocynate inhibited binding of $\alpha$-bgtx in the concentration dependent manner [@gepner1978], suggesting the two compounds share the binding site. Similarly, imidacloprid has been shown to displace $\alpha$-bgtx from brain membrane preparations from honey bee *Apis mellifera* [@tomizawa1992; @tomizawa1993], *Drosophila melanogaster* [@zhang2004], house fly *Musca domestica* and isolated cockroach nerve cords [@bai1991]. -#### Genetic evidence ####{#resgenevidence} +#### High affinity of neonicotinoids to heterologously expressed insect-chimera receptors ####{#chimerareceptors} -Resistance to neonicotinoids arises from mutations in nAChR subunits. Field isolates of peach aphid *Myzus persicae* [@bass2011], the cotton aphid *Aphis gossypii* [@hirata2015; @hirata2017] and the Colorado potato beetle *Leptinotarsa decemlineata* [@szendrei2012], as well as lab-isolates of brown planthopper, *Nilaparvata lugens* [@liu2005], fruit fly *Drosophila melanogaster* [@perry2008] with decreased sensitivity to neonicotinoids have been identified. Behavioral analysis shows that their sensitivity is up to 1500-fold lower in comparison to the reference strains, as shown by the shift in LD50. Analysis of the coding genome of the resistant strains identified mutations in nAChR subunit coding sequence [@bass2011; @perry2008; @hirata2015]. - -### Mode of action of neonicotinoids ###{#moaneonicsinsects} +Due to the difficulties in the expression of native insect receptors (Section \@ref(expressionfail)), the binding affinity of neonicotinoids was determined in hybrid receptors, consisting of insect $\alpha$-subunit and vertebrate $\beta$ subunit. $\beta2$ from rat and chicken has been shown to enable recombinant expression of several insect $\alpha$ subunits in cell lines. -Neonicotinoids can have diverse mode of action. The currents produced by neonicotinoids and ACh on cultured or isolated insect neuronal preparation were compared. Neonicotinoids evoking current lower than that evoked by ACh were classed as partial agonists, those eliciting similar response were classed as true agonists, whereas those more efficacious than ACh, super-agonists. Thiacloprid and imidacloprid are partial agonists, nitenpyram, clothianidin, acetamiprid and dinotefuran are true agonists, whereas thiamethoxam has no effect on the isolated American cockroach thoracic ganglion neurons [@tan2007]. This differs from the mode of action of neonicotinoids on cultured terminal abdominal ganglion neurons of this insect. Currents produced by all neonicotinoids tested was lower than that evoked by ACh [@ihara2006], suggesting they are all partial agonists on these cells. The mode of action of neonicotinoids on the fruit fly [@brown2006] and honey bee neurons [@palmer2013] differs still, implying the presence of distinct nAChRs in different insect species and neuronal preparations. +Mammalian $\alpha4$/$\beta2$ receptor expresses well in Xenopus oocytes [@cooper1991] and cell lines [@lansdell2000] has low affinity to imidacloprid (Kd >1000 $\mu$M) [@lansdell2000]. Chimera of rat $\beta2$ and $\alpha$ subunits from the fruit fly *Drosophila melanogaster* [@lansdell2000], aphid *Myzus Persicae* [@huang1999], planthopper *Nilaparvata lugens* [@liu2009], cat flea *Ctenocephalides felis* [@bass2006] and sheep blowfly *Lucilia cuprina* [@dederer2011] have been generated. It needs to be noted that the potency of neonicotinoids on these receptors is unknown due to the lack of reported data, suggesting these receptors are not functional. However, their pharmacological profiles have been determined using saturation ligand binding studies [@hulme2010] (Table \@ref(tab:bindignrecombinant)). + +The affinity of neonicotinoids to insect-chimera rectors varies, depending on the identity of the $\alpha$ subunit. Imidacloprid did not bind to Mp$\alpha1$/rat$\beta2$ receptor, whereas its Ki at Mp$\alpha2$ and Mp$\alpha3$-containing receptor was 3 and 2.8 nM, respectively [@huang1999]. Four to five fold-difference between the most and least susceptible *Drosophila melanogaster* and *Ctenocephalides felis* receptor assemblies were also identified [@lansdell2000; @bass2006] + +Imidacloprid exhibits the highest affinity against target pest *Myzus Persicae* with the lowest reported Ki of 2.8 nM on $\alpha3$/$\beta2$ receptor [@huang1999]. It binds less tightly to the non-target insect, the fruit fly nAChRs; the Kd values range from 8.4 to 34.9 nM [@lansdell2000]. + +```{r bindignrecombinant, echo=FALSE, warning = FALSE, message=FALSE} +library(kableExtra) + library(dplyr) + +footnotez <- ("Receptors were expressed in insect S2 cell line") +footnotey <- ("Rn = Rattus norvegicus (rat), Dm = *Drosophila melanogaster (fruit fly), Mp = Myzus persicae (aphid), Nl = Nilaparvata lugens (planthopper), Cf = Ctenocephalides felis (cat flea)), N/B = no binding,") + + bindingrecombinant <- data.frame( + Receptor = c("Rn$\\alpha4\\beta2$", "Dm$\\alpha1$/Rn$\\beta2$", "Dm$\\alpha2$/Rn$\\beta2$", "Dm$\\alpha3$/Rn$\\beta2$", "Mp$\\alpha1$/Rn$\\beta2$", "Mp$\\alpha2$/Rn$\\beta2$", "Mp$\\alpha3$/Rn$\\beta2$", "Mp$\\alpha4$/Rn$\\beta2$", "Nl$\\alpha1$/Rn$\\beta2$", "Cf$\\alpha1$/Dm$\\alpha2$/Rn$\\beta2$", "Cf$\\alpha3$/Dm$\\alpha2$/Rn$\\beta2$"), + Kd= c(">1000", "34.9", "20", "8.4", "N/B", "3", "2.8", "N/B", "24.3", "141", "28.7"), + References = c("Lansdell and Millar, 2000", "", "", "", "Huang et al., 1999", "", "", "", "Liu et al., 2005", "Bass et al. 2006", "")) + + bindingrecombinant %>% + mutate_all(linebreak) %>% + kable("latex", align = "c", booktabs = TRUE, escape = F, + col.names = linebreak(c("Receptor", "Kd\n(nM)", "Rerefence")), + caption = 'Binding affinity of imidacloprid to recombinant insect-hybrid receptors') %>% + kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") %>% + add_footnote(notation = "none", c(footnotez, footnotey), + threeparttable = T) +``` + +#### High potency of neonicotinoids on heterologously expressed insect-mammalian hybrid receptors + +The potency of neonicotinoids on insect-mammal hybrid nAChRs have been determined using electrophysiological techniques. Due to the difficulties in heterologous expression of native insect receptors (Section \@ref), $\alpha$ nAChR subunit from the fruit fly, the cat flea and the planthopper were co-expressed with rat or mouse $\beta2$. The responses of the formed channel were recorded in the presence of various neonicotinoids: cyanoamidines clothianidin and imidacloprid, nitroguanidines thiacloprid and acetamiprid and nitromethylene nitenpyram. + +Depolarising current was recorded from cells expressing insect-hybrid nAchRs in responses to all tested neonicotinoids. This response was dose-dependent. The potency of neonicotinoids varied, as indicated by the EC50 value, between 0.04 and 45.8 $\mu$M, however it is generally in the region of 1 $\mu$M. + +The rank order of potency of cyanoamidines, nitroguanidine and nitromethylene differs, depending on the receptor identity. For example, in imidacloprid and clothianidin are the most potent on the fruit fly $\alpha1$ containing receptors [@dederer2011], whereas planthopper $\alpha3\alpha8$ hybrid, thiacloprid is the most efficacious [@yixi2009]. Nitenpyram has consistently the highest EC50. + +```{r potencyrecombinant, echo=FALSE, warning = FALSE, message=FALSE} +library(kableExtra) + library(dplyr) + +footnotew <- ("Receptors were expressed in Xenopus oocytes") +footnotex <- ("Rn = Rattus norvegicus (rat), Gg = Gallus gallus (chicken), Dm = *Drosophila melanogaster (fruit fly), Nl = Nilaparvata lugens (planthopper), Cf = Ctenocephalides felis (cat flea)), Lc = Lucilia cuprina (sheep blowfly)") + + potencyrecombinant <- data.frame( + Receptor = c("Nl$\\alpha1$/Rn$\\beta2$", "Nl$\\alpha2$/Rn$\\beta2$", "Nl$\\alpha3$/Rn$\\beta2$", "Nl$\\alpha3\\alpha8$/Rn$\\beta2$", "", "", "", "Dm$\\alpha1$/Gg$\\beta2$", "", "", "", "Dm$\\alpha2$/Gg$\\beta2$", "", "", "", "Cf$\\alpha1$/Gg$\\beta2$", "", "", "", "Cf$\\alpha2$/Gg$\\beta2$", "", "", "", "Cf$\\alpha4$/Gg$\\beta2$", "", "", ""), + Compound = c("Imidacloprid", "Imidacloprid", "Imidaclorprid", "Imidacloprid", "Clothianidin", "Thiacloprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram"), + EC50 = c("61", "870", "350", "3.2", "5.1", "2.8", "5.6", "0.04", "0.34", "0.23", "0.4", "0.84", "5.4", "2", "35.4", "0.02", "0.15", "0.11", "0.63", "1.31", "1.65", "2.63", "24.4", "13.8", "21.3", "9.4", "45.8"), + References = c("Liu et al. 2009", "", "", "Yixi et al. 2009", "", "", "", "Dederer et al. 2011", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "")) + + potencyrecombinant %>% + mutate_all(linebreak) %>% + kable("latex", align = "c", booktabs = TRUE, escape = F, + col.names = linebreak(c("Receptor", "Compound", "EC50\n($\\mu$M)", "Rerefence")), + caption = 'The potency of neonicotinoids on recombinantly expressed insect hybrid nAChRs.') %>% + kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") %>% + add_footnote(notation = "none", c(footnotew, footnotex), + threeparttable = T) +``` + +<!-- Based on the expression of several potential assemblies have been identified. --> + +<!-- Subunits with various degree of sensitivity to neonicotinoids, suggesting some and not all receptors confer neonicotinoid sensitivity. --> <!-- cultured Drosophila CNS cholinergic neurons, whereas imidacloprid is a partial agonist there . --> @@ -504,100 +699,31 @@ library(kableExtra) nAChR are assemblies of 5 different or identical receptor subunits (Section \@ref(structure)). Each subunit is encoded by a separate gene and is classified as either $\alpha$ or non-$\alpha$, depending on the primary amino acid sequence, whereby $\alpha$ subunits contain a disulphide bond formed between the adjacent cysteines in the ligand binding domain (Figure \@ref(fig:structure-nachr-label)). Genome sequencing projects enabled identification of nAChR subunit families in several insect species. Fruit fly and model organism *Drosophila melanogaster* has 10 subunits, 7 of which are $\alpha$ ($\alpha1-7$) and 3 are $\beta$ ($\beta1-3$) [@adams2000a; @sattelle2005]. There are 11 subunits in the beneficial insect honeybee *A. mellifera* ($\alpha1-9$, $\beta1-2$) [@jones2006a; @consortium2006], 12 subunits in the pest red flour beetle *Tribolium castaneum* ($\alpha1-11$,, $\beta1$) [@consortium2008] and 7 in the Pea Aphid, *Acyrthosiphon pisum* ($\alpha1-6$, $\beta1-2$) [@yi-peng2013; @Consortium2010]. With the aid of molecular cloning techniques, equivalent subunits have been identified in many other insects, including cat flea *Ctenocephalides felis* [@bass2006] and green peach aphid *Myzus persicae* [@huang2000]. Amino acid sequence alignment of equivalent subunits revealed that they are highly conserved, with sequence identity typically greater than 60 % [@jones2010]. -Insect nAChR gene families are among the least diverse when compared to other animal phyla. Mammals express 17 subunits: $\alpha1-10$, $\beta1-4$, $\delta$, $\gamma$ and $\epsilon$ [@millar2009] and there are 29 subunits in the representative of the phylum *Nematoda, C. elegans* [@jones2007b]. +Insect nAChR gene families are among the least diverse when compared to other animal phyla. Mammals express 17 subunits: $\alpha1-10$, $\beta1-4$, $\delta$, $\gamma$ and $\epsilon$ [@millar2009] and there are 29 subunits in the representative of the phylum *Nematoda, C. elegans* [@jones2007a]. -### RIC-3 improves recombinant nAChR assembly ###{#ric3insect} +### Diffuculties in heterologous expression of insect nAChRs <!-- There are different receptor types in insects. --> <!-- https://radar.brookes.ac.uk/radar/file/c59cbdb5-d171-49e0-b0e4-101c261c72ed/1/fulltext.pdf --> -To identify which subunits assemble to form functional receptors, recombinant expression techniques were used. - -Recombinant expression is a technique receptor stoichiometry and function can be studied in a heterologous system. cDNA is injected into the Xenopus oocytes, or used to transfect insect or mammalian cell line. Using internal cellular machinery, it is transcribed, translated and processed to the surface of the cell. Should a protein form, cell-surface expression can be detected using biochemical approaches (such as ligand binding studies), whereas function studied by means of electrical recordings. These approaches were utilised to identify the major receptor assemblies in mammals, nematode and fish (Table \@ref(tab:chlinergic-nts)). +To identify which subunits assemble to form functional receptors, recombinant expression techniques were used. Recombinant expression is a technique receptor stoichiometry and function can be studied in a heterologous system. cDNA is injected into the Xenopus oocytes, or used to transfect insect or mammalian cell line. Using internal cellular machinery, it is transcribed, translated and processed to the surface of the cell. Should a protein form, cell-surface expression can be detected using biochemical approaches (such as ligand binding studies), whereas function studied by means of electrical recordings. These approaches were utilised to identify the major receptor assemblies in mammals, nematode and fish (Table \@ref(tab:chlinergic-nts)). <!-- To determine which insect nAChR subunits come together to form a functional receptor, various nAChR subunits were injected into the expression systems (*Xenopus oocytes* or cell lines) to determine whether cell surface expression and receptor function can be obtained. --> -To determine which insect subunits form functional nAChRs, @lansdell2012 transfected cultured insect cells with over 70 *Drosophila melanogaster* nAChR subunit cDNAs either singularly or in combinations. No cell surface was achieved, as shown by the radiolabelled ligand binding studies. Difficulties in expression of *Drosophila melanogaster* were also encountered in Xenopus oocytes [@lansdell2012] and mammalian cell lines [@lansdell1997]. The attempts to express receptors from other species were also largely unsuccessful. No ligand binding and/or agonist evoked currents were detected from cells transfected with genes encoding for the brown planthopper *Nilaparvata lugens* [@liu2005; @liu2009; @yixi2009], cat flea *Ctenocephalides felis* [@bass2006], aphid *Myzus persicae* nAChR subunits [@huang2000] and brown dog tick *Rhipicephalus sanguineus* [@lees2014]. Homomeric Locust *Schistocerca gregaria* $\alpha1$ [@marshall1990], *Myzus Persicae* $\alpha1$ and *Myzus Persicae* $\alpha2$ [@sgard1998] produced receptors with nAChR-like pharmacological and electrophysiological characteristics, however the channel-generated currents were of low amplitude, and the expression inconsistent. - -Difficulties in recombinant receptor expression highlight the complexity of receptor formation (Figure \@ref(fig:turnover-label)). Assembly and oligomerisation are critical steps in the receptor maturation. These steps require a number of ER and Golgi resident chaperons. RIC-3 (resistant to inhibitors of cholinesterase-3) is an evolutionary conserved, ER-residing [@roncarati2006; @alexander2010] transmembrane protein [@wang2009]. The role of RIC-3 in receptor expression was first described using *C. elegans* and human receptors (Section \@ref(ric-3nacho) and \@ref(ric-3celegans)). More recently, its role in receptor folding and maturation of insect nAChRs has been demonstrated. Co-expression of Dm$\alpha2$-containing and Dm$\alpha5$/$\alpha7$ receptors with RIC-3 improved [@lansdell2008], and in some instances enabled expression in otherwise non-permissible systems [@lansdell2012]. Up to 3.5-fold increase in specific binding of radiolabelled antagonist was noted in insect cells co-transfected with RIC-3, suggesting the presence of greater number of folded receptors on the cell surface [@lansdell2008]. Expressed receptors have been also shown to be functional. In Xenopus oocytes, ionic currents were detected in response to acetylcholine in cells co-expressing RIC-3 [@lansdell2012]. - -RIC-3 enabled identification of potential nAChR in insects: homomeric $\alpha5$ and $\alpha7$ and heteromeric $\alpha5$/$\alpha7$. The identity of other insect receptors is unknown. - -(ref:turnover) **Nicotinic acetylcholine receptor turnover.** Synthesised nAChR subunit peptides undergo folding and oligomerisation in the ER. Correctly folded receptors are transported into the Golgi (1). Misfolded subunits and misassembled receptors are retained in the ER and eventually degraded (2). Receptors transported to the Golgi undergo maturation to be shipped to the plasma membrane (4). Receptors in the plasma membrane are eventually degraded or recycled. Receptors are first packed into the endosome (4) and transported to the lysosome or proteosome for degradation (5) or re-inserted into the plasma membrane (6). - -```{r turnover-label, fig.cap="(ref:turnover)", fig.scap= 'Nicotinic acetylcholine receptor turnover.', fig.align='center', echo=FALSE} - -knitr::include_graphics("fig/general_intro/png/nAChR_turnover.png") -``` - -### Insect sensitivity to neonicotinoids in recombinant systems - -Difficulties in expression of recombinant insect nAChRs (Section \@ref(expressionfail)) hiders their pharmacological analysis and identification of receptors sensitive to neonicotinoids. Insect-mammal hybrid receptors served as a platform to investigate the potency and affinity of neonicotinoids. - -#### High affinity of neonicotinoids to insect-chimera receptors ####{#chimerareceptors} - -Mammalian $\alpha4$/$\beta2$ receptor expresses well in Xenopus oocytes [@cooper1991] and cell lines [@lansdell2000] and it has low affinity to imidacloprid (Kd >1000 $\mu$M) [@lansdell2000]. $\beta2$ from rat and chicken has been shown to enable recombinant expression of several insect $\alpha$ subunits in cell lines. Chimera of rat $\beta2$ and $\alpha$ subunits from the fruit fly *Drosophila melanogaster* [@lansdell2000], aphid *Myzus Persicae* [@huang1999], planthopper *Nilaparvata lugens* [@liu2009], cat flea *Ctenocephalides felis* [@bass2006] and sheep blowfly *Lucilia cuprina* [@dederer2011] have been generated. It needs to be noted that the potency of neonicotinoids on these receptors is unknown due to the lack of reported data, suggesting these receptors are not functional. However, their pharmacological profiles have been determined using saturation ligand binding studies [@hulme2010] (Table \@ref(tab:bindignrecombinant)). - -The affinity of neonicotinoids to insect-chimera rectors varies, depending on the identity of the $\alpha$ subunit. Imidacloprid did not bind to Mp$\alpha1$/rat$\beta2$ receptor, whereas its Ki at Mp$\alpha2$ and Mp$\alpha3$-containing receptor was 3 and 2.8 nM, respectively [@huang1999]. Four to five fold-difference between the most and least susceptible *Drosophila melanogaster* and *Ctenocephalides felis* receptor assemblies were also identified [@lansdell2000; @bass2006] - -Imidacloprid exhibits the highest affinity against target pest *Myzus Persicae* with the lowest reported Ki of 2.8 nM on $\alpha3$/$\beta2$ receptor [@huang1999]. It binds less tightly to the non-target insect, the fruit fly nAChRs; the Kd values range from 8.4 to 34.9 nM [@lansdell2000], suggesting it is selectively toxic to pest insects. - -```{r bindignrecombinant, echo=FALSE, warning = FALSE, message=FALSE} -library(kableExtra) - library(dplyr) - -footnotez <- ("Receptors were expressed in insect S2 cell line") -footnotey <- ("Rn = Rattus norvegicus (rat), Dm = *Drosophila melanogaster (fruit fly), Mp = Myzus persicae (aphid), Nl = Nilaparvata lugens (planthopper), Cf = Ctenocephalides felis (cat flea)), N/B = no binding,") - - bindingrecombinant <- data.frame( - Receptor = c("Rn$\\alpha4\\beta2$", "Dm$\\alpha1$/Rn$\\beta2$", "Dm$\\alpha2$/Rn$\\beta2$", "Dm$\\alpha3$/Rn$\\beta2$", "Mp$\\alpha1$/Rn$\\beta2$", "Mp$\\alpha2$/Rn$\\beta2$", "Mp$\\alpha3$/Rn$\\beta2$", "Mp$\\alpha4$/Rn$\\beta2$", "Nl$\\alpha1$/Rn$\\beta2$", "Cf$\\alpha1$/Dm$\\alpha2$/Rn$\\beta2$", "Cf$\\alpha3$/Dm$\\alpha2$/Rn$\\beta2$"), - Kd= c(">1000", "34.9", "20", "8.4", "N/B", "3", "2.8", "N/B", "24.3", "141", "28.7"), - References = c("Lansdell and Millar, 2000", "", "", "", "Huang et al., 1999", "", "", "", "Liu et al., 2005", "Bass et al. 2006", "")) - - bindingrecombinant %>% - mutate_all(linebreak) %>% - kable("latex", align = "c", booktabs = TRUE, escape = F, - col.names = linebreak(c("Receptor", "Kd\n(nM)", "Rerefence")), - caption = 'Binding affinity of imidacloprid to recombinant insect-hybrid receptors') %>% - kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") %>% - add_footnote(notation = "none", c(footnotez, footnotey), - threeparttable = T) -``` +To determine which insect subunits form functional nAChRs, @lansdell2012 transfected cultured insect cells with over 70 *Drosophila melanogaster* nAChR subunit cDNAs either singularly or in combinations. No cell surface was achieved, as shown by the radiolabelled ligand binding studies. Difficulties in expression of *Drosophila melanogaster* were also encountered in Xenopus oocytes [@lansdell2012] and mammalian cell lines [@lansdell1997]. The attempts to express receptors from other species were also largely unsuccessful. No ligand binding and/or agonist evoked currents were detected from cells transfected with genes encoding for the nAChR subunits of brown planthopper *Nilaparvata lugens* [@liu2005; @liu2009; @yixi2009], cat flea *Ctenocephalides felis* [@bass2006], aphid *Myzus persicae* [@huang2000] and brown dog tick *Rhipicephalus sanguineus* [@lees2014]. Homomeric Locust *Schistocerca gregaria* $\alpha1$ [@marshall1990], *Myzus Persicae* $\alpha1$ and *Myzus Persicae* $\alpha2$ [@sgard1998] produced receptors with nAChR-like pharmacological and electrophysiological characteristics, however the channel-generated currents were of low amplitude, and the expression was inconsistent. -#### High potency of neonicotinoids on insect-hybrid receptors +##### Importance of chaperon proteins in heterologous expression of nAChRs ###{#ric3insect} -The potency of neonicotinoids on insect-mammal hybrid nAChRs have been determined using electrophysiological techniques. $\alpha$ nAChR subunit from the fruit fly, the cat flea and the planthopper were co-expressed with rat or mouse $\beta2$. The responses of the formed channel were recorded in the presence of various neonicotinoids: cyanoamidines clothianidin and imidacloprid, nitroguanidines thiacloprid and acetamiprid and nitromethylene nitenpyram. +Difficulties in recombinant receptor expression highlight the complexity of receptor formation. Assembly and oligomerisation are critical steps in the receptor maturation [@brodsky1999]. Co-expression of mammalian and *C. elegans* nAChRs with chaperon proteins highlight the critical role of ER and Golgi resident chaperons in receptor maturation. @boulin2008 demonstrated that three chaperon proteins are necessary for the expression of *C. elegans* muscle-type receptors in Xenopus oocytes: *C. elegans* UNC-50, UNC-74 and RIC-3 (more details on these proteins can be found in Sections \@ref(ric-3celegans), \@(unc-50) and \@ref(unc74)); ligand binding and agonist-evoked currents were abolished upon exclusion of any of the three proteins. RIC-3 also improves the cell surface expression of the second type of the BWM *C. elegans* receptor [@ballivet1996] and in the of neuron-type receptor in Xenopus oocytes [@halevi2002]. It also plays a role in the maturation of human receptor in Xenopus oocytes and cell lines (Section \@ref(ric-3nacho). More recently, RIC-3 has been shown to influence folding and maturation of insect nAChRs. Co-expression of Dm$\alpha2$-containing and Dm$\alpha5$/$\alpha7$ receptors with RIC-3 improved [@lansdell2008], and in some instances enabled expression in otherwise non-permissible systems [@lansdell2012]. Up to 3.5-fold increase in specific binding of radiolabelled antagonist was noted in insect cells co-transfected with RIC-3, suggesting the presence of greater number of folded receptors on the cell surface [@lansdell2008]. Expressed receptors have been also shown to be functional. In Xenopus oocytes, ionic currents were detected in response to acetylcholine in cells co-expressing RIC-3 [@lansdell2012]. -Upward (depolarising) current was recorded from cells expressing insect-hybrid nAchRs in responses to all tested neonicotinoids. This response was dose-dependent. The potency of neonicotinoids varied, as indicated by the EC50 value, between 0.04 and 45.8 $\mu$M, however it is generally in the region of 1 $\mu$M. +<!-- <!-- RIC-3 enabled identification of potential insect nAChRs. Co expression of Drosophila $\alpha5$ and $\alpha7$ either singlularly or in combonation, gave rise to cell-surface expression, as shown by radiolabelled ligand binding [@lansdell] and heteromeric $\alpha5$/$\alpha7$. The identity of other insect receptors is unknown. --> -The rank order of potency of cyanoamidines, nitroguanidine and nitromethylene differs, depending on the receptor identity. For example, in imidacloprid and clothianidin are the most potent on the fruit fly $\alpha1$ containing receptors [@dederer2011], whereas planthopper $\alpha3\alpha8$ hybrid, thiacloprid is the most efficacious [@yixi2009]. Nitenpyram has consistently the highest EC50. +<!-- (ref:turnover) **Nicotinic acetylcholine receptor turnover.** Synthesised nAChR subunit peptides undergo folding and oligomerisation in the ER. Correctly folded receptors are transported into the Golgi (1). Misfolded subunits and misassembled receptors are retained in the ER and eventually degraded (2). Receptors transported to the Golgi undergo maturation to be shipped to the plasma membrane (4). Receptors in the plasma membrane are eventually degraded or recycled. Receptors are first packed into the endosome (4) and transported to the lysosome or proteosome for degradation (5) or re-inserted into the plasma membrane (6). --> -```{r potencyrecombinant, echo=FALSE, warning = FALSE, message=FALSE} -library(kableExtra) - library(dplyr) +<!-- ```{r turnover-label, fig.cap="(ref:turnover)", fig.scap= 'Nicotinic acetylcholine receptor turnover.', fig.align='center', echo=FALSE} --> -footnotew <- ("Receptors were expressed in Xenopus oocytes") -footnotex <- ("Rn = Rattus norvegicus (rat), Gg = Gallus gallus (chicken), Dm = *Drosophila melanogaster (fruit fly), Nl = Nilaparvata lugens (planthopper), Cf = Ctenocephalides felis (cat flea)), Lc = Lucilia cuprina (sheep blowfly)") - - potencyrecombinant <- data.frame( - Receptor = c("Nl$\\alpha1$/Rn$\\beta2$", "Nl$\\alpha2$/Rn$\\beta2$", "Nl$\\alpha3$/Rn$\\beta2$", "Nl$\\alpha3\\alpha8$/Rn$\\beta2$", "", "", "", "Dm$\\alpha1$/Gg$\\beta2$", "", "", "", "Dm$\\alpha2$/Gg$\\beta2$", "", "", "", "Cf$\\alpha1$/Gg$\\beta2$", "", "", "", "Cf$\\alpha2$/Gg$\\beta2$", "", "", "", "Cf$\\alpha4$/Gg$\\beta2$", "", "", ""), - Compound = c("Imidacloprid", "Imidacloprid", "Imidaclorprid", "Imidacloprid", "Clothianidin", "Thiacloprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram", "Imidacloprid", "Clothianidin", "Acetamiprid", "Nitenpyram"), - EC50 = c("61", "870", "350", "3.2", "5.1", "2.8", "5.6", "0.04", "0.34", "0.23", "0.4", "0.84", "5.4", "2", "35.4", "0.02", "0.15", "0.11", "0.63", "1.31", "1.65", "2.63", "24.4", "13.8", "21.3", "9.4", "45.8"), - References = c("Liu et al. 2009", "", "", "Yixi et al. 2009", "", "", "", "Dederer et al. 2011", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "", "")) - - potencyrecombinant %>% - mutate_all(linebreak) %>% - kable("latex", align = "c", booktabs = TRUE, escape = F, - col.names = linebreak(c("Receptor", "Compound", "EC50\n($\\mu$M)", "Rerefence")), - caption = 'The potency of neonicotinoids on recombinantly expressed insect hybrid nAChRs.') %>% - kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") %>% - add_footnote(notation = "none", c(footnotew, footnotex), - threeparttable = T) -``` - -Based on the expression of several potential assemblies have been identified. - -Subunits with various degree of sensitivity to neonicotinoids, suggesting some and not all receptors confer neonicotinoid sensitivity. +<!-- knitr::include_graphics("fig/general_intro/png/nAChR_turnover.png") --> +<!-- ``` --> <!-- clothiandidin on the abdominal ganglion [@thany2009] and imidacloprid on the Colorado potato beetle (CPB), . --> @@ -630,15 +756,16 @@ Subunits with various degree of sensitivity to neonicotinoids, suggesting some a <!-- "connections between afferents sensory neurons with interneurons or with motoneurons in several insects such as the cockroach" --> -### Recombinant receptors +<!-- ### Recombinant receptors --> -Recombinant insect nAChR are notoriously difficult to express. Several interventions have been tested including expression of hybrid receptor in which insect subunits have been co-expressed with mammalian ones. It need to be noted that this method has several limitations. First, hybrid receptors are not biologically relevant, thus conclusions from these studies should be drawn with caution. Second, some some of the expressed receptors may be folded, but not functional. Lastly, this method enabled expression of only a handful of receptors, thus most remained uncharacterised. This hinders their pharmacological characterisation and identification of subunits important in conferring the agricultural role of neonicotinoids. Heterologous expression of nAChR from insects and other species would allow for the characterisation of the interactions of these proteins with neonicotinoids to better define their mode of action and selective toxicity. Development of the platform in which the heterologous expression of insect nAChRs could be achieved, would open the door to screening of novel insecticides, to combat emerging and spreading neonicotinoid-resistance (Section \@ref(resgenevidence)) and @charaabi2018). In addition, by expressing nAChRs from pest and other species identification of compounds with no adverse effects on beneficial insects and other biologically important species may be achieved. Model organism *C. elegans* is a system in which the mode of action and the selective toxicity can be studied. +<!-- Recombinant insect nAChR are notoriously difficult to express. Several interventions have been tested including expression of hybrid receptor in which insect subunits have been co-expressed with mammalian ones. It need to be noted that this method has several limitations. First, hybrid receptors are not biologically relevant, thus conclusions from these studies should be drawn with caution. Second, some some of the expressed receptors may be folded, but not functional. Lastly, this method enabled expression of only a handful of receptors, thus most remained uncharacterised. This hinders their pharmacological characterisation and identification of subunits important in conferring the agricultural role of neonicotinoids. Heterologous expression of nAChR from insects and other species would allow for the characterisation of the interactions of these proteins with neonicotinoids to better define their mode of action and selective toxicity. Development of the platform in which the heterologous expression of insect nAChRs could be achieved, would open the door to screening of novel insecticides, to combat emerging and spreading neonicotinoid-resistance (Section \@ref(resgenevidence)) and @charaabi2018). In addition, by expressing nAChRs from pest and other species identification of compounds with no adverse effects on beneficial insects and other biologically important species may be achieved. Model organism *C. elegans* is a system in which the mode of action and the selective toxicity can be studied. --> -## Overview of *C. elegans* +## *C. elegans* a model platform for expression of nAChRs +As indicated, the expression of insect receptors is limited due to diffuculties in expression in and cellular environment required . have been studied in model organism *C. elegans* is a transparent non-parasitic nematode, inhabiting temperate soil environments. This worm was first described as a new species in 1900 [@maupas1900] and named *Caenorhabditis elegans* Greek *caeno* meaning recent, *rhabditis* meaning rod-like and Latin *elegans* meaning elegant. The natural isolate of this species was extracted from the compost heap in Bristol by Sydney Brenner in 1960's and named N2. Since, *C. elegans* has become a valued lab tool and a model organism due to ethical, economical and biological reasons. In contrast to vertebral organisms, *C. elegans* is not protected under most animal research legislation. The cost of use is low, due to the cost of purchase (~$6/strain), maintenance, fast life cycle and high fertility of these animals. *C. elegans* has also is also the first multicellular organism to have the whole genome sequenced [@consortium1998] and the neuronal network has been mapped [@white1986]. It has an advantage over other model organisms in that its nervous system is relatively simple and it is amenable to genetic manipulations. -## General biology ##{#genbiology} +### General biology of *C. elegans* ##{#genbiology} *C. elegans* exists as a male and hermaphrodite, with the latter sex being the more prevalent one. In the lab, 99.9 % of worms are hermaphrodites, which self-fertilize their eggs. *C. elegans* has a fast life-cycle (www.wormbook.org), which is temperature-dependent. At 15^o^C, it takes 5.5 days from egg-fertilization to the development of a worm into an adult. This process is shortened to 3.5 and 2.5 days at 20 and 25 deg;C, respectively (Figure \@ref(fig:life-cycle-label)). At 20 degrees, hermaphrodite lay eggs 2.5 hours after the fertilisation. 8 hours later the embryo hatches as a larvae in the first stage of its development (L1). In the presence of food, larvae develops into an adult through three further developmental stages, namely L2, L3 and L4. The transition between each larval stage is marked by a process of maulting, during which the old cuticle is shed and replaced by a new one. In the absence of food, developing L2 and L3 worms enter the dauer stage. The worms can remain arrested at this low metabolic activity state for up to several weeks, and will develop into adults, should the food re-appear. Hermaphrodites remain fertile for the first three days of their adulthood. Their eggs can be fertilised internally with the sperm produced by the hermaphrodite, or, if there are males available, by mating. Unmated worm can lay up to 350 eggs, whereas mated over a 1000 eggs. Figure \@ref(fig:life-cycle-label) illustrated the full *C. elegans* life cycle. @@ -674,19 +801,13 @@ EPG (electropharyngeogram) is an extracellular electrical recording from the pha ### Mode of action studies -*C. elegans* is amenable to genetic manipulations. There is a range of genetic techiques available to generate mutant strains, in which the expression of a certain protein is greatly reduced or eliminated [@boulin2012]. Using these techniques, hundreds of mutant strains have been generated. These strains have been deposited and are available for purchase from the Caenorhabditis Genetics Center (CGC). Behaviour analysis of mutant strains allows for the identification of proteins important in the regulation of many aspects of worm behaviour; an approach used for the mode of action studies. +*C. elegans* is amenable to genetic manipulations. There is a range of genetic techiques available to generate mutant strains, in which the expression of a certain protein is greatly reduced or eliminated [@boulin2012]. Using these techniques, hundreds of mutant strains have been generated. These strains have been deposited and are available from the Caenorhabditis Genetics Center (CGC). Behaviour analysis of mutant strains allows for the identification of proteins important in the regulation of many aspects of worm behaviour; an approach used for the mode of action studies. -## Cholinergic neurotransmission regulates feeding, locomotion and reproduction in *C. elegans* ## {#cholinergicneurotransmissioninworms} +### Acetylcholine regulates feeding, locomotion and reproduction in *C. elegans* ## {#cholinergicneurotransmissioninworms} Many of the *C. elegans* behaviours are regulated by acetylcholine, which is the major neurotransmitter in the nervous system of *C. elegans*. This is evident for the behavioural analysis of mutant strains in which acetylcholine neurotransmission is affected, as well as from the pharmacological effects of cholinergic agents on the behaviour of worms. -### Evidence from behavioural analysis - -The synthesis and packing of acetylcholine into synaptic vesicles are essential steps in cholinergic neurotransmission. These functions are mediated by several proteins (Figure \@ref(fig:cholsynapsecelegand-label)). Choline acetyltransferase (ChAT) encoded by the cha-1 gene catalyses the formation of acetylcholine [@rand1985]. Vesicular acetylcholine transferase (VAChT) encoded by unc-17 loads acetylcholine into synaptic vesicles [@alfonso1993]. Null mutations of these genes are lethal due to the inhibition of worm's locomotion and feeding and its eventual death due to starvation [@rand1989; @alfonso1993]. Polymorphic ChAT and VAChT mutants in which the expression is reduced, but not abolished, revealed somewhat opposite phenotype. The pharyngeal pumping both in the presence and absence of food was reduced [@dalliere2015] the movement highly uncoordinated and jerky [@rand1984], whereas egg-laying increased [@bany2003]. - -### Pharmacological evidence - -#### Aldicarb +The synthesis and packing of acetylcholine into synaptic vesicles are essential steps in cholinergic neurotransmission. These functions are mediated by several proteins. Choline acetyltransferase (ChAT) encoded by the cha-1 gene catalyses the formation of acetylcholine [@rand1985]. Vesicular acetylcholine transferase (VAChT) encoded by unc-17 loads acetylcholine into synaptic vesicles [@alfonso1993]. Null mutations of these genes are lethal due to the inhibition of worm's locomotion and feeding and its eventual death due to starvation [@rand1989; @alfonso1993]. Polymorphic ChAT and VAChT mutants in which the expression is reduced, but not abolished, revealed somewhat opposite phenotype. The pharyngeal pumping both in the presence and absence of food was reduced [@dalliere2015] the movement highly uncoordinated and jerky [@rand1984], whereas egg-laying increased [@bany2003]. Aldicarb is a synthetic carbamate mainly used as a nematicide (compound used to kill plant parasitic nematodes) [@lue1984] in the pest management system. Its mode of action is via inhibition of the acetylcholine esterase (AChE, the enzyme that breakdown acetylcholine released to the synaptic cleft) [@johnson1983]. When applied on worms, aldicarb causes hypercontraction of the body wall muscle ,leading to paralysis [@nguyen1995; @mulcahy2013], hypercontraction of the pharyngeal muscle and inhibition of feeding [@nguyen1995] as well as the inhibition of egg-laying [@nguyen1995]. These observations in conjunction with the phenotypical analysis of *cha-1* and *unc-17* mutants, suggest acetylcholine stimulates feeding, coordinates locomotion and inhibits egg-laying in *C. elegans*. @@ -702,16 +823,16 @@ Aldicarb is a synthetic carbamate mainly used as a nematicide (compound used to <!-- #### Neonicotinoids --> -(ref:cholsynapsecelegand) **Enzymes and transporters at the *C. elegans* cholinergic synapse.** Upon release into the synaptic cleft, acetylcholine is broken down to choline and acetate by acetylcholinesterase (AChE). Choline is taken up to the pre-synapse by a choline transporter (ChT). The acetyl group in transferred onto choline to product acetylcholine; a reaction catalysed by choline transferase (ChAT). Generated acetylcholine is pumped back into the synaptic vesicle by the vesicular acetylcholine transporter (AChT) for re-cycling. Names of genes are depicted in small blue letters. Image taken from @rand2006. +<!-- (ref:cholsynapsecelegand) **Enzymes and transporters at the *C. elegans* cholinergic synapse.** Upon release into the synaptic cleft, acetylcholine is broken down to choline and acetate by acetylcholinesterase (AChE). Choline is taken up to the pre-synapse by a choline transporter (ChT). The acetyl group in transferred onto choline to product acetylcholine; a reaction catalysed by choline transferase (ChAT). Generated acetylcholine is pumped back into the synaptic vesicle by the vesicular acetylcholine transporter (AChT) for re-cycling. Names of genes are depicted in small blue letters. Image taken from @rand2006. --> -```{r cholsynapsecelegand-label, fig.cap="(ref:cholsynapsecelegand)", echo=FALSE, fig.scap='Enzymes and transporters at the *C. elegans* cholinergic synapse.',fig.align='center', echo = FALSE} -knitr::include_graphics("fig/general_intro/png/cholinergic_synapse_C.elegans.jpg") -``` +<!-- ```{r cholsynapsecelegand-label, fig.cap="(ref:cholsynapsecelegand)", echo=FALSE, fig.scap='Enzymes and transporters at the *C. elegans* cholinergic synapse.',fig.align='center', echo = FALSE} --> +<!-- knitr::include_graphics("fig/general_intro/png/cholinergic_synapse_C.elegans.jpg") --> +<!-- ``` --> -### nAChRs +### *C. elegans* nAChRs -The action of acetylcholine is mediated by nAChR. *C. elegans* contains 29 genes encoding for nAChR subunits [@jones2007b]. The receptor subunits are assigned to five groups based on the sequence homology: DEG-3, ACR-16, ACR-8, UNC-38, and UNC-26 Figure (\@ref(fig:seqidentityecd-label)). +The action of acetylcholine is mediated by nAChR. *C. elegans* contains 29 genes encoding for nAChR subunits [@jones2007a]. The receptor subunits are assigned to five groups based on the sequence homology: DEG-3, ACR-16, ACR-8, UNC-38, and UNC-26 Figure (\@ref(fig:seqidentityecd-label)). Sequence identity between the insect and *C. elegans* subunits is low. Mean identity is 35 %. Least homologous are members of the DEG-3 family with the mean value of 28 %. the other three groups between 37 and 41 %. @@ -744,11 +865,11 @@ knitr::include_graphics("fig/general_intro/pdf/identity_clipped_renamed_aligned_ ``` -## Heterologous expression of nAChRs in *C. elegans* ##{hetexpeffectsofphysiology} +## Heterologous expression of nAChRs in *C. elegans* ##{#hetexpeffectsofphysiology} *C. elegans* can be used as a platform to study functional and pharmacological properties of nAChRs. This method relays on the ability to generate transgenic worms by microinjection. -Microinjection is a process by which a plasmid containing cDNA encoding for a protein of interest is injected into the syncytium distal arm of the gonad(s) of the young adult hermaphrodite worm [@stinchcomb1985]. The injected DNA in taken up by the the residing oocytes [@wolke2007], which become fertilised and develop into an adult worm. Using cellular machinery, the DNA plasmid forms extrachromosomal arrays , from which the cDNA becomes transcribed, translated and expressed [@stinchcomb1985; @mello1991]. +<!-- Microinjection is a process by which a plasmid containing cDNA encoding for a protein of interest is injected into the syncytium distal arm of the gonad(s) of the young adult hermaphrodite worm [@stinchcomb1985]. The injected DNA in taken up by the the residing oocytes [@wolke2007], which become fertilised and develop into an adult worm. Using cellular machinery, the DNA plasmid forms extrachromosomal arrays , from which the cDNA becomes transcribed, translated and expressed [@stinchcomb1985; @mello1991]. --> *C. elegans* expresses nAChRs are the neuromuscular junction and in nervous cells, thus it possesses cellular machinery necessary for the processing of these proteins. Several *C. elegens* chaperons involved in nAChRs maturation and function have been identified. RIC-3 is a ubiquitously expressed in *C. elegans* (Section \@ref(ric-3celegans)). It has a role in folding and assembly of nematode, insect (Section \@ref(ric3insect)) and vertebrate nAChRs (Section \@ref(ric3insect)). *C. elegans* RIC-3 has been shown to improve heterologous expression of insect hybrid [@lansdell2012] and mammalian nAChR [@lansdell2005] in cell lines and Xenopus oocytes. UNC-74, UNC-50 are ER and Golgi residing proteins, respectively, involved in maturation of *C. elegans* nAChRs. Whereas EAT-18 is a transmembrane protein, expressed on the cell surface, required for the function of nAChRs in the pharyngeal muscle. Details of their function can be found in Sections \@ref(unc50), \@ref(unc74) and \@ref(eat18)). It is therefore predicted that *C. elegans* has a favorable cellular environment for the expression of nAChRs. @@ -772,10 +893,10 @@ Thus, heterologous expression combined with behavioural and pharmacological anal ## Aims -The overall aim of this project is to develop *C. elegans* as a platform for the heterologous expression of nAChRs, with the aim to investigate selective toxicity of neonicotinoids insecticides. In order to use *C. elegans* as a heterologous expression system, it is necessary to achieve several goals: +The overall aim of this project is to develop *C. elegans* as a platform for the heterologous expression of nAChRs, with the aim to gain insight into selective toxicity of neonicotinoids insecticides : -1. Define sensitivity of *C. elegans* to these compounds. The representatives of three distinct chemical classes of neonicotinoids will be used: cyanoamidine clothianidin, nitroguanidine thiacloprid and nitromethylene nitenpyram. Their effects on *C. elegans* will by tested utilising behavioural and cellular assays to define their potency on distinct neuronal circuits and anatomical structured of the worm. +1. Define sensitivity of *C. elegans* to these compounds. The representatives of three distinct chemical classes of neonicotinoids will be used: cyanoamidine clothianidin, nitroguanidine thiacloprid and nitromethylene nitenpyram. Their effects on *C. elegans* will by tested utilising behavioural and cellular assays to define their potency on distinct neuronal circuits. -2. Identify suitable *C. elegans* genetic background for the expression of nAChRs. +2. Identify suitable *C. elegans* genetic background with defined cholinergic function for the expression of nAChRs. 3. Develop assays by which the functional nAChR expression and drug-sensitivity can be tested. diff --git a/02-methods.Rmd b/02-methods.Rmd index fd6f873a74c0c8c8c18d6c49c4a5d2024b355d15..542733ec9c011c5406ac1de6449db5f7212a2299 100644 --- a/02-methods.Rmd +++ b/02-methods.Rmd @@ -19,7 +19,7 @@ library(kableExtra) ## General bacterial methods ### Transformation of *E. coli* with DNA vectors -The standard protocol was followed. Briefly, from 25 to 50 $\mu$L of chemically competent Mach1 or DH5$\alpha$ *E.coli* cells were combined and gently mixed with ~10 pg of plasmid DNA. The mix was left on ice for 30 minutes. Cells were placed in 42°C water bath and after 45 seconds placed back on ice. Next, 250-500 $\mu$L of growth medium (Luria-Bertani (LB) broth) was added and cells placed in the 37°C shaking incubator for 45 minutes to 1 hour. Entire volume of cells was spread onto 10 cm LB-agar plate containing an appropriate antibiotic for selection. Antibiotics used for each vector selection are listed in Table \@ref(tab:antibiotics-used). Cells were spread on plates were left in the 37°C incubator overnight to allow for growth of transformed cells into colonies. +Briefly, 25 to 50 $\mu$L of chemically competent Mach1 or DH5$\alpha$ *E.coli* cells were combined and gently mixed with ~10 pg of plasmid DNA. The mix was left on ice for 30 minutes. Cells were placed in 42$^\circ$C water bath and after 45 seconds placed back on ice. Next, 250-500 $\mu$L of growth medium (Luria-Bertani (LB) broth) was added and cells placed in the 37 $^\circ$C shaking incubator for 45 minutes to 1 hour. The entire volume of cells was spread onto 10 cm LB-agar plate containing an appropriate antibiotic for selection. Antibiotics used for each vector selection are listed in Table \@ref(tab:antibiotics-used). Cells were spread on plates were left in the 37$^{\circ}$C incubator overnight to allow for growth of transformed cells into colonies. ```{r antibiotics-used, echo=FALSE} library(kableExtra) @@ -29,17 +29,17 @@ text_tbl <- data.frame( knitr::kable(text_tbl, format = "latex", caption = 'Selection pressure for DNA plasmids used in this study.', booktabs = TRUE) %>% kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") %>% - footnote(general = "Ampicillin used at 0.1 mg/mL, kanamycin and spectinomycin at 0.05 mg/mL. ", + footnote(general = "Ampicillin used at a final concentration of 0.1 mg/mL, whereas kanamycin and spectinomycin at 0.05 mg/mL.", threeparttable=T) ``` \newpage ### Isolation of DNA plasmid from *E. coli* ### {#miniprep} -Transformed *E.coli* colony was picked, placed in 5 mL of LB supplemented with appropriate antibiotic and incubated overnight at 37°C whilst shaking. DNA was extracted using the MiniPrep Kit (Thermo Scientific or Qiagen) following the manufacturers instructions. Centrifugation was carried out in table top centrifuge at 12 000 g. Isolated DNA was quantified in a Nanodrop UV-Vis spectophotometer. +Transformed *E.coli* colony was picked, placed in 5 mL of LB supplemented with appropriate antibiotic and incubated overnight at 37$^{\circ}$C whilst shaking. DNA was extracted using the MiniPrep Kit (Thermo Scientific or Qiagen) following the manufacturers instructions. Centrifugation was carried out in table top centrifuge at 12 000 g. Isolated DNA was quantified in a Nanodrop UV-Vis spectophotometer. ### Analytic digestion of DNA plasmids -To confirm the sizes of DNA samples, plasmids were digested with a single cutter enzyme (Promega). The reaction mix (Table \@ref(tab:RE-reaction) was incubated at 37 °C for 2-8 hours and the DNA fragments were resolved on the agarose gel (Section \@ref(electrophoresis)). +DNA plasmids were digested with restriction enzyme(s) (Promega). The reaction mix (Table \@ref(tab:RE-reaction) was incubated at 37 $^{\circ}$C for 2-8 hours and the DNA fragments were resolved on the agarose gel (Section \@ref(electrophoresis)). ```{r RE-reaction, echo=FALSE} @@ -60,7 +60,7 @@ knitr::kable(RE_reaction, "latex", escape = FALSE, booktabs = TRUE, caption = "R ### Amplification of DNA fragments by Polymerase Chain Reaction (PCR) #### Primer design -To enable the amplification of the DNA of interest, appropriate PCR primers were designed applying the following criteria: primers were unique to the annealing site on the designated DNA, 18 to 25 nucleotides long, guanine-cytosine content from 40 to 60%, melting temperature from 55 to 75°C. Where possible, primers rich in guanine and cytosine at 3’ end were selected to ensure high specificity of primer binding to the target. The primers were ordered from Eurofins Genomics, subsequently diluted in ddH~2~O to the concentration of 100 pmol/$\mu$l and stored at -20 °C. Sequences of primers used in this study can be found in Table \@ref(tab:primer-seq1). +To enable the amplification of the DNA of interest, appropriate PCR primers were designed applying the following criteria: primers were unique to the annealing site on the designated DNA, 18 to 25 nucleotides long, guanine-cytosine content from 40 to 60%, melting temperature from 55 to 75$^{\circ}$C. Where possible, primers rich in guanine and cytosine at 3’ end were selected to facilitate high specificity of primer binding to the target. The primers were ordered from Eurofins Genomics, subsequently diluted in ddH~2~O to the concentration of 100 pmol/$\mu$l and stored at -20 $^{\circ}$C. Sequences of primers used in this study can be found in Table \@ref(tab:primer-seq1). ```{r primer-seq1, echo=FALSE} library(kableExtra) @@ -146,7 +146,7 @@ library(kableExtra) library(dplyr) phusion_components <- data.frame( Component = c("Buffer", "dNTP mix", "Reverse/\nForward primer", "DNA", "Polymerase", "ddH$_2$O"), -Concentration = c("1x", "200 $\\mu$M", "500 nM", "10ng / 10 $\\mu$L reaction", "0.5U / 10$\\mu$L reaction", "up to 50 $\\mu$L")) +Concentration = c("1x", "200 $\\mu$M", "500 nM", "10ng / 50 $\\mu$L reaction", "0.5U / 50$\\mu$L reaction", "up to 50 $\\mu$L")) phusion_components %>% mutate_all(linebreak) %>% @@ -177,7 +177,7 @@ library(kableExtra) library(dplyr) phusion_components <- data.frame( Component = c("Buffer", "dNTP mix", "Reverse/\nForward primer", "DNA", "Polymerase", "ddH$_2$O"), -Concentration = c("1x", "200 $\\mu$M", "500 nM", "25ng / 10 $\\mu$L reaction", "0.25U / 10$\\mu$L reaction", "up to 50 $\\mu$L")) +Concentration = c("1x", "200 $\\mu$M", "500 nM", "25ng / 50 $\\mu$L reaction", "0.25U / 50$\\mu$L reaction", "up to 50 $\\mu$L")) phusion_components %>% mutate_all(linebreak) %>% @@ -206,7 +206,7 @@ caption = "Components assembled for Pfu polymerase-mediated PCR reaction.") %>% <!-- +-----------------------------------------------------------+ --> ### Amplification of eat-2 ### {#eat2pcr} -PCR product was gel excised and purified. 3' A overhangs were added by incubation of the purified DNA with Taq polymerase. The gene was subsequently cloned into the TOPO vector (Figure \@ref(fig:eat-topo-label)). Eat-2 was cloned into the expression vector, downstream of pmyo-2, by the recombinant cloning (Figure \@ref(fig:pdest-eat2-label)). Cloned vector was first analytically digested and then sequenced to ensure the correct DNA sequence. +PCR product was gel excised and purified. 3' A overhangs were added by incubation of the purified DNA with Taq polymerase (Section \@ref(gatewaycloning) and Table \@ref(tab:a-overhangs-addition)). The gene was subsequently cloned into the TOPO vector (Figure \@ref(fig:eat-topo-label)). Eat-2 was cloned into the expression vector, downstream of pmyo-2, by the recombinant cloning (Figure \@ref(fig:pdest-eat2-label)). Cloned vector was first analytically digested and then sequenced to ensure the correct DNA sequence. ```{r eat2-amplification, echo=FALSE} eat2_amplification <- data.frame( @@ -218,7 +218,7 @@ eat2_amplification <- data.frame( eat2_amplification %>% mutate_all(linebreak) %>% kable("latex", booktabs = T, escape = F, - col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of eat-2 from pTB207 plasmid with Pfu polymerase.") %>% + col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of eat-2 from pTB207 plasmid with Pfu polymerase (Promega).") %>% kable_styling(latex_options = "hold_position") ``` @@ -236,7 +236,7 @@ CHRNA7_amplification <- data.frame( CHRNA7_amplification %>% mutate_all(linebreak) %>% kable("latex", booktabs = T, escape = F, - col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of human $\\alpha$7 nAChR (CHRNA7) from pcDNA3.1 plasmid with Phusion polymerase.") %>% + col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of human $\\alpha$7 nAChR (CHRNA7) from pcDNA3.1 plasmid with Phusion polymerase (Thermo Scientific.") %>% kable_styling(latex_options = "hold_position") %>% footnote(general = "gradient annealing temperatures were: 50, 51,1, 53.4, 57.2, 60.2", threeparttable = T) @@ -260,7 +260,7 @@ mbp_amplification <- data.frame( mbp_amplification %>% mutate_all(linebreak) %>% kable("latex", booktabs = T, escape = F, - col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of MBP from pET26-GLIC plasmid with Pfu polymerase.") %>% + col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of MBP from pET26-GLIC plasmid with Pfu polymerase (Promega).") %>% kable_styling(latex_options = "hold_position") ``` @@ -277,7 +277,7 @@ humanlgd_amplification <- data.frame( humanlgd_amplification %>% mutate_all(linebreak) %>% kable("latex", booktabs = T, escape = F, - col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of human $\\alpha$7 nAChR ligand binding domain from pBMH plasmid with Phusion HF polymerase.") %>% + col.names = linebreak(c("Step", "Duration", "Temperature $^\\circ$C", "Number\nof cycles")), caption = "Thermal cycling conditions for amplification of human $\\alpha$7 nAChR ligand binding domain from pBMH plasmid with Phusion HF polymerase (Thermo Scientific).") %>% kable_styling(latex_options = "hold_position") ``` @@ -285,7 +285,7 @@ kable("latex", booktabs = T, escape = F, \newpage ### DNA electrophoresis ### {#electrophoresis} -To resolve the size of DNA samples, agarose gel electrophoresis was run using BioRad Wide horizontal electrophoresis system and PowerPac Basic Power Supply. The resolving gel was prepared by addition of agarose (0.6-1.2 % (w/v); Sigma Aldrich) to 1x TAE (40 mM Tris, 20 mM acetic acid, 1 mM EDTA) buffer. This mix was heated in the microwave until agarose completely melted and left on the bench to cool down to ~ 50 °C. Subsequently, Nancy-520 DNA Gel Stain (Sigma-Aldrich) at 5mg/mL was added in 1:1000 (v/v) dilution and the mixture was poured into the gel caster. Meanwhile, the DNA samples were prepared by mixing them with 1 % (v/v) loading dye. Once the gel set, the samples were loaded into wells alongside the indicated molecular weight marker. Markers variously used in this thesis include 1kb Hyperladder (Bioline), 1kb ladder (Promega) or 1 kb Plus DNA ladder (Thermo Scientific). Electrophoresis was run at 70 V until the samples were sufficiently resolved (typically 30 minutes to 2 hours) and gels imaged using Syngenta GBox. +To resolve the size of DNA samples, agarose gel electrophoresis was run using BioRad Wide horizontal electrophoresis system and PowerPac Basic Power Supply. The resolving gel was prepared by addition of agarose (0.6-1.2 % (w/v); Sigma Aldrich) to 1x TAE (40 mM Tris, 20 mM acetic acid, 1 mM EDTA) buffer. This mix was heated in the microwave until agarose completely melted and left on the bench to cool down to ~ 50 $^\circ$C. Subsequently, Nancy-520 DNA Gel Stain (Sigma-Aldrich) at 5mg/mL was added in 1:1000 (v/v) dilution and the mixture was poured into the gel caster. Meanwhile, the DNA samples were prepared by mixing them with 1 % (v/v) loading dye (Blue/Orange Loading Dye, Promega). Once the gel set, the samples were loaded into wells alongside the indicated molecular weight marker. Markers variously used in this thesis include 1kb Hyperladder (Bioline), 1kb ladder (Promega) or 1 kb Plus DNA ladder (Thermo Scientific). Electrophoresis was run at 70 V until the samples were sufficiently resolved (typically 30 minutes to 2 hours) and gels imaged using Syngenta GBox. ### DNA purification following PCR and electrophoresis Following gel electrophoresis, the band of interest was visualised under the UV light and isolated by cutting with a surgical blade. @@ -295,7 +295,7 @@ DNA was subsequently purified using GeneJET Gel Extraction Kit (Thermo Scientifi <!-- ```{r, t4-ligation-label, fig.cap="(ref:t4-ligation)", echo=FALSE, fig.width=9} --> <!-- knitr::include_graphics("fig/methods/t4_cloning.png") --> <!-- ``` --> -Vector for expression of human nAChR was generated by T4 dependent ligation. PCR-amplified, gel-excised and digested with SalI and NdeI pelB-HIS-MBP-3C was inserted into the digested pET27 plasmid. The complementary sequences were ligated with T4 ligase (Table \@ref(tab:T4-ligase)). Next, PCR-amplified, gel-excised and digested with SalI and NheI human $\alpha7$ ECD was ligated into the digested pET27-pelB-HIS-MBP-3C. Both times reaction mixtures were incubated at room temperature for 3-4 hours and used to transform chemically competent Mach1 cells. 50-100 $\mu$L of cells were transformed with 2.5-8 $\mu$L ligation reaction mix. +The vector for expression of human nAChR was generated by T4 dependent ligation. PCR-amplified, gel-excised and digested with SalI and NdeI pelB-HIS-MBP-3C was inserted into the digested pET27 plasmid. The complementary sequences were ligated with T4 ligase (Table \@ref(tab:T4-ligase)). Next, PCR-amplified, gel-excised and digested with SalI and NheI human $\alpha7$ ECD was ligated into the digested pET27-pelB-HIS-MBP-3C. Both times reaction mixtures were incubated at room temperature for 3-4 hours and used to transform chemically competent Mach1 cells. 50-100 $\mu$L of cells were transformed with 2.5-8 $\mu$L ligation reaction mix. ```{r T4-ligase, echo=FALSE} @@ -305,15 +305,13 @@ ligation_table <- data.frame( names(ligation_table) <- NULL -kable(ligation_table, format = "latex", escape = FALSE, align = 'l', booktabs = TRUE, caption = "T4 ligase reaction.") %>% kable_styling(position = "center", latex_options = "hold_position") %>% - footnote(general = "Here is a general comments of the table. ", - footnote_as_chunk = T, title_format = c("italic", "underline")) +kable(ligation_table, format = "latex", escape = FALSE, align = 'l', booktabs = TRUE, caption = "T4 ligase reaction.") %>% kable_styling(position = "center", latex_options = "hold_position") # use the option escape=FALSE to be able to pass greek letters to the table, booktabs = TRUE means there will only be a top and bottom, and not all borders, caption = NA (no caption, but the table will be in the middle, otherwise it is ligned to the left of the page) ``` -### Gateway cloning +### Gateway cloning ###{#gatewaycloning} Vectors for generation of *C. elegans* transgenic genes were generated by recombinant Gateway Cloning. <!-- (ref:gateway-cloning) Gateway recombinant cloning to generate expression vectors. The gene of interest was PCR amplified, gel pufiried and 3' A overhangs added (1) by Taq polymerase. It was then cloned into TOPO vector by TA recombination (2) reaction to generate the entry clone containing a gene of interest. Expression vector was generated by LR recombination between the L site containing entry clone and R sites containing destination vector. The desired vector was selected with an antibiotic. --> @@ -361,8 +359,7 @@ knitr::kable(topo_reaction_tb, escape = FALSE, align = 'l', booktabs = TRUE, cap ``` #### Generation of the expression vector by LR reaction -LR reaction was assembled using Gateway LR Clonase II Enzyme Mix (Invitrogen) (Table \@ref(tab:LR-reaction). Reaction was incubated at room temperature for 2 hours. To inactivate the enzyme, 2 μL of proteinase K was added and the reaction mix was incubated at 37 °C for 10 minutes. 1 μL of reaction mix was used to transform 50 μL of One Shot OmniMAX 2 T1 phage resistant cells (Invitrogen). -Following, plasmid was isolated from transformed cells and and subject to sequencing to ensure successful formation of the plasmid. +LR reaction was assembled using Gateway LR Clonase II Enzyme Mix (Invitrogen) (Table \@ref(tab:LR-reaction). Reaction was incubated at room temperature for 2 hours. To inactivate the enzyme, 2 $\mu$L of proteinase K was added and the reaction mix was incubated at 37 $^\circ$C for 10 minutes. 1 $\mu$L of reaction mix was used to transform 50 $\mu$L of One Shot OmniMAX 2 T1 phage resistant cells (Invitrogen). Transformed cells were plated and grew overnight. Following, plasmid was isolated from transformed cells and subjected to sequencing to ensure successful formation of the plasmid. ```{r LR-reaction, echo=FALSE} gateway_cloning2 <- data.frame( @@ -390,10 +387,10 @@ knitr::include_graphics("fig/methods/purification-process.png") ``` ### Growth of transformed *E. coli* cells -Chemically competent bacterial cells (BL21(DE3)) engineered for high efficiency protein expression were transformed with the authenticated expression vector as described (Section \@ref(miniprep)). Transformed colonies were resuspended and placed in 5 mL of growth medium supplemented with the appropriate antibiotic. Seed culture was placed in the shaking incubator at 37 °C and left to grow until OD600nm of 1-2. This starter culture was used to inoculate growth medium supplemented with appropriate antibiotic in 2 L baffled flasks, to the final OD600nm of 0.01-0.05. Inoculated flasks were placed in a shaking incubator at 37 °C, 250 RPM. The following protocol was followed, unless otherwise stated: At OD600nm = 0.5, the temperature was lowered to 18 °C. When the 18 °C culture reached and OD600nm ≈ 1, 0.2 mM Isopropyl β-D-1-thiogalactopyranoside (IPTG) was added and the growth continued overnight. +Chemically competent bacterial cells (BL21(DE3)) engineered for high efficiency protein expression were transformed with the authenticated expression vector as described (Section \@ref(miniprep)). Transformed colonies were resuspended and placed in 5 mL of growth medium supplemented with the appropriate antibiotic. Seed culture was placed in the shaking incubator at 37 $^\circ$C and left to grow until OD600nm of 1-2. This starter culture was used to inoculate growth medium supplemented with appropriate antibiotic in 2 L baffled flasks, to the final OD600nm of 0.01-0.05. Inoculated flasks were placed in a shaking incubator at 37 $^\circ$C, 250 RPM. The following protocol was followed, unless otherwise stated: At OD600nm = 0.5, the temperature was lowered to 18 $^\circ$C. When the 18 $^\circ$C culture reached an OD600nm ≈ 1, 0.2 mM Isopropyl β-D-1-thiogalactopyranoside (IPTG) was added and the growth continued overnight at 18 $^\circ$C. ### Protein purification ### {#purification-general-methods} -*E.coli* were harvested by centrifuging the cell culture at 5000g for 20 minutes at 4 °C and either used immediately or stored at -20 °C for further use. +*E.coli* were harvested by centrifuging the cell culture at 5000g for 20 minutes at 4 $^\circ$C and either used immediately or stored at -20 $^\circ$C for further use. Harvested cells were kept on ice throughout the purification procedure. Two methods of purification were tested: HIS-tag purification using Ni-NTA resin and maltose binding protein (MBP) purification with Sepharose-Dextrin Beads (GE Healthcare Life Sciences). ### HIS-tag purification #### {#his} @@ -405,7 +402,7 @@ Wash buffer 2: 0.1 M TRIS (pH=8), 1 M NaCl Wash buffer 3: 0.1 M TRIS, (pH=8), 0.15 M NaCl Elution buffer: 0.1 M TRIS, (pH=8), 0.15 M NaCl, 0.2 M imidazole (pH=7.5) -Cells harvested from 1 L of culture medium were re-suspended in 40 mL supplemented with 2 Pierce™ Protease Inhibitor Mini Tablets (Thermo Fisher Scientific) and sonicated on ice using the following settings: power 7, pulse on: 10 seconds, pulse off: 20 seconds, total time 6 minutes. Sonicated cells were subject to low speed spin (16000g for 45 minutes at 4 °C) to sediment cellular debris. The supernatant was collected and spun again at 100 000 g for 1 hour at 4 °C to separate non-soluble fraction (e.g. aggregated proteins) in the pellet from the supernatant containing soluble fraction. Ultra-supernatant was mixed with 0.5 mL of Ni-NTA resin (previously equilibrated in the resuspension buffer) and equilibrated for 1 hour at 4°C on the rotating tube rotator (speed 8-9). Following this overnight incubation, the mix was decanted into a low pressure 5 mL chromatography column. Resin was washed with 10 mL of each one of the 3 washing buffers. Lastly, bound to Ni-NTA resin proteins were eluted off by addition of 5 x 0.5 mL of elution buffer. Eluted fractions were stored at 4°C. At each stage, a samples consisting of the pre induction (pre-I; post induction (post-I) Homogenate (H) (Whole cells), high speed SnT (LOAD), Flow through (FT0) wash (W) and eluate (E) fractions were collected for SDS-PAGE analysis (Section \@ref(samples)). +Cells harvested from 1 L of culture medium were re-suspended in 40 mL re-suspension buffer supplemented with 2 Pierce™ Protease Inhibitor Mini Tablets (Thermo Fisher Scientific) and sonicated on ice using the following settings: power 7, pulse on: 10 seconds, pulse off: 20 seconds, total time 6 minutes. Sonicated cells were subject to 16000g spin for 45 minutes at 4 $^\circ$C to sediment cellular debris. The supernatant was collected and spun again at 100 000 g for 1 hour at 4 $^\circ$C to separate non-soluble fraction (e.g. aggregated proteins) in the pellet from the supernatant containing soluble fraction. Ultra-supernatant was mixed with 0.5 mL of Ni-NTA resin (previously equilibrated in the resuspension buffer) and equilibrated for 1 hour or overnight at 4°C on the rotating tube rotator (speed 8-9). Following this incubation, the mix was decanted into a low pressure 5 mL chromatography column. Resin was washed with 10 mL of each one of the 3 washing buffers. Lastly, bound to Ni-NTA resin proteins were eluted off by addition of 5 x 0.5 mL of elution buffer. Eluted fractions were stored at 4°C. At each stage, a samples consisting of the pre induction (pre-I; post induction (post-I) Homogenate (H) (Whole cells), high speed SnT (LOAD), Flow through (FT0) wash (W) and eluate (E) fractions were collected for SDS-PAGE analysis (Section \@ref(samples)). <!-- ### MBP purification --> <!-- The composition of buffers used is as follows : --> @@ -421,22 +418,22 @@ Cells harvested from 1 L of culture medium were re-suspended in 40 mL supplement ### Quantification of protein expression and purification Protein content of the eluted samples was measured with NanoDrop 1000 Spectrophotometer V3.7 at 280 nM and the following parameters, as measured by Compute pI/Mw tool (http://web.expasy.org/compute_pi/): Mw (kDa) of pentameric full length protein = 420.05 kDa, extinction coefficient (/1000)= 132.95. 2 $\mu$L of the elution buffer/Buffer C were used to blank the spectrophotometer, and 2 $\mu$L of the elution fractions was used to estimate the protein concentration of the sample. -### Analysis of protein sizes using denaturing sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) +### Analysis of protein molecular weight using denaturing sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) #### Sample preparation #### {#samples} -Pre and post induction whole cell samples preparation: 1 mL of E. coli cell culture was taken, spun down in tabletop centrifuge at max speed for 5 minutes. Supernatant was discarded, pellet re-suspended in 150 $\mu$L dH2O. Total protein content measured with NanoDrop by measuring protein absorbance at 280 nm. 70mg/ml of protein was loaded onto a gel in each sample. Cell lysate: following sonication, 30 $\mu$L of cell lysate was taken. Cell-debris and supernatant samples: 30 μL of cell lysate sample taken, spun down in tabletop centrifuge for 10 mins at maximum speed, at 4 °C. Supernatant was pipetted into another micro centrifuge (labelled supernatant) tube whereas pellet re-suspended in 30 $\mu$L dH2O (labelled whole-cell). Ultra-supernatant and ultra-pellet samples: 50 μL of cell lysate spun down in tabletop centrifuge for 10 mins at maximum speed, at 4 °C. 30 $\mu$L of the supernatant taken, spun down in ultracentrifuge at 100 000 g, at 4 °C for 1 hour. Supernatant was pipetted into another micro centrifuge tube (ultra-supernatant) whereas debris was re-suspended in 30 $\mu$L of dH20. The same volumes of cell-lysate, cell-debris, supernatant, ultra-supernatant, ultra-pellet and flow-through were loaded onto SDS-PAGE gels. Protein samples were mixed with sample buffer (2 % SDS, 2mM DTT, 4 % glycerol, 0.04 M Tris pH = 6.8, 0.01 % bromophenol blue) and boiled for 5 – 10 minutes. Next, 4 – 10 $\mu$L samples were loaded onto 8 – 12 % acrylamide SDS-PAGE gel alongside 4 $\mu$L of Protein Marker PageRulerTM Prestained/Unstained Protein (Thermo Fisher Scientific). +Pre and post induction whole cell samples preparation: 1 mL of E. coli cell culture was taken, spun down in tabletop centrifuge at max speed for 5 minutes. Supernatant was discarded, pellet re-suspended in 150 $\mu$L dH2O. Total protein content of 2 $\mu$L samples were measured with NanoDrop by measuring protein absorbance at 280 nm. 70mg/ml of protein was loaded onto a gel in each sample. Cell lysate: following sonication, 30 $\mu$L of cell lysate was taken. Cell-debris and supernatant samples: 30 $\mu$L of cell lysate sample taken, spun down in tabletop centrifuge for 10 mins at maximum speed, at 4 °C. Supernatant was pipetted into another micro centrifuge (labelled supernatant) tube whereas pellet re-suspended in 30 $\mu$L dH2O (labelled whole-cell). Ultra-supernatant and ultra-pellet samples: 50 $\mu$L of cell lysate spun down in tabletop centrifuge for 10 mins at maximum speed, at 4 $^\circ$C. 30 $\mu$L of the supernatant taken, spun down in ultracentrifuge at 100 000 g, at 4 $^\circ$C for 1 hour. Supernatant was pipetted into another micro centrifuge tube (ultra-supernatant) whereas debris was re-suspended in 30 $\mu$L of dH20. The same volumes of cell-lysate, cell-debris, supernatant, ultra-supernatant, ultra-pellet and flow-through were loaded onto SDS-PAGE gels. Protein samples were mixed with sample buffer (2 % SDS, 2mM DTT, 4 % glycerol, 0.04 M Tris pH = 6.8, 0.01 % bromophenol blue) and boiled for 5 – 10 minutes. Next, 4 – 10 $\mu$L samples were loaded onto 8 – 12 % acrylamide SDS-PAGE gel alongside 4 $\mu$L of Protein Marker PageRulerTM Prestained/Unstained Protein (Thermo Fisher Scientific). #### Gel electrophoresis ##### Gel preparation ####{#gelprep} -Protein samples were subject to denaturing SDS-PAGE and stained with the Commassie stain to visualise and estimate the size of protein species. SDS-PAGE constituted from a stucking gel (5 % Acrylamide/bisacrylamide, 0.72 M Tris pH = 8.4, 0.025 % ammonium persulfate, 0.4 % TEMED, 0.1 % SDS) casted over a resolving gel (12 % Acrylamide/bisacrylamide, 1 M Tris pH = 8.4, 0.06 % ammonium persulfate, 0.13 % TEMED, 0.1 % SDS). Protein samples were loaded onto a stacking gel to be concentrated before entering the resolving gel where they are separated. +Protein samples were subject to denaturing SDS-PAGE and stained with the Commassie stain to visualise and estimate the size of protein species. SDS-PAGE constituted from a stucking gel (5 % Acrylamide/bisacrylamide, 0.72 M Tris pH = 8.4, 0.025 % ammonium persulfate, 0.4 % TEMED, 0.1 % SDS) casted over a resolving gel (12 % Acrylamide/bisacrylamide, 1 M Tris pH = 8.4, 0.06 % ammonium persulfate, 0.13 % TEMED, 0.1 % SDS). BioRad electrophoresis apparatus was used. Electrophoresis chamber was filled with the running buffer (25mM Tris, 192mM glycine, 0.1 % SDS) and the electrophoresis proceeded at 80 V for 1 hour and then 120V for 2 hours. The gel was either stained to visualise all proteins present in samples, or used in Western Blot to detect the presence of a specific protein. #### Coomassie staining and imaging ####{#coomassiestaining} -Following SDS-PAGE electrophoresis, the stack and resolving gel were incubated in fixing buffer (10% acetic acid, 40% ethanol, 50 % dH2O) placed on an oscillating platform for at least 1 hour to remove gel buffer components. The fixed gel was then washed with dH2O and incubated with Coomassie stain (14 mg of Coomassie Blue R-250 (ThermoScientific) /L of dH~2~O) overnight. The gel was de-stained by incubation with dH~2~O for at least 8 hours and imaged with Gel Doc^TM^ XR+ (Bio-Rad). +Following SDS-PAGE electrophoresis, the stack and resolving gel were incubated in fixing buffer (10% acetic acid, 40% ethanol, 50 % dH2O) placed on an oscillating platform for at least 1 hour to remove background staining. The fixed gel was then washed with dH2O and incubated with Coomassie stain (14 mg of Coomassie Blue R-250 (ThermoScientific) /L of dH~2~O) overnight. The gel was de-stained by incubation with dH~2~O for at least 8 hours and imaged with Gel Doc^TM^ XR+ (Bio-Rad). -### Analysis of protein sizes using one-dimensional non-denaturing polyacrylamide gel electrophoresis +### Analysis of protein molecular weight using one-dimensional non-denaturing polyacrylamide gel electrophoresis #### Sample preparation. Two protein eluate samples were collected from the Immobilized metal affinity chromatography (IMAC) and mixed with sample buffer (4 % glycerol, 0.04 M Tris pH = 6.8, 0.01 % bromophenol blue). One sample was boiled for 5 minutes to denature proteins, whereas the other was not. Next, 4 – 10 $\mu$L prepared samples were loaded onto 12 % nondenaturing polyacrylamide gel, alongside 4 $\mu$L of 1 mg/mL of bovine serum albumin, which served as a marker. @@ -450,10 +447,10 @@ BioRad electrophoresis apparatus was used. Electrophoresis chamber was filled wi ### Western Blots ###{#western} #### Protein Transfer -Resolved protein are transferred to PVDF (Polyvinylidene difluoride) membrane cut to the size of the resolving gel was equilibrated for 15 minutes to 1 hour in the transfer buffer (12.1g Tris, 57.6 g glycine, 800 mL methanol in total volume of 4 L) then washed with dH2O followed by methanol. Freshly run polyacrylamide gel was placed on top of the submerged in transfer buffer sponge, 2 x filter paper and PVDF membrane stack and covered with 2 x filter paper. Assembled transfer mount with the gel and PVDF membrane was placed in the BioRad Mini Trans-Blot Module which was in turn inserted into Mini-PROTEAN® Tetra Cell tank. The tank was filled with transfer buffer and the protein transferred from the gel onto the membrane at 100 V constant voltage for for 1 - 3 hours at 4 °C. +Resolved protein are transferred to PVDF (Polyvinylidene difluoride) membrane cut to the size of the resolving gel was equilibrated for 15 minutes to 1 hour in the transfer buffer (12.1g Tris, 57.6 g glycine, 800 mL methanol in total volume of 4 L) then washed with dH2O followed by methanol. Freshly run polyacrylamide gel was placed on top of the submerged in transfer buffer sponge, 2 x filter paper and PVDF membrane stack and covered with 2 x filter paper. Assembled transfer mount with the gel and PVDF membrane was placed in the BioRad Mini Trans-Blot Module which was in turn inserted into Mini-PROTEAN® Tetra Cell tank. The tank was filled with transfer buffer and the protein transferred from the gel onto the membrane at 100 V constant voltage for for 1 - 3 hours at 4 $^\circ$C. #### Antibody binding ####{#abs} -Potential transfer of his-tagged recombinant proteins were detected using 1mg/mL monoclonal mouse anti-Hexa-His primary antibodies (Thermo Fisher Scientific) and 1mg/mL IRDye® 680RD Goat anti-Mouse IgG (Li-Cor) used at 1 in 1000 dilution. PVDF membrane was incubated for at least 1 hour in blocking, primary and secondary antibody buffer (Table \@ref(tab:WB-buffers)). To remove residual solution, three 10-minute-long washes were carried out in-between and after last incubations. +Transfer of his-tagged human $\alpha7$ nAChR ECD-chimera protein were detected using 1mg/mL monoclonal mouse anti-Hexa-His primary antibodies (Thermo Fisher Scientific) and 1mg/mL IRDye® 680RD Goat anti-Mouse IgG (Li-Cor) used at 1 in 1000 dilution. PVDF membrane was incubated for at least 1 hour in blocking, primary and secondary antibody buffer (Table \@ref(tab:WB-buffers)). To remove residual solution, three 10-minute-long washes were carried out in-between and after last incubations. ```{r WB-buffers, echo=FALSE, fig.pos = 'H'} @@ -471,13 +468,13 @@ knitr::kable(wb_bfrs, escape = FALSE, align = 'l', booktabs = TRUE, caption = "C ``` #### Western Blot imaging -Immunodecorated PVDF were imaged using Odyssey® imaging system (Li-Cor Biosciences). Images in the 800 nm channel detects protein bands tagged by the IRDye 800CW secondary antibody. This was cross referenced to images scanned in the 700 nm to detect protein ladder bands and 800 nm channels. +Immunodecorated PVDF were imaged using Odyssey imaging system (Li-Cor Biosciences). Images in the 800 nm channel detects protein bands tagged by the IRDye 800CW secondary antibody. This was cross referenced to images scanned in the 700 nm to detect protein ladder bands and 800 nm channels. #### Gel filtration -Protein purified by the Ni-NTA resin were subject to size exclusion chromatography with GE Healthcare Superdex^TM^ 200 10/300GL column with the separation range between 10 and 600 kDa. This methods allows for the molecular weight assessment and separation of proteins present in the sample. +Protein purified and eluted with the Ni-NTA resin were subject to size exclusion chromatography with GE Healthcare Superdex^TM^ 200 10/300GL column with the separation range between 10 and 600 kDa. This methods allows for the molecular weight assessment and separation of proteins present in the sample based on their mobility through the resin-filled column. #### Sample preparation -Sample prepared with VIVASPIN20 column with the cut off point of 30 kDa (Sartorius) by spinning down in a centrifuge at 36 000 RPM at 4 °C. +Sample prepared with VIVASPIN20 column with the cut off point of 30 kDa (Sartorius) by spinning down in a centrifuge at 36 000 RPM at 4 $^\circ$C. #### Buffers Buffer used : 0.1M TRIS (pH=8), 0.15 M NaCl degassed and ddH20 degassed. @@ -534,27 +531,27 @@ eat-2 (ad465) II Ex; [[pDESTgcy32 (Pmyo-2::CHRNA7)]; [pDESTgcy32 (Pmyo-3::GFP)]] eat-2 (ad465) II Ex; [[pDESTgcy32 (Pmyo-2::EAT-2); [pDESTgcy32 (Pmyo-3::GFP)]] ### *C. elegans* culture -*C. elegans* strains were cultured at 20 °C on the nematode growth medium (NGM) [@brenner1974] and fed with *E.coli* OP50. Worms were picked with a platinum wire. +*C. elegans* strains were cultured at 20 $^\circ$C on the nematode growth medium (NGM) [@brenner1974] and fed with *E.coli* OP50. Worms were picked with a platinum wire. ### NGM plates ### {#plates} -NGM was prepared weekly in 4 or 8 L batches as described: 2% agar (w/v), 0.25% peptone (w/v), 50 mM NacL (w/v) in dH~2~0. The components were autoclaved and cooled to 55°C, then 1 mM MgSO~4~, 1mM CaCl~2~, 1 mM K~2~HPO~4~ and 0.1 % cholesterol were added. 10 mL NGM portions were poured into 5.5 cm Petri dishes with a peristaltic pump. Once solidified, NGM were seeded with 50 $\mu$L of OP~50~ Escherichia coli strain. OP was applied in the middle of the plate, creating a round food patch for *C. elegans* to feed on, and left overnight to grow. +NGM was prepared weekly in 4 or 8 L batches as described: 2% agar (w/v), 0.25% peptone (w/v), 50 mM NacL (w/v) in dH~2~0. The components were autoclaved and cooled to 55$^\circ$C, then 1 mM MgSO~4~, 1mM CaCl~2~, 1 mM K~2~HPO~4~ and 0.1 % cholesterol were added. 10 mL NGM portions were poured into 5.5 cm Petri dishes with a peristaltic pump. Once solidified, NGM were seeded with 50 $\mu$L of OP~50~ Escherichia coli strain. OP was applied in the middle of the plate, creating a round food patch for *C. elegans* to feed on, and left overnight to grow. ### OP~50~ plate preparation -Fresh stock of OP50 plates were prepared at monthly intervals. A single colony was picked from the OP~50~ stock plate and placed in 10 mL of LB. Following the overnight growth, cells were streaked on a plate and allowed to form colonies by incubation at 37 °C. +Fresh stock of OP50 plates were prepared at monthly intervals. A single colony was picked from the OP~50~ stock plate and placed in 10 mL of LB. Following overnight growth, cells were streaked on a plate and allowed to form colonies by incubation at 37 $^\circ$C. ### OP~50~ culture -To prepare OP~50~ culture, a single colony was picked the OP~50~ stock plate and placed in 10 mL of LB. Bacterial culture was grown in a shaking incubator at 37 °C until OD~600nm~ reached 0.6 to reach the exponentially growing phase. Cultures were stored at 4 °C for up to 2 week and used to seed NGM plates. +To prepare OP~50~ culture, a single colony was picked the OP~50~ stock plate and placed in 10 mL of LB. Bacterial culture was grown in a shaking incubator at 37 $^\circ$C until OD~600nm~ reached 0.6 to reach the exponentially growing phase. Cultures were stored at 4 $^\circ$C for up to 2 week and used to seed NGM plates. ### General *C. elegans* methods -All experiments, with the exception of the development assay, were performed on young hermaphrodite adults (L4+1 day). Drugs and reagents were purchased from Sigma Aldrich, unless otherwise stated. Behavioral observations were made using a binocular microscope, unless otherwise stated. Results are expressed as mean ± SEM of ‘N’ determinations. Graph generation and measurement of EC~50~ or IC~50~ were performed in GraphPad (version 6.07). Concentration response curves were fitted into nonlinear regression sigmoidal dose-response (three parameter logistic) equation. +All experiments, with the exception of the development assay, were performed on young hermaphrodite adults (L4+1 day). Drugs and reagents were purchased from Sigma Aldrich, unless otherwise stated. Behavioral observations were made using a binocular microscope, unless otherwise stated. Results are expressed as mean ± SEM of ‘N’ determinations. Graph generation and measurement of EC~50~ or IC~50~ were performed in GraphPad (version 6.07). Concentration response curves were fitted into nonlinear regression sigmoidal dose-response (three parameter logistic) equation [@hill1910]. ### Drug stocks -5-HT was used in form of serotonin creatinine sulfate monohydrate, ampicillin in form of sodium salt, whereas nicotine in form of nicotine salt. Stock concentration of FITC-alpha-bungarotoxin (FITC-$\alpha$-Bgtx) at 500$\mu$g/ml was made in ddH~2~O. Thiacloprid and clothianidin were dissolved in 100% dimethyl sulfoxide (DMSO). Nitenpyram and nicotine stocks were prepared by dissolving drugs in dH~2~0 and diluted to the indicated final concentrations. Working concentration of 100$\mu$g/mL FITC-$\alpha$Bgtx was prepared and stored at 4°C for up to 2 weeks. Solution was span down briefly before use to precipitate aggregates. Drugs were stored at -18 °C for long time storage (>1 month). Once defrosted, they were used within 2 weeks or discarded. Nitenpyram stock was made immediately prior to the experiment and it was protected from light using foil to prevent photo-degradation. Buffers used for the behavioral assays in liquid were supplemented with 0.1% (w/v) Bovine Serum Albumin (BSA), which prevents worms from sticking to the bottom of the experimental plate. Therefore, in-text M9 and Dent’s solution refer to buffers supplemented with BSA, unless otherwise stated. +5-HT was used in form of serotonin creatinine sulfate monohydrate, ampicillin in form of sodium salt, whereas nicotine in form of hydrogen tartrate salt. Stock concentration of FITC-alpha-bungarotoxin (FITC-$\alpha$-Bgtx) at 500$\mu$g/ml was made in ddH~2~O. Thiacloprid and clothianidin were dissolved in 100% dimethyl sulfoxide (DMSO). Nitenpyram and nicotine stocks were prepared by dissolving drugs in dH~2~0 and diluted to the indicated final concentrations. Working concentration of 100$\mu$g/mL FITC-$\alpha$Bgtx was prepared and stored at 4$^\circ$C for up to 2 weeks. Solution was span down briefly before use to pellet aggregates. Drugs were stored at -18 $^\circ$C for long time storage (>1 month). Once defrosted, they were used within 2 weeks or discarded. Nitenpyram stock was made immediately prior to the experiment and protected from light using foil to prevent photo-degradation. Buffers used for the behavioral assays in liquid were supplemented with 0.1% (w/v) Bovine Serum Albumin (BSA), which prevents worms from sticking to the bottom of the experimental plate. Therefore, in-text M9 and Dent’s solution refer to buffers supplemented with BSA, unless otherwise stated. ### Effects of drugs on intact *C. elegans* locomotion and feeding behavior upon acute exposure. {#liquidassay} All assays were performed in M9 medium. M9 buffer composition is (g/litre): 6g Na~2~HPO~4~, 3g KH~2~PO~4~, 5g NaCl, 0.25g MgSO~4~.H~2~O. Worms were exposed to varying indicated concentrations of nicotine or neonicotinoids for a maximum period of 2 hours. The effects of these compounds on locomotion and feeding was scored. -10 x stock concentrations nicotine, nitenpyram and 5-HT were added to the assay to give the indicated final concentration. To keep the concentration of DMSO below the concentration that have known effects the stocks of thiacloprid and clothianidin in 100 % DMSO were used in 1 in 200 (0.5%), dilution and mixed vigorously with buffer. +10 x stock concentrations nicotine, nitenpyram and 5-HT were added to the assay to give the indicated final concentration. To keep the concentration of DMSO below the concentration that have known effects (data not shown) the stocks of thiacloprid and clothianidin in 100 % DMSO were used in 1 in 200 (0.5%), dilution and mixed vigorously with buffer. #### Effects of drugs on of intact *C. elegans* in liquid ####{#thrashing} Whilst in liquid, worms exhibit rhythmical swimming-like behaviour known as thrashing. A single thrash was defined as a complete bend in the mid-point of the body. Experiments were performed in a 24-well plate filled with 450 or 497.$\mu$L buffer. 50 $\mu$L nicotine/ nitenpyram/vehicle or 2.5 $\mu$L thiacloprid/clothianidin was added to the final volume of 500 $\mu$L to achieve final desired concentration. @@ -576,19 +573,20 @@ Following the initial thrashing count (Section \@ref(thrashing)), worms were tra Alongside this test group, a positive and a negative control experiments were carried out. For the positive control, worms were transferred from buffer to drug containing medium and to drug containing medium. For a negative control, worms were transferred from buffer to buffer containing a drug solvent and back to the buffer. #### Effects of drugs on pharmacologically induced pharyngeal pumping of intact *C. elegans* #### {#pumping} -To determine the effects of compounds on feeding behavior of intact worms, pharyngeal pumping assay was used. Experiments were performed in a 24-well plate in a total volume of 500 $\mu$L (Section \@ref(liquidassay)). Worms were picked off the food and placed in a well containing buffer. To paralyse and stimulate their pharyngeal pumping, 5-HT was added to the final concentration of 10 mM. After 30 minutes, basal pumping rate was measured by counting the number of grinder movements per minute (where forward lateral movement of the grinder and its return to the resting place was counted as 1). Following, the treatment/solvent was added and the effects on pumping were recorded 30 minutes later. Data were displayed in pumps per second (Hz). Pharyngeal pumping assay was employed to determine the effects of compounds on the pharynx- a feeding organ of worms. Pharyngeal pumping is mediated by three main muscular anatomical structures (the corpus, anterior isthmus and the terminal bulb) which contract and relax to suck and push in the food. This activity is coupled with a movement of the grinder - a structure responsible for crushing the food into smaller particles so it can be passed down into the intestine. Therefore, to score this behaviour, the number of grinder movements per minute (where forward lateral movement of the grinder and its return to the resting place was counted as 1). In this assay, worms were assayed in the pharyngeal stimulant 5-HT. In liquid the presence of 5-HT causes immobility and stimulate pharyngeal pumping. Experiments were performed in a 24-well plate in a total volume of 500 μL (or in 250 μL for nitenpyram). Worms were picked off the food and placed in a well containing buffer. 5-HT was added from stock to a final concentration of 10 mM. After 30 minutes, the 5-HT stimulated pump rate was measured. Following, the treatment/solvent was added and the effects on pumping were recorded 30 minutes later. Data was collected in collaboration with Amelia Lewis and displayed in pumps per second (Hz). -#### Effects of drugs on *C. elegans* morphology +To determine the effects of compounds on feeding behavior of intact worms, pharyngeal pumping assay was used. Experiments were performed in a 24-well plate in a total volume of 500 $\mu$L drug-containign buffer (Section \@ref(liquidassay)). Worms were picked off the food and placed in a well containing buffer. To paralyse and stimulate their pharyngeal pumping, 5-HT was added to the final concentration of 10 mM. After 30 minutes, basal pumping rate was measured by counting the number of grinder movements per minute (where forward lateral movement of the grinder and its return to the resting place was counted as 1). Following, the treatment/solvent was added and the effects on pumping were recorded 30 minutes later. Data were displayed in pumps per second (Hz). + +#### Effects of drugs on *C. elegans* size To determine the effects of drug exposure on worms size, *bus-17* worms were submerged in 1 mL of buffer or 100 $\mu$L for nitenpyram experiment containing 50 mM nicotine, 50 mM nitenpyram, 1.5 mM thiacloprid or 2.5 mM clothianidin or vehicle control (dilutions described in Section \@ref(onset)) in 12 well plates. 4 hours later, worms were transferred by pipetting onto 2% agarose pads and immobilised with 6 $\mu$L of 10 mM sodium azide. Images were taken immediately using Nikon Eclipse Microscope. Size of worms was determined in ImageJ. The scale was set using a graticule and length measured from the tip of the tail to the tip of the head with the freehand function. For improved accuracy, three measurements of each worm were taken and an average derived. -### Effects of drugs on intact *C. elegans* behaviour upon 24-hour exposure. +### Effects of drugs on intact *C. elegans* behaviour upon 24-hour exposure ###{#onplateassay} On-plate assays were carried out to determine the effects of prolonged drug exposure on *C. elegans* behaviour. Worms were placed on agar plates containing the indicated drug / drug vehicle and a food source in form of *E. coli* OP50 patch. All drugs were added at 1 in 200 dilution. ### Plate preparation -NGM was prepared as described in Section \@ref(plates). 50 $\mu$L of drug solution at appropriate concentration was added to 10 mL of molten NGM at approx 50 °C and mixed by gentle inversion. 3 mL of such mix was placed in each of the three successive wells of a 6-well plate (Figure \@ref(fig:on-plate-assay-method)). The medium was left overnight to solidify. One well was then seeded with 50 $\mu$L of OP~50~ culture, whereas the other two wells remained unseeded. This provided an experimental arena with the food on, the washing well and the experimental arena containing no food. In parallel, control plates containing drug solvent (water or 0.5% DMSO) were prepared. +NGM was prepared as described in Section \@ref(plates). 50 $\mu$L of drug solution at appropriate concentration was added to 10 mL of molten NGM at approx 50 $^\circ$C and mixed by gentle inversion. 3 mL of such mix was placed in each of the three successive wells of a 6-well plate (Figure \@ref(fig:on-plate-assay-method)). The medium was left overnight to solidify. One well was then seeded with 50 $\mu$L of OP~50~ culture, whereas the other two wells remained unseeded. This provided an experimental arena with the food on, the cleaning well and the experimental arena containing no food. In parallel, control plates containing drug solvent (water or 0.5% DMSO) were prepared. Due to heat instability, nitenpyram plates were prepared by pipetting 50 $\mu$L of drug solution onto solidified 3 mL NGM. The plates were left overnight to enable diffusion of the compounds into the solid agar. The appropriate well was then seeded. Nitenpyram-containing plates were covered with aluminium foil at all times. (ref:on-plate-assay-fig) **Diagram of the 24-hour “on-plate” assay arena.** Drug or drug solvent was incorporated into the NGM and poured into rows of 6-well plate. Wells in the first column were seeded with the OP~50~. 2-4 L4+1 worms were placed on the experimental arena containing food source. After 24 hour exposure, pumping rate on food and the number of eggs laid per worm were counted. Following, worms were transferred to the cleaning well and left for 5-10 minutes to remove the residual food. Worms were then transferred to the experimental arena containing no food source. After period of acclimatisation (5-10 minutes), their locomotion on food was measured by counting body bends. @@ -621,7 +619,7 @@ knitr::include_graphics("fig/methods/developmental_stages_annotated.jpg") ### Effects of drugs on *C. elegans* pharyngeal pumping in dissected head preparation. -#### Dissection of worms to remove the cuticular barrier +#### Dissection of worms to remove the cuticular barrier ####{#cuthead} L4+1 worms were picked off food and placed in 3.5 cm Petri dish filled with 3 mL Dent's saline. Heads containing pharyngeal musculature and nerves is separated from the rest of the body (Figure \@ref(fig:cut-head-image)). By doing so, the cuticular barrier is removed and a portion of the pharynx is exposed to the external solution. The pharynx in cut-head preparation retains its function. It pumps at an average rate of 0.13 Hz over the period of 120 minutes (Figure \@ref(fig:cut-head-ctr-label)). Pumping was defined as described previously (Section \@ref(pumping)), counted for a period of 30 seconds and expressed in Hz. Only worms pumping at rate >0 were used in subsequent experiments. #### Experimental arena @@ -659,7 +657,7 @@ knitr::include_graphics("fig/results3/liquid_basal_modified.png") ### Stimulatory effects of drugs on pharyngeal pumping of dissected *C. elegans* -#### Effects of 5-HT ####{#cuthead} +#### Effects of 5-HT ####{#cuthead-5ht} Following dissection, the heads were placed in Dent's solution. After 5 minutes the initial count of pharyngeal pumping was made and heads were transferred to a drug containing well. Pharyngeal pumping was estimated at 10, 20, 30, 60 minutes after being placed in the drug. Heads were transferred to Dent’s solution for recovery and pumping measured 30 mins later (90 minutes after starting the measurements). As a negative control, worms were incubated in buffer throughout the duration of the experiment. #### Effects of neonicotinoids and nicotine @@ -673,7 +671,7 @@ Cut heads were exposed to 1 $\mu$M 5-HT for 10 minutes to stimulate pumping. Fol Cut heads were prepared (Section \@ref(cuthead)) and transferred to the experimental arena by pipetting. Extracellular recordings were made with an electropharyngeogram (EPG) technique (Figure \@ref(fig:EPG-setup-method)). #### Preparation of a microelectrode -Non-filamented borosillicate capillary tube (Havard apparatus) with outer diameter (OD) of 1.5 mm and internal diameter (ID) of 0.1 mm was pulled with a Narishige puller (model PC:10). The puller was set at 98.2 °C for step 1 and 72.8 °C for step 2 to make a tip of ~ 10 $\mu$m. The needle was back-filled with Dent’s using a micropipette filler (250 $\mu$m ID, 350 $\mu$m OD, World Precision Instruments). +Non-filamented borosillicate capillary tube (Havard apparatus) with outer diameter (OD) of 1.5 mm and internal diameter (ID) of 0.1 mm was pulled with a Narishige puller (model PC:10). The puller was set at 98.2 $^\circ$C for step 1 and 72.8 $^\circ$C for step 2 to make a tip of ~ 10 $\mu$m. The needle was back-filled with Dent’s using a micropipette filler (250 $\mu$m ID, 350 $\mu$m OD, World Precision Instruments). #### Experimental set-up The microelectrode was inserted into a microelectrode holder containing a a silver wire. The microelectrode was inserted into a headstage (HS-2A Asoclamp) and carefully lowered using a micromanipulator (Burleigh) into a recording chamber filled with Dent’s saline and resting on a stage of Axoscope 2 (Zeiss) microscope. The reference electrode was made with a glass capillary filled with 2 % agar in 3 M KCl. The reference electrode was placed in the recording chamber and connected to the amplifier headstage via a dish filled with 3 M KCl solution and a silver wire electrode. The cut head was placed in a recording chamber and a tight seal between the tip of the nose and the microelectrode was made by applying suction. The extracellular electrical signals from the pharynx were amplified by an Axoclamp-2B Microelectrode Amplifier, digitized by Digidata 1322A and recorded with Axoscope 9.2. @@ -697,7 +695,7 @@ Pump duration: the average duration of all EPGs in the period of the maximum pum ### Microinjection to generate *C. elegans* transgenic lines ###{#microinjection} #### Preparation of a needle -Alluminosilicate capillaries SM100F-10 (1 mm external diameter, 0.5mm internal diameter) needle was pulled with Narishige puller (model PC:10) using the following settings: step 1 at 99 °C, step 2 at 79 °C. The pulled needle was filled with 1 $\mu$L of injection mix and assembled into Transferman NK2 (Eppendorf) micromanipulator. Microinjection was performed with FemtoJet Microinjector (Eppendorf). +Alluminosilicate capillaries SM100F-10 (1 mm external diameter, 0.5mm internal diameter) needle was pulled with Narishige puller (model PC:10) using the following settings: step 1 at 99 $^\circ$C, step 2 at 79 $^\circ$C. The pulled needle was filled with 1 $\mu$L of injection mix and assembled into Transferman NK2 (Eppendorf) micromanipulator. Microinjection was performed with FemtoJet Microinjector (Eppendorf). #### Generation of transgenic lines @@ -707,6 +705,8 @@ Test DNA plasmid was prepared with a Green Fluorescent Protein (GFP) co-injected ##### Injection L4+1 was picked from NGM plate, was immobilised by gently pressing it into a drop of Halocarbon oil 700 on 2 % agarose pad. The agarose pad was placed on a stage of Nikon Eclipse TE200 microscope and the syncytium of the anterior and/or posterior arm of the *C. elegans* gonad was injected with the DNA mix. Injected worms were gently liberated from the oil with a pick and placed on individual seeded NGM plates. +\newpage + ##### Screening of injected plates The progeny of injected worms were viewed under the fluorescent microscope and GFP filter. Green F1 worms were picked individually onto separate seeded NGM plates and left to propagate. Plates containing green F2s were collected and kept as separate stable lines (Figure \@ref(fig:selection-process-label). @@ -716,11 +716,12 @@ The progeny of injected worms were viewed under the fluorescent microscope and G knitr::include_graphics("fig/methods/select-transgenic-worms.png") ``` +\newpage ### Determination of human nAChR expression in the *C. elegans* pharynx by staining with conjugated $\alpha7$ selective antagonist FITC-$\alpha$Bgtx ###{#fitcmethod} #### Worm preparation -Worms were submerged in 3 mL of Dent's saline in 5 cm Petri dish. To ease dissection, they were paralysed by placing the dish at -20 °C for 5 minutes. Following this, the tip of the nose was cut perpendicular to the head to allow the cuticle to roll back and expose the pharynx. Next, the cut just below the terminal bulb was made and liberated pharynxes collected (Figure \@ref(fig:exposed-pharynx-label)). +Worms were submerged in 3 mL of Dent's saline in 5 cm Petri dish. To ease dissection, they were paralysed by placing the dish at -20 $^\circ$C for 5 minutes. Following this, the tip of the nose was cut perpendicular to the head to allow the cuticle to roll back and expose the pharynx. Next, the cut just below the terminal bulb was made and liberated pharynxes collected (Figure \@ref(fig:exposed-pharynx-label)). (ref:exposed-pharynx-method) **Exposure of the *C. elegans* pharynx.** Using surgical blade, the cut was made at a tip of the nose and just below the terminal bulb (left image, black lines) to expose the pharynx (right). diff --git a/03-results-01.Rmd b/03-results-01.Rmd index b7ac25cbda0797a2bd442106b3f54315188f5be5..3f6d91deaedd202379c4039b10f8a9ab46f4db15 100644 --- a/03-results-01.Rmd +++ b/03-results-01.Rmd @@ -13,7 +13,7 @@ library(knitr) ``` ## Introduction -Neonicotinoids are the most commonly used insecticides worldwide due to their high efficacy against pest insects (Section \@ref(potentpests)), selective toxicity to insect pests over mammals (Section \@ref(seltox)) and advantageous physicochemical attributes (Section \@ref(physchem)). The main disadvantage of these compounds is that they can be toxic to non-target species, including bees (Section \@ref(sublethal)). This undesired ecotoxicological effect spurred a debate over their environmental impact and revealed a necessity to further investigate their effects on other ecologically important organisms such as worms. +Neonicotinoids are the most commonly used insecticides worldwide due to their high efficacy against pest insects (Section \@ref(potentpests)), selective toxicity to insect pests over mammals (Section \@ref(seltox)) and advantageous physicochemical attributes (Section \@ref(physchem)). The main disadvantage of these compounds is that they can be toxic to non-target species, including bees (Section \@ref(sublethal)). This undesired ecotoxicological effect spurred a debate over their environmental impact and revealed a necessity to further investigate their effects on other ecologically important organisms such as worms. ## Ecological role of non-parasitic worms @@ -34,7 +34,7 @@ The levels of neonicotinoids in terrestrial terrains vary depending on the compo Cholinergic system is the primary target of neonicotinoids in insects (Section \@ref(neonicstarget)). Acetylcholine is pivotal in regulation of worm behaviour (Section \@ref(cholinergicneurotransmissioninworms)). Most of the current knowledge is derived from work on soil nematode and model organism *C.elegans*. #### Locomotion ####{#locomotion} -*C. elegans* exhibits distinct locomotory behaviours in liquid and on the solid medium (Section \@ref(locomotionbehaviour)). These behaviours are mediated by the body musculature composed of 95 muscle cells. The muscle cells are arranged into 4 muscle rows: a pair of longitudinal ventral rows and a pair of dorsal rows. Their function is under the control of the nervous system (Figure \@ref(fig:motility-intro-label)). +*C. elegans* exhibits distinct locomotory behaviours in liquid and on the solid medium (Section \@ref(locomotionbehaviour)). In the liquid medium, it flexes back and forth, whereas on solid medium it crawls is a sinusoidal fashion. These behaviours are mediated by the body musculature composed of 95 muscle cells. The muscle cells are arranged into 4 muscle rows: a pair of longitudinal ventral rows and a pair of dorsal rows. Their function is under the control of the nervous system (Figure \@ref(fig:motility-intro-label)). There are 4 motor neuron classes synapsing onto dorsal muscle (AS, DA, DB, and DD) and 4 innervating ventral muscle (VA, VB, VC, and VD). Motor neurons belonging to class A, B and AS release ACh and are excitatory, whereas motor neurons of class D are inhibitory and release GABA [@mcintire1993]. Bend of dorsal side is associated with excitation and contraction of the dorsal side and simultaneous inhibition and relaxation of the ventral side, whereas the reverse is true when the ventral side bends. A and B neurons not only innervate muscle, but also send out processes to the collateral side, and synapse onto D, inhibitory neurons [@white1986]. By doing so, acetylcholine acts directly on the muscle to elicit contraction and indirectly to relax the opposite side. Taken together, this allows the bending of a particular portion of one and the relaxation of the opposing side of the body to enable worm’s locomotory activities. Whereas the propagation of the electrical signal down the axis of the muscle whilst on solid medium, results in the forward movement. ##### Regulation of locomotory behaviour @@ -43,8 +43,8 @@ The rhythmical pattern of muscular contraction and relaxation of the BWM is not ##### Regulation of the direction of movement The direction of worm’s movement is controlled by so called command interneurons [@chalfie1985; @white1986]. There are 5 command interneurons, namely PVC, AVB, AVA, AVD and AVE. These make synaptic connections with appropriate motor neurons of the BWM. PVC and AVB innervate VB and DB neurons which regulate forward movement. AVA, AVD and AVE innervate VA and VB which regulate backward movement [@chalfie1985; @white1986]. -#### Sensory regulation of the locomotion -Locomotion can be regulated by the environmental cues detected by the sensory neurons which relay information into locomotory circuitry. There are a range of stimuli *C. elegans* respond to, including noxious stimuli and olfactory cues. For example, in response to a range of nociceptive stimuli ASH head neurons are activated [@hilliard2005]. This leads to rapid and transient backward movement, followed by a change of direction in the forward movement (reviewed in @bono2005). +#### Sensory regulation of the locomotion ####{#sensoryregulation} +Locomotion can be regulated by the environmental cues detected by the sensory neurons which relay information into locomotory circuitry. Locomotion on solid medium is greatly influenced by the present of food [@dalliere2017]. Whilst on food, *C. elegans* exhibits two types of locomotory behaviour: dwelling and roaming. Dwelling is characterised by enahnced turning frequency but low movement speed rate, whereas roaming is associated with decreased turning frequency but higher movement speed. Upon transfer to the area with no food source, worms search of food evident by enahnced movement speed. *C. elegans* locomotion is also influenced by noxious stimuli and olfactory cues. For example, in response to a range of nociceptive stimuli ASH head neurons are activated [@hilliard2005]. This leads to rapid and transient backward movement, followed by a change of direction in the forward movement (reviewed in @bono2005). (ref:motility-circuit) **Locomotory circuit in *C. elegans*.** Release of acetylcholine onto dorsal muscles (+) leads to their excitation and contraction. At the same time, acetylcholine activates GABAergic neurons contralaterally. Release of GABA leads to inhibition of ventral muscles. The signal propagates down the axis and leads to coordinated sinusoidal movement. Figure taken from www.wormatlas.org. @@ -61,14 +61,23 @@ Egg-laying is controlled by the contraction of vulvar muscles under the influenc knitr::include_graphics("fig/intro_2/vulva.jpg") ``` -### Pharmacology ###{#pharmacelegans} +#### *C. elegans* nAChRs ####{#muscletypenachr} +The identity of two muscle-type nAChRs was depicted in a combination of behavioural, pharmacological and electrophysiological approaches. + +##### L-type receptors +Behavioural analysis of *C. elegans* mutants identified several strains in which locomotion was disrupted, including unc-29, unc-38 and unc-63 [@lewis1980b]. unc-29, unc-38 and unc-63, as well as lev-1 and lev-8 were also resistant to levamisole [@lewis1980b]. Expression of lev-1, unc-29 and unc-38 in Xenopus oocytes generated a protein with nAChR-like properties: in response to acetylcholine and levamisole, depolarising current was elicited [@fleming1997]. @richmond1999 provided evidence that these receptors are expressed at the NMJ of the body wall muscle. Intracellular recordings from the post-synaptic membrane at the NMJ of the body wall muscle showed that in response to acetylcholine and levamisole inward current is elicited. That current was abolished in unc-29 and unc-38 mutants [@richmond1999]. The identity of the levamisole sensitive nAChRs was revealed by @boulin2008, who showed that eight genes are required for the generation of fully functional receptor in Xenopus oocytes. Five genes encode for nAChR subunits UNC-29, UNC-38, UNC-63, LEV-1 and LEV-8, two of which, viz. UNC-29 and LEV-1 are non-$\alpha$. In the absence of any one of the 5 subunits, agonist-evoked currents were abolished, suggesting all subunits are essential for the receptor function. The remaining 3 genes encode for the auxiliary subunits RIC-3, UNC-50, AND UNC-74. Their role is described in Section \@ref(cematnachr). + +##### N-type receptors +Work of @richmond1999 identified second type of nAChR at the muscular junction of the body wall muscle. This receptor showed high sensitivity to nicotine, thus was named N-type nAChR. N-type receptor is composed of ACR-16 subunits, which form homomeric receptors in Xenopus oocytes [@ballivet1996]. + +### Effects of nAChR agonists on *C. elegans* behaviour ###{#pharmacelegans} Pharmacological experiments in which nAChR agonists were tested against *C. elegans* behaviours provide evidence for the important role of these receptors in the regulation of locomotion and egg laying. #### Levamisole Levamisole is a synthetic compound used in treatment of parasitic worm infestation in both humans and animals [@miller1980]. It is an agonist of a subset of receptors present at a body wall muscle [@richmond1999]. Levamisole causes spastic paralysis of worms [@lewis1980b] and stimulates egg-laying [@trent1983]. -#### Nicotine -Nicotine is an exhogenous agonist, naturally occurring in Tobacco plant. Nicotine is an agonist of the second type receptor at a body wall muscle, namely the N-type, but based on the nicotine-intoxication worm phenotype, it is likely to target receptors regulating pharyngeal pumping and vulva muscle. Nicotine inhibits locomotion [@kudelska2017] pharyngeal pumping [@kudelska2018], and egg-laying. +#### Nicotine +Nicotine is an alkaloid naturally occuring in the Tobacco plant [@steppuhn2004]. It is an agonist of the second type receptor at a body wall muscle, namely the N-type [@], but based on the nicotine-intoxication worm phenotype, it is likely to target receptors regulating pharyngeal pumping and vulva muscle. Nicotine inhibits locomotion [@kudelska2017] pharyngeal pumping [@kudelska2018], and egg-laying. <!-- ### Effects of neonicotinoids on earthworms --> @@ -82,15 +91,6 @@ Neonicotinoids have variable effects on *C. elegans*. @mugova2018 reports an inh Variable effects of neonicotinoids on egg-laying are also reported. Low mM concentrations of clothianidin and thiacloprid inhibit egg-laying [@gomez-amaro2015]. In contrast, imidacloprid at a single concentration of 20 nM, elevates the number of egg-laid, but has no effect at 120 $\mu$M - 2 mM, suggesting this effect is not dose-dependent [@ruan2009]. -#### *C. elegans* nAChRs ####{#muscletypenachr} -The identity of two muscle-type nAChRs was depicted in a combination of behavioural, pharmacological and electrophysiological approaches. - -##### L-type receptors -Behavioural analysis of *C. elegans* mutants identified several strains in which locomotion was disrupted, including unc-29, unc-38 and unc-63 [@lewis1980b]. unc-29, unc-38 and unc-63, as well as lev-1 and lev-8 were also resistant to levamisole [@lewis1980b]. Expression of lev-1, unc-29 and unc-38 in Xenopus oocytes generated a protein with nAChR-like properties: in response to acetylcholine and levamisole, depolarising current was elicited [@fleming1997]. @richmond1999 provided evidence that these receptors are expressed at the NMJ of the body wall muscle. Intracellular recordings from the post-synaptic membrane at the NMJ of the body wall muscle showed that in response to acetylcholine and levamisole inward current is elicited. That current was abolished in unc-29 and unc-38 mutants [@richmond1999]. The identity of the levamisole sensitive nAChRs was revealed by @boulin2008, who showed that eight genes are required for the generation of fully functional receptor in Xenopus oocytes. Five genes encode for nAChR subunits UNC-29, UNC-38, UNC-63, LEV-1 and LEV-8, two of which, viz. UNC-29 and LEV-1 are non-$\alpha$. In the absence of any one of the 5 subunits, agonist-evoked currents were abolished, suggesting all subunits are essential for the receptor function. The remaining 3 genes encode for the auxiliary subunits RIC-3, UNC-50, AND UNC-74. Their role is described in Section \@ref(cematnachr). - -##### N-type receptors -Work of @richmond1999 identified second type of nAChR at the muscular junction of the body wall muscle. This receptor showed high sensitivity to nicotine, thus was named N-type nAChR. ACR-16 forms homomeric receptors in Xenopus oocytes [@ballivet1996], albeit the current produced in response to agonists were of small amplitude. This was markedly markedly improved when acr-16 was co-expressed with RIC-3 [@ballivet1996]. The role of RIC-3 in the maturation of this receptor type was also demonstrated in-vivo. The nicotine induced current at the body wall muscle was markedly reduced in ric-3 mutant, in comparison to the wild-type [@halevi2002]. - <!-- DEET was discovered in 1944 and was originally intendeed for use in agriculture. It is currently used as an insect repellent effective agains flies, mosquitos, ticks and fleas. --> <!-- Levamisole, discovered in 1960s, has a potent antihelmintic action [@pinnock1988]. It causes contraction of the body wall muscle of the parasitic worm **A.suum** [@martin1991] and nematode **C. elegans** [@lewis1980b], which leads to their paralysis. Body wall muscle of both **A.suum** and **C. elegans** express N- and L-type nAChR types [@qian2006; @richmond1999]. Genetic studies shed light on the receptor type targeted by levamisole. *C. elegans* mutants deficient in several constituents of L-type, and not N-type nAChR, exihibited markedly reduced levamisole-sensitivity [@lewis1987; @lewis1980], suggesting L-type receptor is the principal site of action of this compound. --> @@ -107,7 +107,7 @@ The aim of this chapter is to better understand the effects of neonicotinoids on ## Results ### Effects on thrashing -Upon immersion of *C. elegans* in liquid, it exhibits rhythmic swimming-like locomotory behaviour driven by the body wall musculature and inputs from the central nervous system (ref to intro). This locomotory behavior is known as thrashing. It can be easily scored and used as an assessment for the effects of acute exposure to nicotine and neonicotinoid on motility of *C. elegans*. Worms placed in untreated liquid medium retain a constant thrashing rate of ~40-45 repeats per 30s throughout the duration of the experiment (2 hours) (Figure \@ref(fig:thrashing-nicotine)). Addition of nicotine at concentrations ranging from 1 to 100 mM leads to dose-dependent inhibition of motility (Figure \@ref(fig:thrashing-nicotine)). The time course for the effects of nicotine varied dependent on the concentration. At doses eliciting partial paralysis (i.e. 10 and 25 mM) 2 “phases” of inhibition can be seen. The immediate one seen after 10 minutes which recovers slightly, and the second which reaches a steady state inhibition after 60 minutes. Nicotine at 100 mM led to a complete inhibition of thrashing. This effect was visible 10-minutes post exposure and sustained for 2 hours. +Upon immersion of *C. elegans* in liquid, it exhibits rhythmic swimming-like locomotory behaviour driven by the body wall musculature and inputs from the central nervous system (Section \@ref(locomotion)). This locomotory behavior is known as thrashing. It can be easily scored and used as an assessment for the effects of acute exposure to nicotine and neonicotinoid on motility of *C. elegans*. Worms placed in untreated liquid medium retain a constant thrashing rate of ~40-45 repeats per 30s throughout the duration of the experiment (2 hours) (Figure \@ref(fig:thrashing-nicotine)). Addition of nicotine at concentrations ranging from 1 to 100 mM leads to dose-dependent inhibition of motility (Figure \@ref(fig:thrashing-nicotine)). The time course for the effects of nicotine varied dependent on the concentration. At doses eliciting partial paralysis (i.e. 10 and 25 mM) 2 “phases” of inhibition can be seen. The immediate one seen after 10 minutes which recovers slightly, and the second which reaches a steady state inhibition after 60 minutes. Nicotine at 100 mM led to a complete inhibition of thrashing. This effect was visible 10-minutes post exposure and sustained for 2 hours. The EC~50~ of nicotine on thrashing was 26.2 (95% CI= 17.4 to 38.8) mM, respectively) (Figure \@ref(fig:thrashing-nicotine)b). This low efficacy may be due to reduced bioavailability of nicotine in the worm. (ref:thrashing-data) **Concentration and time dependence of the effects of nicotine on thrashing of *C. elegans*.** a) Wild type N2 worms were exposed to varying concentrations of nicotine. The number of thrashes were recorded for 30 seconds at the indicated time points. b) Concentration dependence of nicotine inhibition of thrashing on wild-type N2 worms. Dose-response curve were generated by taking the 60 minute time- points; that is when the steady-state inhibition of thrashing was reached, and expressed as % of control thrashing. EC~50~ values (dose at which thrashing was reduced by half) is shown. Data are mean $\pm$ SEM of $\ge$ 14 individual worms collected from experiments done on 3 days. @@ -130,7 +130,7 @@ knitr::include_graphics("fig/results2/final/pngpdf/Nic-DR-thrashing-n2_pH.png") \newpage ### Effects of the cuticle on nicotine induced inhibition of thrashing -The second factor limiting drugs’ bioavailability is worm’s cuticle. This idea is supported by the observation that the application of 0.1mM of nicotine on intact worm has no effects on thrashing (Figure \@ref(fig:thrashing-nicotine)), but when applied on the isolated body wall muscle or dissected worm, it induced large inward current/paralysis, respectively [@richmond1999; @matta2007]. This suggests that the cuticle is a major physical barrier for drug entry. To provide a platform for investigation of the importance of the cuticle in drug permeability, *C. elegans* *bus-17* mutant strain was used. *Bus-17* is a GT13 glycosyltransferase mutant [@yook2007] exhibiting defective glycoprotein production resulting in abnormal surface coat and altered cuticular integrity (ref to general intro). +The second factor limiting drugs’ bioavailability is worm’s cuticle. This idea is supported by the observation that the application of 0.1mM of nicotine on intact worm has no effects on thrashing (Figure \@ref(fig:thrashing-nicotine)), but when applied on the isolated body wall muscle or dissected worm, it induced large inward current/paralysis, respectively [@richmond1999; @matta2007]. This suggests that the cuticle is a major physical barrier for drug entry. To provide a platform for investigation of the importance of the cuticle in drug permeability, *C. elegans* *bus-17* mutant strain was used. *Bus-17* is a GT13 glycosyltransferase mutant [@yook2007] exhibiting defective glycoprotein production resulting in abnormal surface coat and altered cuticular integrity. Mutation of *bus-17* genes have no significant effect on the thrashing behavior of *C. elegans* frequency. Worms retained a constant thrashing rate of 40-45 thrashes per 30s over the duration of the experiment (Figure \@ref(fig:thrashing-cuticle-label)). Immersion in nicotine led to concentration dependent paralysis, but the potency of nicotine on the mutant vs the wild-type strain is almost 10-fold greater (Figure \@ref(fig:thrashing-cuticle-label)). Moreover, the inhibitory effects of nicotine at 10 and 25 mM on *bus-17* worms lacks 2 phases of inhibition seen previously. This might suggest that nicotine reaches the internal molecular targets more quickly. (ref:thrashing-cuticle) **The effects of the cuticle on the concentration and time dependence of nicotine inhibition of *C. elegans* thrashing.** N2 wild type (a) and *bus-17* mutant (b) worms were exposed to varying concentrations of nicotine. The number of thrashes were recorded for 30 seconds at the indicated time points. b) Concentration dependence of nicotine dependent inhibition of thrashing on N2 (black) and *bus-17* worms (grey). Dose-response curve were generated by taking the 120-minute time- points; that is when the steady-state of thrashing inhibition was reached, and expressed as % of control thrashing. EC~50~ values are shown on graphs. Data are mean $\pm$ SEM of $\ge$ 15 individual worms collected from paired experiments done on 3 days. @@ -170,7 +170,7 @@ To observe penetration properties of compounds, the thrashing experiment was rep \newpage -Recovery assay gives an indication of how quickly the effects of compounds reverse. This reversal when drug inhibited worms are moved into a larger volume of drug free are thought to be due to a diffusion out of the worm or/and drug metabolism via various detoxifying systems (references). In this experiment, worms were placed in drug concentration that induced full paralysis for 20 minutes in case of nicotine and 60 minutes in case of nitenpyram and thiacloprid. Once paralysis was achieved, worms were transferred to drug-free medium and the thrashing rates were monitored over time (Figure \@ref(fig:merged-recovery-title)). Following exposure to high concentration of nicotine and 2.5 hours of washing, a proportion of worms remained paralysed: 50 % of wild-type and 25 % of *bus-17* (data not shown). The remaining wild-type and *bus-17* worms recovered with 1/2 of 1.5 hours and 50 minutes respectively. +Recovery assay gives an indication of how quickly the effects of compounds reverse. This reversal when drug inhibited worms are moved into a larger volume of drug free are thought to be due to a diffusion out of the worm or/and drug metabolism via various detoxifying systems [@lindblom2006]. In this experiment, worms were placed in drug concentration that induced full paralysis for 20 minutes in case of nicotine and 60 minutes in case of nitenpyram and thiacloprid. Once paralysis was achieved, worms were transferred to drug-free medium and the thrashing rates were monitored over time (Figure \@ref(fig:merged-recovery-title)). Following exposure to high concentration of nicotine and 2.5 hours of washing, a proportion of worms remained paralysed: 50 % of wild-type and 25 % of *bus-17* (data not shown). The remaining wild-type and *bus-17* worms recovered with 1/2 of 1.5 hours and 50 minutes respectively. In contrast, all worms paralysed by nitenpyram or thiacloprid returned to normal basal thrashing within 2 hours of washing. The time taken for half recovery for both compounds was 1 hour. (ref:recovery-thrashing) **Recovery kinetics of nicotine and neonicotinoid-paralysed *C. elegans*.** N2 wild-type and *bus-17* mutant worms were exposed to indicated concentrations of nicotine (a and b), nitenpyram (c) and thiacloprid (d). Paralysed worms were transformed to drug-free dish and recovery was scored by noting a number of thrashes / 30s. Only worms recovered are included in this analysis. Alongside, worms were transferred from drug-containing to drug containing dish (+ve ctr ) and from drug-free to drug-free dish (-ve ctr). Data are mean $\pm$ SEM of 8 individual worms collected from experiments done $\ge$ 2 days. @@ -224,6 +224,8 @@ shrinking_tidy <- data19 %>% ylim(0, 1.5) + annotate("text", x=2, y=1.5, label= "**") + theme(axis.text.x = element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.ticks.x = element_blank(), axis.title.x = element_blank()) shrinking_plot @@ -232,7 +234,7 @@ shrinking_plot \newpage ### Effects of chronic exposure on behaviour -Liquid assays allow for relatively short-term exposure. To test whether protracted exposure of worms provides a better paradigm for sensitivity on-plate assay was employed (ref methods). The concentrations used were ranging from 0.5 to 25 mM nicotine, 1 mM nitenpyram, 1 $\mu$M to 1.5 mM thiacloprid and 0.5 to 3.75 mM clothianidin. Worms were exposed to treatment for a period of 24-hours and their effects on locomotion and fertility were measured. This allows for prolonged drug exposure which may lead to accumulation of the drug inside the worm and increased efficacy of compounds on worm behavior. +Liquid assays allow for relatively short-term exposure. To test whether protracted exposure of worms provides a better paradigm for sensitivity on-plate assay was employed (Section \@ref(onplateassay)). The concentrations used were ranging from 0.5 to 25 mM nicotine, 1 mM nitenpyram, 1 $\mu$M to 1.5 mM thiacloprid and 0.5 to 3.75 mM clothianidin. Worms were exposed to treatment for a period of 24-hours and their effects on locomotion and fertility were measured. This allows for prolonged drug exposure which may lead to accumulation of the drug inside the worm and increased efficacy of compounds on worm behavior. #### Effects of nicotine on avoidance During the experimentation, an observation that the proportion of worms disappeared from nicotine containing plates was made. After 24 hour incubation with nicotine at concentrations $\ge$ 25 mM, the number of worms remaining on the plate was significantly reduced in comparison to the control (Figure \@ref(fig:avoid-label). Closer observation revealed that in the presence of nicotine, worms escaped the experimental arena by crawling to the side of the plate. Neither of the three neonicotinoids had such effect (data not shown). @@ -277,6 +279,8 @@ avoid <- on_plate_dat_trans_1 %>% xlab("Nicotine, [mM]") + theme(axis.text = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), text = element_text(size=12, family="sans")) avoid @@ -285,7 +289,7 @@ avoid <- on_plate_dat_trans_1 %>% \newpage #### Effects on body bends ####{#bodybendsneonics} -Whilst on solid medium, *C. elegans* exhibits sinusoidal movement (ref to intro). This can be quantified by counting a number of forward body bends per unit of time and is a measure of the motor function. The presence of food modifies this behavior (ref to intro), therefore the measurements were made on treatment- soaked solid medium containing no OP50 food patch (reference to method). +Whilst on solid medium, *C. elegans* exhibits sinusoidal movement (Section \@ref(locomotionbehaviour)). This can be quantified by counting a number of forward body bends per unit of time and is a measure of the motor function. The presence of food modifies this behavior (Section \@ref(sensoryregulation)), therefore the measurements were made on treatment - soaked solid medium containing no OP50 food patch (Section \@ref(onplateassay)). Untreated wild-type worms move at a rate of 39 body bends per minute (Figure \@ref(fig:BB-plot-label), left panel). This is reduced to 33 bends per minute in *bus-17* mutant (Figure \@ref(fig:BB-plot-label) right panel), due to a reduced traction of the body on agar medium [@yook2007]. The body bends of wild-type *C. elegans* was altered by nicotine with with the EC~50~ of 3.6 mM (95 % CI= 2.6 to 4.4 mM), whereas nitenpyram, thiacloprid and clothianidin had no effect (Figure \@ref(fig:BB-plot-label) and \@ref(fig:DR-body-bends-label)). In contrast, the body bends rate of *bus-17* mutant was reduced by all compounds, except for up to the 1 mM nitenpyram. The EC~50~ for the effects of nicotine and clothianidin was 1.6 (CI= ) and 3.3 (CI = ) mM, respectively. Thiacloprid was the most potent with the EC~50~ of 721.2 $\mu$M (95 % CL= 502.4 μM to 1.0 mM) (Figure \@ref(fig:DR-body-bends-label)). @@ -381,6 +385,8 @@ bb_dat_plot_nic <- on_plate_stats %>% theme(axis.text = element_text(size=12), axis.title.x=element_blank(), axis.title = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), strip.text.x = element_text(size=12), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -401,6 +407,8 @@ bb_dat_plot_nit <- on_plate_stats %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -419,6 +427,8 @@ bb_dat_plot_thia <- on_plate_stats %>% theme(axis.text = element_text(size=12), axis.title.x=element_blank(), axis.title = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), strip.text.x = element_text(size=12), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -439,6 +449,8 @@ bb_dat_plot_clo <- on_plate_stats %>% theme(axis.text = element_text(size=12), axis.title.x=element_blank(), axis.title = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), strip.text.x = element_text(size=12), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -461,7 +473,7 @@ knitr::include_graphics("fig/results2/DR-body-bends.png") \newpage #### Effects on egg laying -On-plate experiments allow to assay for other aspects of *C. elegans* biology such as egg-laying (ref to general intro). The number of eggs laid per worm in the presence of nicotine and neonicotinoids over a period of 24 hours was counted and compared to the control (Figure \@ref(fig:EL-plot-label)) and \@ref(fig:egg-laying-lbl)). Both N2 wild-type and *bus-17* mutants lay ~ 95 egg/day/worm. No effects on wild-type worm of either compound was observed. However, egg-laying rate of *bus-17* mutant was reduced by low mM concentrations of thiacloprid and clothianidin. +On-plate experiments allow to assay for other aspects of *C. elegans* biology such as egg-laying (Section \@ref(gglayingbehaviour)). The number of eggs laid per worm in the presence of nicotine and neonicotinoids over a period of 24 hours was counted and compared to the control (Figure \@ref(fig:EL-plot-label)) and \@ref(fig:egg-laying-lbl)). Both N2 wild-type and *bus-17* mutants lay ~ 95 egg/day/worm. No effects on wild-type worm of either compound was observed. However, egg-laying rate of *bus-17* mutant was reduced by low mM concentrations of thiacloprid and clothianidin. (ref:EL-plot-capt) **The concentration-dependence for the effects of nicotine and neonicotinoids on egg-laying of *C. elegans*.** Wild type (left panel) and *bus-17* (right panel) worms were exposed for 24 hours to varying concentrations of nicotine, thiacloprid, clothianidin or drug vehicle (0), incorporated into solid medium. Number of eggs laid in 24 hours were counted and expressed as eggs laid per worm. Data are mean $\pm$ SEM collected from $\ge$ 8 individual on $\ge$ 2 days. One way Anova (Kruskal-Wallis test) with Dunnet’s Corrections, $*$ P $\le$ 0.05, $**$ P $\le$ 0.01, $***$ P $\le$ 0.001, $****$ P $\le$ 0.0001. @@ -486,6 +498,8 @@ el_dat_plot_nic <- on_plate_stats %>% theme(axis.text = element_text(size=12), axis.title.x=element_blank(), axis.title = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), strip.text.x = element_text(size=12), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -506,6 +520,8 @@ el_dat_plot_nit <- on_plate_stats %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -526,6 +542,8 @@ el_dat_plot_thia <- on_plate_stats %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -546,6 +564,8 @@ el_dat_plot_clo <- on_plate_stats %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -564,7 +584,7 @@ knitr::include_graphics("fig/results2/DR-egg-laying.png") \newpage #### Effects on egg hatching -Eggs laid on the plate hatch after 8 hours of exo-utero development (ref to general intro). To investigate the effects of nicotine and neonicotinoids on egg-hatching L4+1 worms were incubated with nicotine and neonicotinoids. After 24-hour incubation, they were removed from the experimental plate, leaving the progeny and eggs behind. After further 24 hours, the number of unchanged eggs and larvae present were counted to derive the % hatching rate. Almost 100 % of eggs laid by N2 and *bus-17* hatched (Figure \@ref(fig:EH-plot-label)). Neither compound had an effect on hatching of N2 worms (Figure \@ref(fig:EH-plot-label), left panel). However, thiacloprid at 1.5 mM and clothianidin at 2 mM reduced the proportion of hatched eggs of *bus-17* worms by 19 and 13 %, respectively (Figure \@ref(fig:EH-plot-label), right panel)). +Eggs laid on the plate hatch after 9 hours of exo-utero development (figure \@ref(fig:life-cycle-label). To investigate the effects of nicotine and neonicotinoids on egg-hatching L4+1 worms were incubated with nicotine and neonicotinoids. After 24-hour incubation, they were removed from the experimental plate, leaving the progeny and eggs behind. After further 24 hours, the number of unchanged eggs and larvae present were counted to derive the % hatching rate. Almost 100 % of eggs laid by N2 and *bus-17* hatched (Figure \@ref(fig:EH-plot-label)). Neither compound had an effect on hatching of N2 worms (Figure \@ref(fig:EH-plot-label), left panel). However, thiacloprid at 1.5 mM and clothianidin at 2 mM reduced the proportion of hatched eggs of *bus-17* worms by 19 and 13 %, respectively (Figure \@ref(fig:EH-plot-label), right panel)). (ref:EH-plot-capt) **The concentration-dependence for the effects of nicotine and neonicotinoids on *C. elegans* egg-hatching.** N2 wild-type (a) and *bus-17* mutant (b) worms laid eggs in the presence of varying concentrations of nicotine, thiacloprid, clothianidin or drug vehicle (0). After 24 hours adult worms were removed and eggs left behind. Number of unhatched eggs and larvae were counted 24 hours later. Data are mean $\pm$ SEM, of $\ge$ 2 paired experiments performed on $\ge$ days. One way Anova (Kruskal-Wallis test) with Dunn’s Corrections, $*$ P $\le$ 0.05, $**$ P $\le$ 0.01, $***$ P $\le$ 0.001, $****$ P $\le$ 0.0001. @@ -588,8 +608,11 @@ eh_dat_plot_nic <- on_plate_stats %>% ylab("% eggs hatched") + theme(axis.text = element_text(size=12), axis.title.x=element_blank(), + panel.grid.minor = element_blank(), + panel.background = element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -608,6 +631,8 @@ eh_dat_plot_nit <- on_plate_stats %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -627,6 +652,8 @@ eh_dat_plot_thia <- on_plate_stats %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -646,10 +673,12 @@ scale_fill_manual(values=c('#000000','#993300', '#996633','#CC9933', '#FFCC33',' axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) -eh_grid <- plot_grid(el_dat_plot_nic, el_dat_plot_nit, el_dat_plot_thia, el_dat_plot_clo, nrow = 4) +eh_grid <- plot_grid(eh_dat_plot_nic, eh_dat_plot_nit, eh_dat_plot_thia, eh_dat_plot_clo, nrow = 4) eh_grid = eh_grid + draw_label("Concentration [mM]", x = 0.4, y = 0, hjust = 0, vjust = 0) eh_grid ``` @@ -738,6 +767,8 @@ sel_dev_plot <- dev_t3 %>% axis.title.x=element_blank(), axis.title = element_text(size=12), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), text = element_text(size=12, family="sans")) @@ -756,7 +787,8 @@ Wild-type animals were exposed acutely to nicotine and neonicotinoids and their Despite common effects of nicotine and neonicotinoids on locomotion, the mode of action is likely to be different. Exposure of worms to nicotine for 4 hours led to significant reduction in the size of the worm. This is due to the proposed mode of action of nicotine. Nicotine activates ACR-16 nicotinic acetylcholine receptors present at the body wall muscle [@touroutine2005; @richmond1999], which leads to BWM hypercontraction [@sobkowiak2011]. BWM is physically attached to the cuticle [@altun2009], therefore prolonged muscle stiffness and hypercontraction lead to shrinkage of the cuticle [@petzold2011] and the reduction in the body size observed in this study. In contrast, neonicotinoids did not have the same effect. Thiacloprid and clothianidin treated worms showed uncoordinated, twitchy phenotype and no reduction in the body length. Taken together, this data suggest that nicotine and neonicotinoids act to inhibit locomotion differently. It is possible that they all act on nAChRs in the worm, as these molecules are the primary targets for nicotine and neonicotinoids in other species, but they are likely to act on different types of *C. elegans* nAChRs. To provide an insight into the mode of action of these compounds, studies on wild-type and nAChR mutant worms should be performed. Behavioral analysis of wild-type and mutant strains exposed to nicotine and neonicotinoids might allow for identification of strains resistant to these compounds and hence discover a potential molecular targets. ### Nicotine inhibition of thrashing -The time course for the effects of 10 and 25 mM nicotine on thrashing of wild-type worm revealed two “phases” of inhibition. First, seen after 10 minutes, followed by partial recovery and a second phase seen after 40 minutes. This could suggest nicotine targets multiple sites to alter thrashing. Previous research has shown that nicotine acts at a body wall muscle but also at sensory neurons. Nicotine is an agonist of TRP receptors [@feng2006] which are expressed in nociceptive ASH and ADL neurons [@colbert1997]. These neurons send out processes to the nerve ring where they make connections with a diversity of circuits, including those regulating movement [@rogers2006]. A nicotine-related compound quinine has an effect on locomotion via nociceptive circuit [@hilliard2004]. It is therefore possible that the first and rapid effect of nicotine on thrashing could be due to the action on sensory neurons. Sensory neurons have processes exposed to the external environment [@hall2008], which are easily accessible to nicotine. Indeed, nicotine at high doses inhibits locomotion within 1 minute of incubation (ref). In addition, this effect is equally rapid on wild-type and *bus-17* mutant worms. This suports the notion that nicotine affects locomotion by targeting structures exposed to the surface and not buried within the worm. + +The time course for the effects of 10 and 25 mM nicotine on thrashing of wild-type worm revealed two “phases” of inhibition. First, seen after 10 minutes, followed by partial recovery and a second phase seen after 40 minutes. This could suggest nicotine targets multiple sites to alter thrashing. Previous research has shown that nicotine acts at a body wall muscle but also at sensory neurons. Nicotine is an agonist of TRP receptors [@feng2006] which are expressed in nociceptive ASH and ADL neurons [@colbert1997]. These neurons send out processes to the nerve ring where they make connections with a diversity of circuits, including those regulating movement [@rogers2006]. A nicotine-related compound quinine has an effect on locomotion via nociceptive circuit [@hilliard2004]. It is therefore possible that the first and rapid effect of nicotine on thrashing could be due to the action on sensory neurons. Sensory neurons have processes exposed to the external environment [@hall2008], which are easily accessible to nicotine. Indeed, nicotine at high doses inhibits locomotion within 1 minute of incubation (Figure \@ref(fig: onset-plot-label)a). In addition, this effect is equally rapid on wild-type and *bus-17* mutant worms. This suports the notion that nicotine affects locomotion by targeting structures exposed to the surface and not buried within the worm. The second phase of inhibition could be due to the effects of nicotine on the body wall muscle. It may take longer to reach muscular targets because worms ingest little material whilst in liquid [@gomez-amaro2015] and so nicotine must cross the cuticle to reach body wall muscle. Complex structure and the thickness of the cuticle may slow the kinetics of absorption. This is supported by the lack of two phases of nicotine-induced paralysis in the leaky cuticle *bus-17* mutant. The effects of nicotine on thrashing of a mutant strain equilibrate after 10 minutes of incubation which may suggest improved permeability and hence reflect synergistic sensory and muscular effects of nicotine on locomotion. @@ -768,8 +800,11 @@ Permeability of drugs across lipidic structures is dependent on the physicochemi To investigate the role of surface coat and cuticle in drug permeability *bus-17* mutant with fragile and more permeable cuticle was employed in acute and moderate exposure assays. Exposure of *bus-17* worms increased potency of all compounds. For example, in acute-exposure, thrashing experiments, the EC~50~ for the effects of nicotine and nitenpyram increased by 8- and 5-fold, respectively. Moreover, thiacloprid and clothianidin had no effect on motility of the wild-type worm, but on *bus-17* they induced paralysis with the EC~50~ of 480 $\mu$M and 2.2 mM, respectively. Increased drug sensitivity was also observed in other cuticle-mutant strains for example *bus-8* [@partridge2008], *bus-5* and *bus-16* [@xiong2017]. This increased sensitivity is thought to be due to an increased cuticular permeability in mutant strains [@partridge2008; @xiong2017]. These data highlights the importance of the cuticle in protecting *C. elegans* against the outer environment. The cuticle is a common structural feature of all soil nematodes [@decraemer2003]. It is likely that it limits bioavailability of residual insecticides in all soil nematodes, hindering their potential toxic effects. #### Nicotine and thiacloprid have a neurodevelopmental effect on *C. elegans*. + Worms growing in the presence of 1 mM nicotine and thiacloprid developed into adults slower than the control worms. Neonicotinoids also disrupt larval development in bees [@souzarosa2016]. In would be interesting to investigate whether there is a common mechanism of neonicotinoid-induced neurodevelopmental defect in worms and bees. In worms, thiacloprid acts by disrupting L2/L3 transition. L2 stage is a stage at which multiple cell divisions and differentiation occurs [@hall2008]. Nicotinic acetylcholine receptors containing UNC-63 subunits seem to be involved in this process [@ruaud2006]. Developmental assays on *unc-63* and other nAChR mutants should be carried out to determine if the action of thiacloprid depends on this protein. +\newpage + ------------------------------------------------------ Behavioral Compound Strain EC~50~ assay diff --git a/04-results-02.Rmd b/04-results-02.Rmd index 3805dc70fa88d689fec461ab7135f60a71573c1c..6daee5f13c1bb671c4e2f420ca75d9c9337bdff9 100644 --- a/04-results-02.Rmd +++ b/04-results-02.Rmd @@ -4,34 +4,36 @@ Results from the previous results chapter show low susceptibility of *C. elegans* to neonicotinoids and that the cuticle is a limiting factor of the efficacy of these compounds on locomotion. This chapter aims to further characterise the concentration-dependent effects of neonicotinoids on worm and the role of the cuticle in their efficacy, by utilising the pharyngeal pumping assay. -The pharynx is responsible for feeding. It functions to capture the bacterial suspension, expel the fluid and trap bacteria inside the pharyngeal lumen. The bacteria is then smashed and passed to the gut for digestion. +The pharynx is responsible for feeding. It functions to capture the bacterial suspension, expel the fluid and trap bacteria inside the pharyngeal lumen [@song2012]. The bacteria is then smashed and passed to the gut for digestion [@avery1987]. -These complex pharyngeal functions are performed by two motions: pumping and peristalsis (Figure \@ref(fig:feeding-label) [@avery1989]. Pumping is the contraction and a subsequent relaxation of the corpus, anterior isthmus and the terminal bulb. Peristalsis is the motion of the posterior isthmus that pushes the bacteria to the terminal bulb for grinding. On average, peristalsis occurs per every 3.4 pumps [@song2013] and begins after the relaxation of the pharyngeal muscle. Grinding of the food particles is performed by the grinder. The grinder is positioned in the terminal bulb and composed of 3 pairs of muscle cells (ref). Contraction of these cells leads to their rotation, resulting in food maceration. +These complex pharyngeal functions are performed by two motions: pumping and peristalsis (Figure \@ref(fig:feeding-label) [@avery1989]. Pumping is the contraction and a subsequent relaxation of the corpus, anterior isthmus and the terminal bulb. Peristalsis is the motion of the posterior isthmus that pushes the bacteria to the terminal bulb for grinding. On average, peristalsis occurs per every 3.4 pumps [@song2013] and begins after the relaxation of the pharyngeal muscle. Grinding of the food particles is performed by the grinder. The grinder is positioned in the terminal bulb and composed of 3 pairs of muscle cells [@albertson1976]. Contraction of these cells leads to their rotation, resulting in food maceration. -```{r synapses-celegans-pharynx, echo=FALSE, warning=FALSE, message=FALSE} +\newpage -library(kableExtra) -library(dplyr) +(ref:feeding) **C. elegans* feeding.** As the corpus and anterior isthmus contract, bacterial suspension enters the pharynx through the mouth (top). Subsequent relaxation expels water out, trapping bacteria in the corpus-anterior isthmus lumen (middle). This pumping movement is synchronised with the terminal bulb contraction-relaxation cycle leading to movement of the grinder and crashing of food trapped between the muscle segments (not shown). This happens on average 3.4 times to allow food accumulation [@song2012] and passage to the intestine. The peristalsis of the posterior isthmus opens the isthmus-terminal bulb lumen and pushes the next portion of food in [@avery1987] for fragmentation (bottom). -innervation_pharynx_tbl <- data.frame( - Muscle = c("pm1", "pm2", "pm3", "pm4", "pm5", "pm6", "pm7", "pm8"), - Chemical = c("M1", "M1", "M1", "M2, M3, MC", "M2, M3, M4, I5", "M5 , M4?", "M5", " "), - Gap = c("", "", "", "MC via mc2", " ", "M5 via mc3", "M5 via mc3", "M5 via mc3")) +```{r feeding-label, fig.cap="(ref:feeding)", fig.scap='\\textit{C. elegans} feeding.', fig.align='center', echo=FALSE} +knitr::include_graphics("fig/results3/feeding.png") +``` -innervation_pharynx_tbl %>% -mutate_all(linebreak) %>% -kable("latex", booktabs = T, escape = F, - col.names = linebreak(c("Muscle cell", "Chemical synapse", "Gap junction")), - caption = "Connectivity of the pharyngeal neuromuscular system.") %>% - kable_styling(latex_options = "hold_position") +<!-- ```{r synapses-celegans-pharynx, echo=FALSE, warning=FALSE, message=FALSE} --> -``` +<!-- library(kableExtra) --> +<!-- library(dplyr) --> -(ref:feeding) ***C. elegans* feeding.** As the corpus and anterior isthmus contract, bacterial suspension enters the pharynx through the mouth (top). Subsequent relaxation expels water out, trapping bacteria in the corpus-anterior isthmus lumen (middle). This pumping movement is synchronised with the terminal bulb contraction-relaxation cycle leading to movement of the grinder and crashing of food trapped between the muscle segments (not shown). This happens on average 3.4 times to allow food accumulation [@song2012] and passage to the intestine. The peristalsis of the posterior isthmus opens the isthmus-terminal bulb lumen and pushes the next portion of food in [@avery1987] for fragmentation (bottom). +<!-- innervation_pharynx_tbl <- data.frame( --> +<!-- Muscle = c("pm1", "pm2", "pm3", "pm4", "pm5", "pm6", "pm7", "pm8"), --> +<!-- Chemical = c("M1", "M1", "M1", "M2, M3, MC", "M2, M3, M4, I5", "M5 , M4?", "M5", " "), --> +<!-- Gap = c("", "", "", "MC via mc2", " ", "M5 via mc3", "M5 via mc3", "M5 via mc3")) --> -```{r feeding-label, fig.cap="(ref:feeding)", fig.scap='\\textit{C. elegans} feeding.', fig.align='center', echo=FALSE} -knitr::include_graphics("fig/results3/feeding.png") -``` +<!-- innervation_pharynx_tbl %>% --> +<!-- mutate_all(linebreak) %>% --> +<!-- kable("latex", booktabs = T, escape = F, --> +<!-- col.names = linebreak(c("Muscle cell", "Chemical synapse", "Gap junction")), --> +<!-- caption = "Connectivity of the pharyngeal neuromuscular system.") %>% --> +<!-- kable_styling(latex_options = "hold_position") --> + +<!-- ``` --> ### Anatomy of the *C. elegans* pharynx @@ -46,24 +48,23 @@ There are 8 layers of muscle cells encapsulating the pharynx (pm1-pm8). pm1 is t There are nine marginal cells in the pharynx: mc1 - mc3 each with three fold symmetry. These cells run along the pharynx from the pm1 to pm8. They receive chemical synapses from M5 and form gap junctions with muscle cells. +\newpage + (ref:pharyngeal-muscle) **The musculature of the *C. elegans* pharynx.** Cartoon representation of the muscle cells constituting each of the three anatomical features: the corpus, isthmus and the terminal bulb (a) A single cell of each layer is pictured. Epiflueorescence image of pharyngeal muscle cells from the transgenic worm expressing myofilaments GFP reporter gene (b, left panel) and epifluorescence image of the transgenic worm expressing mitochondrial GFP reporter gene (b, right panel), to highlight the muscle cells of the terminal bulb. Images adapted from @albertson1976 (a) and @altun2009a (b). ```{r pharyngeal-muscle-label, fig.cap="(ref:pharyngeal-muscle)", fig.scap= "The musculature of the \\textit{C. elegans} pharynx.", fig.align='center', echo=FALSE} knitr::include_graphics("fig/general_intro/png/pharynx_muscle.png") ``` +\newpage + ### Sensory regulation of pumping There is a single point of connection between the pharyngeal and somatic system: a pair of gap junctions between the extrapharyngeal RIP and pharyngeal I1 neurons [@albertson1976]. Laser ablation of RIP has no effect on pumping rates on or off food [@dalliere2015]. This suggests that, the pharyngeal system is sufficient to drive pharyngeal responses. However, there is evidence the pharyngeal pumping can be influenced by the humoral transmission. The pharynx expresses receptors activated by neurotransmitters not synthesised by the pharynx, such as dopamine [@sugiura2005]. Mutation of genes not expressed in the pharynx has an effect on the pharyngeal response to food [@calahorro2018]. In addition, animals with abolished sensory neurons and not RIP neurons have blunted pharyngeal response to light touch [@riddle1997], light [@bhatla2015], familial food, [@song2013], or attractive and repellent odours [@li2012]. This evidence supports the sensory regulation of the pharyngeal activity. Numerous sensory cues associated with food are detected by the *C. elegans* to modulate pharyngeal pumping including odour [@li2012] and mechanical stimulation [@chalfie1985]. These cues are detected by the sensory neurons. There are 60 sensory neurons in *C. elegans*. There are also pharyngeal neurons which are likely to serve sensory function. This includes NSM and all I neurons with the exception of I4. -### Pharyngeal nervous system -There are 20 neurons in the pharynx [@albertson1976] and Table \@ref(tab:pharynx-neurons)). Laser ablation studies combined with behavioural analysis of generated worms provides an explanation of the role of the entire pharyngeal nervous system, and the role of individual neurons in the pharyngeal pumping. - -Pharyngeal nervous system is not essential for the function of the pharynx, but it is crucial for the regulation and modulation of the pharyngeal function in response to the environment. In the absence of food, wild-type worm pumps at a low rate. This increases markedly in the presence of food. The laser ablation of the pharyngeal nervous system does not abolish pumping entirely [@avery1989]. In the absence of food, wild-type worm makes 43 pumps per minute. This is reduced to 16 in worms lacking pharyngeal neurons. A stronger phenotype of neuron-ablated worms can be seen upon introduction of food. In the presence of food, pharyngeal pumping rate drops from 224 to 26 in laser ablated worms. In addition, there are abnormalities in the mechanism of pumping of worms lacking the pharyngeal nervous system: little food passes into the intestine resulting in retarded growth and compromised fertility [@avery1989; @avery1993] showing the essential role of the pharyngeal nervous system in the feeding response. - -Three out of 14 pharyngeal neuron types are sufficient to elicit feeding. These neurons are MC, M3 and M4. Laser ablation of MC neuron (MC^-^strain) leads to reduction of pumping rate by 75% on food and 37% off food. Therefore, MC is important in initiation of pumping [@avery1989; @raizen1995]. Laser ablation of M3 or M4 has little effect on the pumping rate [@raizen1995], but it effects the mechanism of pumping. M3^-^ animals have markedly extended latency of a single pump [@avery1993] suggesting M3 governs the timing of pumping. The sensory endings of M3 synapse onto the M4^-^ animals accumulate bacteria in the corpus suggesting M4 initiates peristalsis [@avery1989; @avery1993] by stimulating isthmus opening via mechanism that is not yet fully understood. +\newpage -```{r pharynx-neurons, echo=FALSE} +```{r pharynx-neurons, echo=FALSE, warning=FALSE} library(kableExtra) library(dplyr) pharyngeal_nrs <- data.frame( @@ -83,9 +84,16 @@ kable("latex", booktabs = T, escape = F, ``` -### Neurotransmitters of the pharynx +\newpage -Genetic studies of worm mutant strains provide evidence for a critical role of neurotransmission in the regulation of feeding. UNC-13 protein is involved in the regulation of neurotransmitter release at the synapse, as shown by the biochemical and behavioural analysis of the *unc-13 C. elegans* strain. Mutants deficient in UNC-13 show severe retention of vesicles in the pre-synapse [@richmond1999] and impaired synaptic transmission [@aravamudan1999]. Their feeding is also affected: 70 % reduction of the pharyngeal pumping rate was noted [@richmond2001]. These data highlight the key role of neurotransmitters in the regulation of pumping. The activity of the pharynx is influenced by acetylcholine, glutamate and 5-HT (Table \@ref(tab:pharynx-neurons) and Figure \@ref(fig:pharyngeal-nervous-system-label)), and potential tyramine and octopamine [@alkema2005]. +### Pharyngeal nervous system +There are 20 neurons in the pharynx [@albertson1976] and Table \@ref(tab:pharynx-neurons)). Laser ablation studies combined with behavioural analysis of generated worms provides an explanation of the role of the entire pharyngeal nervous system, and the role of individual neurons in the pharyngeal pumping. + +Pharyngeal nervous system is not essential for the function of the pharynx, but it is crucial for the regulation and modulation of the pharyngeal function in response to the environment. In the absence of food, wild-type worm pumps at a low rate. This increases markedly in the presence of food. The laser ablation of the pharyngeal nervous system does not abolish pumping entirely [@avery1989]. In the absence of food, wild-type worm makes 43 pumps per minute. This is reduced to 16 in worms lacking pharyngeal neurons. A stronger phenotype of neuron-ablated worms can be seen upon introduction of food. In the presence of food, pharyngeal pumping rate drops from 224 to 26 in laser ablated worms. In addition, there are abnormalities in the mechanism of pumping of worms lacking the pharyngeal nervous system: little food passes into the intestine resulting in retarded growth and compromised fertility [@avery1989; @avery1993] showing the essential role of the pharyngeal nervous system in the feeding response. + +Three out of 14 pharyngeal neuron types are sufficient to elicit feeding. These neurons are MC, M3 and M4. Laser ablation of MC neuron (MC^-^strain) leads to reduction of pumping rate by 75% on food and 37% off food. Therefore, MC is important in initiation of pumping [@avery1989; @raizen1995]. Laser ablation of M3 or M4 has little effect on the pumping rate [@raizen1995], but it effects the mechanism of pumping. M3^-^ animals have markedly extended latency of a single pump [@avery1993] suggesting M3 governs the timing of pumping. The sensory endings of M3 synapse onto the M4^-^ animals accumulate bacteria in the corpus suggesting M4 initiates peristalsis [@avery1989; @avery1993] by stimulating isthmus opening via mechanism that is not yet fully understood. + +\newpage (ref:pharyngeal-nervous-system) **Pharyngeal nervous system.** Simplified pharyngeal nervous system showing the major neurons, synaptic connection and neurotransmitters. Synapses between I1-RIP connect the extrapharyngeal and pharyngeal nervous system. @@ -93,11 +101,17 @@ Genetic studies of worm mutant strains provide evidence for a critical role of n knitr::include_graphics("fig/results3/pharyngeal_system_2.png") ``` +\newpage + +### Neurotransmitters of the pharynx + +Genetic studies of worm mutant strains provide evidence for a critical role of neurotransmission in the regulation of feeding. UNC-13 protein is involved in the regulation of neurotransmitter release at the synapse, as shown by the biochemical and behavioural analysis of the *unc-13 C. elegans* strain. Mutants deficient in UNC-13 show severe retention of vesicles in the pre-synapse [@richmond1999] and impaired synaptic transmission [@aravamudan1999]. Their feeding is also affected: 70 % reduction of the pharyngeal pumping rate was noted [@richmond2001]. These data highlight the key role of neurotransmitters in the regulation of pumping. The activity of the pharynx is influenced by acetylcholine, glutamate and 5-HT (Table \@ref(tab:pharynx-neurons) and Figure \@ref(fig:pharyngeal-nervous-system-label)), and potential tyramine and octopamine [@alkema2005]. + #### 5-HT 5-HT is synthesised in two pharyngeal neurons NSM and I5 [@chase2007]. Mutant deficient in enzyme in the 5-HT biosynthetic pathway has blunted response to food [@sze2000]. Exogenous application of 5-HT induces feeding response in the absence of food whereas competitive 5-HT antagonists inhibit pumping [@horvitz1982; @avery1990]. Collectively, this suggests that serotonergic neurotransmission induce food-evoked feeding response. -In the presence of food, 5-HT can be released from multiple sites, including NSM, ADF and HSN neurons. NSM are neurosecretory neurons in the pharyngeal nervous system. In the presence of food, they release 5-HT into the pseudocoelomic fluid [@horvitz1982] to inhibit locomotion, induce pumping and alter other behaviours [@horvitz1982]. ADF are chemosensory neurons present on the head of the worm. Release of 5-HT selectively from ADF neurons is sufficient to drive the feeding response [@cunningham2012]. Similarly, selective release of 5-HT from extrapharyngeal HSN neurons when NSM and ADF neurotransmission is defective, results in potent pumping response [@lee2017]. Therefore, there are 3 possible routes by which elevated levels of 5-HT in the presence of food can be achieved. It is possible that these routes co-function or operate at different conditions. +In the presence of food, 5-HT can be released from multiple sites, including NSM, ADF and HSN neurons. NSM are neurosecretory neurons in the pharyngeal nervous system. In the presence of food, they release 5-HT into the pseudocoelomic fluid [@horvitz1982] to inhibit locomotion, induce pumping and alter other behaviours [@horvitz1982]. ADF are chemosensory neurons present on the head of the worm. Release of 5-HT selectively from ADF neurons is sufficient to drive the feeding response [@cunningham2012]. Similarly, selective release of 5-HT from extrapharyngeal HSN neurons when NSM and ADF neurotransmission is defective, results in potent pumping response [@lee2017]. Therefore, there are 3 possible routes by which elevated levels of 5-HT in the presence of food can be achieved. It is possible that these routes co-function or operate at different conditions. Detection of food leads to the elevation of pumping rate via 5-HT acting at multiple G-protein coupled receptors [@avery2012]. 5-HT can regulate feeding response by binding to neuronal SER-4 receptors and SER-1 receptors expressed both in the pharyngeal muscle cells and neurons [@tsalik2003]. It also binds to SER-5 receptors expressed on extrapharyngeal interneurons [@cunningham2012]. However, the main driver of the 5-HT driven pharyngeal response it the activation of SER-7 receptors expressed on cholinergic MC and M4 neurons and and on glutametergic M3 neurons [@hobson2003; @song2013]. Acetylcholine released from MC and M4 neurons increases contraction frequency and induce isthmus peristalsis, respectively [@avery1987; @raizen1994]. This leads to an increase in the activity of the pharynx to ~260 pumps/min. Glutamate released from M3 shortens pump duration to <200ms. @@ -126,22 +140,17 @@ Genetic and pharmacological studies suggest that acetylcholine stimulates pharyn The effects of known nAChR agonists and antagonists were evaluated in pharyngeal assays [@raizen1995]. Application of acetylcholine and nicotine resulted in contraction of the pharyngeal muscle in the absence of food. In the presence of food, pharyngeal pumping was inhibited by antagonist d-tubacurarine. #### Acetylcholine-sensitive receptors in the pharynx ####{#nachrinpharynx} +Although there are at least 29 nAChRs expressed in *C. elegans* (Figure \@ref(fig:seqidentityecd-label)), only one, namely EAT-2 has been identified as essential in mediation of the feeding response [@mckay2004]. EAT-2 is expressed in pm4 and pm5 muscle cells [@mckay2004], which make synaptic connections with the MC [@albertson1976]. *C. elegans eat-2* mutant shows significantly reduced pumping in the presence of food [@raizen1995; @mckay2004]. Similar phenotype was noted in *eat-18* mutants. EAT-18 however is not a nAChR subunit. Instead, it is predicted to be a single transmembrane protein. Based on the localisation and behavioural phenotype, EAT-18 and EAT-2 are believed to co-assembly to form a functional receptor [@mckay2004]. -Although there are at least 29 nAChRs expressed in *C. elegans* (Table \@ref(tab:celegans-nachrs)), only one, namely EAT-2 has been identified as essential in mediation of the feeding response [@mckay2004]. EAT-2 is expressed in pm4 and pm5 muscle cells [@mckay2004], which make synaptic connections with the MC [@albertson1976]. *C. elegans eat-2* mutant shows significantly reduced pumping in the presence of food [@raizen1995; @mckay2004]. Similar phenotype was noted in *eat-18* mutants. EAT-18 however is not a nAChR subunit. Instead, it is predicted to be a single transmembrane protein. Based on the localisation and behavioural phenotype, EAT-18 and EAT-2 are believed to co-assembly to form a functional receptor [@mckay2004]. - -ACR-7 is also expressed at the pharyngeal muscle [@saur2013]. *C. elegans* mutant deficient in ACR-7 pumps normally in the presence of food [@saur2013], suggesting this subunits is not involved in mediation of feeding. +ACR-7 is also expressed at the pharyngeal muscle [@saur2013], as shown with the reporter construct, however its function in pharyngeal pumping is unclear as *acr-7 C. elegans* mutant pumps normally in the presence of food [@saur2013]. -nAChR are likely to be expressed not only at the neuromuscular junction, as suggested by the EAT-18 expression pattern. Expression of GFP-tagged eat-18 gene under the native promoter leads to fluorescence in all types of pharyngeal muscle cells and in M5 neuron [@mckay2004]. The identity of other subunits remains to be elucidated. +<!-- nAChR are likely to be expressed not only at the neuromuscular junction, as suggested by the EAT-18 expression pattern. Expression of GFP-tagged eat-18 gene under the native promoter leads to fluorescence in all types of pharyngeal muscle cells and in M5 neuron [@mckay2004]. The identity of other subunits remains to be elucidated. --> -nAChRs are not the only acetylcholine - sensitive receptors in the pharynx. +Bsides nAChRs, there are other acetylcholine - sensitive receptors in the pharynx. GAR-3 is a ACh-sensitive GPCR receptor [@hwang1999] expressed in metacorpus, isthmus, terminal bulb of the pharyngeal muscle and in the I3 pharyngeal neuron [@steger2004]. Its role may involve regulation of the membrane electrical potential [@steger2004] and control of feeding during starvation [@you2006]. -Acetylcholine-gated chloride channels (ACC) are ionotropic channels and like nAChRs, members of Cys-loop receptor family. There are at least 8 members isoforms: ACC-1 to ACC-4, LGC-46 to LGC-49 [@takayanagi-kiya2016], which form homo- and hetero-pentamers [@putrenko2005]. - -The expression pattern of these proteins in *C. elegans* was investigated using reported construct [@pereira2015; @takayanagi-kiya2016]. They are generally expressed in a distinct subset of cholinergic and glutametergic neurons (including acc-1 in pharyngeal M1 and M3). Interestingly, acc-4 is expressed in almost all cholinergic neurons. Sequence analysis and electrophysiological data suggest ACC channels are inhibitory but they may be playing multiple functions. Acc-4 may be acting as autoinhibitory, as most neurons predicted to express acc-4 do not receive direct synaptic input from other neurons [@albertson1976]. LGC-49 are expressed in presynaptic specialisations of cholinergic motor neurons where they regulate synaptic vesicle release [@takayanagi-kiya2016]. - -Based on pharmacologically characterised ACC-1 and ACC-2 in vivo, ACC receptors are also pharmacologically distinct from other ACh receptors. Some of the nAChR and GPCR receptor compounds were potent at modulating the activity of ACC channels, but not others. For example, ACC channels are insensitive to nAChR compounds nicotine, cytisine and antagonist $\alpha$-bgtx but are sensitivity to tubocurarine. This mixed pharmacological profile suggest ligand binding site is distinct from the binding site of nAChRs and cholinergic GPCRs. +Acetylcholine-gated chloride channels (ACC) are ionotropic channels and like nAChRs, members of Cys-loop receptor family. There are at least 8 members isoforms: ACC-1 to ACC-4, LGC-46 to LGC-49 [@takayanagi-kiya2016], which form homo- and hetero-pentamers [@putrenko2005]. The expression pattern of these proteins in *C. elegans* was investigated using reported construct [@pereira2015; @takayanagi-kiya2016]. They are generally expressed in a distinct subset of cholinergic and glutametergic neurons (including acc-1 in pharyngeal M1 and M3). Interestingly, acc-4 is expressed in almost all cholinergic neurons. Sequence analysis and electrophysiological data suggest ACC channels are inhibitory but they may be playing multiple functions. Acc-4 may be acting as autoinhibitory, as most neurons predicted to express acc-4 do not receive direct synaptic input from other neurons [@albertson1976]. LGC-49 are expressed in presynaptic specialisations of cholinergic motor neurons where they regulate synaptic vesicle release [@takayanagi-kiya2016].Based on pharmacologically characterised ACC-1 and ACC-2 in vivo, ACC receptors are also pharmacologically distinct from other ACh receptors. Some of the nAChR and GPCR receptor compounds were potent at modulating the activity of ACC channels, but not others. For example, ACC channels are insensitive to nAChR compounds nicotine, cytisine and antagonist $\alpha$-bgtx but are sensitivity to tubocurarine. This mixed pharmacological profile suggest ligand binding site is distinct from the binding site of nAChRs and cholinergic GPCRs. ### Assays for scoring the effects of compounds on pharyngeal pumping @@ -173,7 +182,7 @@ library(magick) Pharyngeal pumping is a feeding behaviour of the intact worm mediated by the pharynx. In the presence of food, the pharynx pumps at an approximate rate of 4 pumps/s (4Hz) to ingest food particles Figure \@ref(fig:pump-on-food-plot-label). A typical way of assessing the effects of compounds on feeding is to place *C. elegans* on agar plate soaked with drug solution and laced with OP50 food patch. A drug present on the plate comes in direct contact with foraging worm, but also can enters the worm via ingestion and/or diffusion cross the cuticle. To assess the effects of nicotine and neonicotinoids, wild-type worms were exposed to nicotine, nitenpyram, thiacloprid and clothianidin for 24-hours before scoring their effects on pharyngeal pumping (Figure \@ref(fig:pump-on-food-plot-label) left panel)). Nicotine at concentrations $\ge$ 1 mM inhibited pumping in a dose - dependent manner. Nitenpyram and thiacloprid at 1 mM as well as clothianidin at 3.75 mM had no effect. -Analysis of responses to compounds in *bus-17* mutants show that the worm's cuticle can hinder the efficacy of drugs. To determine whether the cuticle affects the efficacy of nicotine and neonicotinoids on the feeding behaviour, pharyngeal pumping experiments were repeated on the *bus-17*, cuticle-disrupted mutant of *C. elegans* (Figure \@ref(fig:pump-on-food-plot-label) right panel)). As in the wild-type, the pharyngeal pumping of the *bus-17* mutant was inhibited by nicotine at 1 and 10mM, whereas nitenpyram had no effect. In contrast, the dose of thiacloprid and clothianidin ineffective on wild-type, inhibited pumping of the mutant at low mM concentrations. +Analysis of responses to compounds in *bus-17* mutants show that the worm's cuticle can hinder the efficacy of drugs (Chapter 3). To determine whether the cuticle affects the efficacy of nicotine and neonicotinoids on the feeding behaviour, pharyngeal pumping experiments were repeated on the *bus-17*, cuticle-disrupted mutant of *C. elegans* (Figure \@ref(fig:pump-on-food-plot-label) right panel)). As in the wild-type, the pharyngeal pumping of the *bus-17* mutant was inhibited by nicotine at 1 and 10mM, whereas nitenpyram had no effect. In contrast, the dose of thiacloprid and clothianidin ineffective on wild-type, inhibited pumping of the mutant at low mM concentrations. To compare the efficacy of compounds on wild-type versus mutant strain, dose-response curves for the effects of treatment on pharyngeal pumping were generated (Figure \@ref(fig:dr-pumping-on-food-label)). Almost a fold difference in the potency of nicotine was observed. The EC~50~ on wild-type worm was 4.3 mM. This decreased to 2.3 mM in a mutant strain. Nicotine was also the most efficacious out of all compounds tested at inhibiting pumping. The estimated EC~50~ of thiacloprid and clothianidin on a mutant strain were 2.6 and 6.2 mM, respectively. Since they had no effect on wild-type it is not possible to estimate the fold-potency change between the wild-type and mutant strain. @@ -242,6 +251,8 @@ pump_on_food_plot_nic <- on_plate_pump_stats %>% ylab("Pumping (Hz)") + theme(axis.text = element_text(size=12), axis.title.x=element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), strip.text.x = element_text(size=12), axis.title = element_text(size=12), text = element_text(size=12, family="sans")) @@ -260,6 +271,8 @@ scale_fill_manual(values=c('#000000','#339900')) + ylab("Pumping (Hz)") + theme(axis.text = element_text(size=12), axis.title.x=element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), strip.text.x = element_text(size=12), text = element_text(size=12, family="sans")) @@ -279,6 +292,8 @@ pump_on_food_plot_thia <- on_plate_pump_stats %>% theme(axis.text = element_text(size=12), axis.title.x=element_blank(), strip.text.x = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), text = element_text(size=12, family="sans")) @@ -296,6 +311,8 @@ pump_on_food_plot_clo <- on_plate_pump_stats %>% ylab("Pumping (Hz)") + theme(axis.text = element_text(size=12), axis.title.x=element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), strip.text.x = element_text(size=12), plot.margin = unit(c(5.5,5.5,12,5.5), "pt"), @@ -318,6 +335,8 @@ knitr::include_graphics("fig/results3/DR-pumping_on_food.png") During the course of the investigation, it was noted that high concentrations of nicotine had an antimicrobial effect on *C. elegans* food source - the OP50 *E. coli*. This raised a concern that the observed effects of nicotine on feeding could be partially due to the effects of this compound on the density of bacteria. To circumvent this issue, an alternative assay was developed in which the need for bacteria is removed. This alternative assay is performed in liquid, in the presence of 10 mM 5-HT. 5-HT has dual effect: it makes the worms immobile and stimulates their pumping (Figure \@ref(fig:5HT-pumping-label) a). After 5 minute incubation with 10 mM 5-HT, 45 % of worms were paralysed. This increased to 65 % after 1 hour of incubation. The paralysing effect of 5-HT enabled measurements of the pharyngeal pumping activity of worms. Whilst in liquid, worms display negligible food intake [@gomez-amaro2015]. 10 mM 5-HT stimulated pumping to 4 Hz - an effect seen after 5-minute exposure and sustained for 1 hour (Figure \@ref(fig:5HT-pumping-label) b). +\newpage + (ref:10mM-5HT-pumping-in-liquid) **The effects of 5-HT on *C. elegans* behaviour in liquid.** Worms were exposed to 10mM 5-HT or vehicle control (0). The effects on locomotion over time was scored by counting the number of immobile worms pre- (time point zero) and post-exposure to treatment or vehicle control. Data are expressed as % of worms paralysed (a). Additionally, the effects of 5-HT on pumping of immobile worms was scored. The measurements were made immediately after addition of 5-HT or vehicle control (time point 0) and post-exposure at indicated time points. Pumping was scored by visual observation by counting the number of pumps over the period of 30 seconds and expressed in Hz. Data are mean $\pm$ SEM of 3 independent repeats. Motility of 10 worms per condition was scored during each experiment. ```{r 5HT-pumping-label, echo=FALSE, fig.cap="(ref:10mM-5HT-pumping-in-liquid)", fig.scap = "The effects of 5-HT on\\textit{C. elegans} behaviour in liquid.", fig.align='center', message=FALSE, echo=FALSE, warning=FALSE} @@ -335,13 +354,15 @@ ht_paralysis_plot <- ht_paralysis_transf %>% se = sd/sqrt(length(paralysed))) %>% ggplot(aes(Time, mean_paralysed, colour = Dose)) + scale_color_manual(values=c("grey","black"))+ - geom_line() + - geom_point() + + geom_line(size=1) + + geom_point(size=1) + geom_errorbar(aes(ymin = mean_paralysed-se, ymax = mean_paralysed+se)) + theme(legend.position="none") + xlab("Time (mins)") + ylab("% paralysed") + - theme(text=element_text(size=12, family="sans")) + theme(panel.background = element_blank(), + axis.line = element_line(colour = "black"), + text=element_text(size=12, family="sans")) ht_pump_in_liq$Pump <- ht_pump_in_liq$Pump/60 ht_pump_liq_stats <- ht_pump_in_liq %>% @@ -353,13 +374,15 @@ ht_pump_liq_stats <- ht_pump_in_liq %>% n()) ht_pump_liq_plot <- ht_pump_liq_stats %>% ggplot(aes(Time, mean_pump)) + - geom_line() + - geom_point() + + geom_line(size=1) + + geom_point(size=1) + geom_errorbar(aes(ymin = mean_pump-se, ymax = mean_pump+se)) + xlab("Time (mins)") + ylab("Pumping (Hz)") + ylim(0,5) + - theme(text=element_text(size=12, family="sans")) + theme(panel.background = element_blank(), + axis.line = element_line(colour = "black"), + text=element_text(size=12, family="sans")) #+ guides(col = guide_legend(title = "Dose [mM]")) plot_grid(ht_paralysis_plot, ht_pump_liq_plot) ``` @@ -370,6 +393,9 @@ To score the effects of compounds on 5-HT induced pumping, wild-type worms were Incubation of *bus-17* mutant resulted in a decrease of EC~50~ of nicotine from 1.7 to 3.6 mM. A greater shift in potency of nitenpyram was noted. The EC~50~ increased from 72.9 in wild-type to 41.2 mM in a mutant strain. Estimated EC~50~ of thiacloprid was 4 mM whereas clothianidin at 2.5 mM did not significantly alter pumping. +\newpage + + (ref:pumping-liquid) **The effects of nicotine and neonicotinoids on 5-HT stimulated pharyngeal pumping.** Pharyngeal pumping was stimulated by incubation of worms in 10 mM 5-HT for 30 minutes. Following, indicated concentrations of nicotine, nitenpyram, thiacloprid or clothianidin were added. The effect of nicotine and neonicotinoids on 5-HT induced pumping on N2 wild-type (left panel) and *bus-17* (right panel) was scored. Pharyngeal pumping was measured by visual observation for a period of 30 seconds and expressed in Hz. Data are mean $\pm$ SEM of 3-17 individual worms collected on $\ge$ 2 separate days. One way Anova (Kruskal-Wallis test) with Sidak Corrections, $*$P $\le$ 0.05, $**$P $\le$ 0.01, $***$P $\le$ 0.001, $****$P $\le$ 0.0001. ```{r pumpining-liquid-label, fig.cap="(ref:pumping-liquid)", fig.scap = "The effects of nicotine and neonicotinoids on 5-HT stimulated pharyngeal pumping.",fig.align='center', fig.asp=1.2, echo=FALSE, message=FALSE, warning=FALSE} @@ -413,6 +439,8 @@ pump_liq__plot_nic <- pump_liq_stats %>% ylab("Pumping (Hz)") + theme(axis.title.x = element_blank()) + theme(axis.text = element_text(size=12), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), strip.text.x = element_text(size=12), text = element_text(size=12, family="sans")) @@ -432,6 +460,8 @@ scale_fill_manual(values=c('#000000','#003300', '#006600','#009900', '#00FF33', ylab("Pumping (Hz)") + theme(axis.text = element_text(size=12), axis.title.x = element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), strip.text.x = element_text(size=12), text = element_text(size=12, family="sans")) @@ -451,6 +481,8 @@ scale_fill_manual(values=c('#000000','#000066')) + ylab("Pumping (Hz)") + theme(axis.text = element_text(size=12), axis.title.x=element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), strip.text.x = element_text(size=12), text = element_text(size=12, family="sans")) @@ -468,6 +500,8 @@ scale_fill_manual(values=c('#000000','#993300')) + ylab("Pumping (Hz)") + theme(axis.text = element_text(size=12), axis.title.x=element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), strip.text.x = element_text(size=12), text = element_text(size=12, family="sans"), @@ -534,7 +568,6 @@ knitr::include_graphics("fig/results3/cuthead-5ht-combined.png") \newpage - To examine the effects of nicotine and neonicotinoids on pharyngeal pumping, cut heads were placed in 1 $\mu$M 5-HT for 10 minutes. 1 $\mu$M concentration was chosen because it elicits maximal pharyngeal response, whereas 10 minutes is sufficient for the response to equilibrate. Following 5-HT incubation, cut heads were transferred to a dish containing 1 $\mu$M 5-HT and an indicated concentration of nicotine, nitenpyram, thiacloprid or clothianidin and the effects of nicotine or neonicotinoids on 5-HT induced pumping was measured at multiple time point over 50 minutes. To determine if the response was reversible, cut heads were then transferred to 1 $\mu$M 5-HT and recovery scored over the period of 15 minutes (Figure \@ref(fig:N2-antagonist-timecourse-label)). Nicotine at concentration ranging from 1 - 20 $\mu$M inhibited 5-HT induced pumping partially, whereas 100 $\mu$M incubation resulted in a complete seasure of pumping activity (Figure \@ref(fig:N2-antagonist-timecourse-label) a). The maximal effects were typically observed after 10 minutes of incubation. For some concentrations i.e. 10, 20 and 50 $\mu$M, these effects weakened with time. Generally, the inhibitory effects of nicotine were reversible. Cut heads recovered from treatment with nicotine concentrations ranging from 1 - 50 $\mu$M after 15 minutes of washing. Cut heads previously incubated with 100 $\mu$M nicotine, pumped at half a rate of the control. @@ -794,6 +827,8 @@ geom_errorbar(aes(ymin=mean_pumping-se, ymax=mean_pumping+se, width = 0.4)) + ylab("Pumping (HZ)") + ylim(0, 5) + theme(axis.title.x = element_blank(), + panel.background = element_blank(), + axis.line = element_line(colour = "black"), axis.title = element_text(size=12), axis.text = element_text(size=12)) mutant_pumping_plot @@ -858,7 +893,6 @@ knitr::include_graphics("fig/results3/cuthead_DR_eat2.png") In this chapter, the effects of nicotine and neonicotinoids on pharyngeal pumping of intact and dissected, cut-head *C. elegans* are described. Pharyngeal pumping was assayed by visually scoring the frequency of pharyngeal pumps. These investigations were carried out to further investigate the toxicity of nicotine and neonicotinoids on worms, and to explore the role of worm's cuticle in drug susceptibility. ## 5-HT induces fast pumping in *C.elegans* by the activation of EAT-2 containing nAChRs - Application of 5-HT on cut-head preparation elevated pumping from 0.17 Hz to 3.34 Hz with the EC~50~ of 169 nM (Table \@ref(tab:pharynx-summary)).These data suggest that 5-HT drives a feeding response in worms. The maximum pumping frequency achieved by the exhogenous 5-HT is comparable to the pharyngeal pumping rate of the worm in the presence of food (3.34 Hz and 4.33 Hz, respectively). Pumping rate on food of a mutant with defective 5-HT biosynthesis pathway is markedly reduced [@sze2000]. Endogenous 5-HT is released from NSM and ADF neurons in response to the presence of food. It then acts on MC and M4 neurons [@raizen1995; @niacaris2003] to increase pumping frequency and on M3 neurons [@song2013; @niacaris2003] to reduce the pumping latency. Application of 5-HT bypasses the sensory pathway to activate MC, M4 and M3 neurons directly by acting on GPCRs [@hobson2003; @song2013]. To provide an insight into the mechanism of 5-HT induced *C. elegans* responses, the effects of 5-HT on pharyngeal pumping of cut head *eat-2* nAChR mutant were performed and compared to the wild-type. The maximum response achieved by a 5-HT was reduced by 70 %, whereas the EC~50~ increased from 169 nM in wild-type to 150 $\mu$M in a mutant (Table \@ref(tab:pharynx-summary)). This relative 5-HT insensitivity of *eat-2* strain suggests 5-HT induces pumping by eliciting cholinergic neurotranmission via EAT-2 containing nAChRs. 5-HT acts on cholinergic MC and M4 motorneurons to stimulate ACh release. ACh binds to EAT-2 nAChRs expressed at the MC NMJ to stimulate pumping [@mckay2004]. Hence 5-HT evokes pharyngeal activity by indirectly activating EAT-2 containing nAChRs. diff --git a/05-results-03.Rmd b/05-results-03.Rmd index 44312715b23f05a4f07c7b1f0a5f51779961f5c4..966bae2dc459262e54a3e56eb542b4d3b816bd75 100644 --- a/05-results-03.Rmd +++ b/05-results-03.Rmd @@ -2,8 +2,7 @@ ## Introduction -Previous chapter describes the effects of nicotine, 5-HT and neonicotinoids on pharyngeal pumping of the cut-head worm, scored by visual observation. An alternative pharyngeal assay is an extracellular recording of an electrical function of the pharynx, or electropharyngeogram (EPG). Unlike scoring pharyngeal pumping by visual observation, EPG recordings allow for resolution of early time points. Additionally, investigations into drug-induced changes of the EPG waveform may inform on the potential mode of action of compounds. - +Previous chapter describes the effects of nicotine, 5-HT and neonicotinoids on pharyngeal pumping of the cut-head worm, scored by visual observation (Chapter 4). An alternative pharyngeal assay is an extracellular recording of an electrical function of the pharynx, or electropharyngeogram (EPG). Unlike scoring pharyngeal pumping by visual observation, EPG recordings allow for resolution of early time points. Additionally, investigations into drug-induced changes of the EPG waveform may inform on the potential mode of action of compounds. In an EPG assay, a worm's head is placed in a recording chamber. The chamber can be perfused, exposing the pharynx to different drug solutions. A tight seal between the electrode and the tip of the *C. elegans* nose is made. Contracting pharyngeal muscle produces currents which flows out of the worm's mouth; this is detected by the electrode. Each cycle of contraction and relaxation gives rise to a single waveform on the trace, known as an EPG. There are several phases constituting an individual EPG (Figure \@ref(fig:example-epg-label)). The beginning of the EPG signal marks excitatory phase. This phase mirrors depolarisation and contraction of the corpus and the terminal bulb and constitutes from 2 spikes. e spike arises due to the release of ACh from MC neurons and an activation of of nAChRs [@raizen1995]. E peak is due to a subsequent calcium channels activation [@lee1997; @shtonda2005]. e is often unseen on the EPG trace due to merging with the larger E. I or inhibitory spikes are diverse in number and amplitude and arise as a result of the inhibitory currents. These currents are produced by ligand-gated chloride channels in response to glutamate release from M3 neurons [@dent1997; @li1997]. Lastly, R and r reflect relaxation of the corpus and the terminal bulb, due to a repolarisation of the terminal bulb muscle cells caused by the flow of potassium through the potassium ion channel [@shtonda2005]. r spikes are frequently merged with larger in amplitude R. @@ -233,6 +232,8 @@ Comparing the effects of nicotine on the pharynx as revealed by EPG and visual s knitr::include_graphics("fig/results3/nic-epg-trace-long-exposure-comb.png") ``` +\newpage + ### Effects of cytisine The effects of cytisine, an agonist of nAChR was tested. Cytisine was applied at concentrations ranging from 1 to 100 $\mu$M. As in case of acetylcholine and nicotine, two types of responses were observed. Moderate but sustained stimulation of the pharyngeal activity was elicited by 5 $\mu$M, whereas at concentrations $\ge$ 10 $\mu$M, the pharynx was stimulated and subsequently inhibited (Figure \@ref(fig:cyt-epg-label)). The EC~50~ of cytisine on EPG was 3 $\mu$M (Figure \@ref(fig:cyt-epg-graph-label)). @@ -269,6 +270,8 @@ knitr::include_graphics("fig/results3/cyt-traces.png") knitr::include_graphics("fig/results3/epg-cyt.png") ``` +\newpage + ### Effects of neonicotinoids The effects of neonicotinoids on EPG were also examined. Pharynges were exposed to 100 $\mu$M nitenpyram, 50 $\mu$M thiacloprid and 75 $\mu$M clothianidin. Neither nitenpyram (Figure \@ref(fig:Nit-EPG-label)), nor thiacloprid had an effect on the frequency of pharyngeal activity (Figure \@ref(fig:epg-thia-label)). In contract, clothianidin stimulated pharyngeal activity. The frequency increased from 0.6 to 1.1 Hz and returned to basal following 5 minute wash (Figure \@ref(fig:clo-epg-label)). EPGs from clothianidin-perfused pharynges were examined and a reduction of R peak in relation to E peak was noted. Clothianidin significantly increased the E/R ratio from 1.3 to 1.8 (Figure \@ref(fig:clo-er-ratio-label) a and b). 5-minute wash did not reverse this effect. A change in duration of pumping activity was also observed. The latency of EPG decreased from 130 ms to 110 ms when pharynges exposed to clothianidin (Figure \@ref(fig:clo-er-ratio-label) a and c). This effect was not reversed upon 5 minute wash. @@ -470,7 +473,7 @@ Table: (\#tab:pharynx-summary2) Summary of the effects of compounds on the phary +--------------+--------------------------------+-----------------------------------+ | | Pump frequency | EPG waveform | +==============+================================+===================================+ -|5-HT |1. Dose-dependent, sustained | 1. Reduced pump duration | +|5-HT |1. Dose-dependent, sustained | 1. Reduced pump duration | | |stimulation | | | |2. EC~50~=255$\mu$ | | +--------------+--------------------------------+-----------------------------------+ diff --git a/06-results-04.Rmd b/06-results-04.Rmd index 2de2727e3835c6b3ea1a2210d6eb19b87fb84639..f80a4fac04c47dbf09888b2ebeec2f7588f2fc2a 100644 --- a/06-results-04.Rmd +++ b/06-results-04.Rmd @@ -34,7 +34,7 @@ One of the most studies nAChR subunit is the vertebrate homomeric $\alpha7$. Het #### Rapidly desensitising -Acetylcholine and nicotine are classical nAChR agonists that activate vertebrate $\alpha7$ and many other nAChR types. In addition, there are selective compounds that bind to $\alpha7$ receptors, such as cytisine and choline (cross-ref general intro). The rank order of potency of these agonists is: cytisine > nicotine > ACh > choline (EC50 values in the general introduction, cross-ref). The EC50 values vary depending on the method of measure and the subunit origin [@papke2002], however nicotine is generally at least 5 times more potent than ACh [@couturier1990], whereas the potency of choline is at least 10 times lower than that of ACh [@papke2002]. The EC50 of the most potent compound cytisine is between 5.6 and 7.1 $\mu$M [@wonnacott2007]. +Acetylcholine and nicotine are classical nAChR agonists that activate vertebrate $\alpha7$ and many other nAChR types. In addition, there are selective compounds that bind to $\alpha7$ receptors, such as cytisine and choline. The rank order of potency of these agonists is: cytisine > nicotine > ACh > choline [@papke2000]. The EC50 values vary depending on the method of measure and the subunit origin [@papke2002], however nicotine is generally at least 5 times more potent than ACh [@couturier1990], whereas the potency of choline is at least 10 times lower than that of ACh [@papke2002]. The EC50 of the most potent compound cytisine is between 5.6 and 7.1 $\mu$M [@wonnacott2007]. The kinetics of agonist-evoked nAChR responses are reminiscent to those of other nAChR types. Briefly, in the presence of agonist, receptor channels open rapidly allowing flux of ions, which gradually declines [@corrie2011] until a full depolarisation and desentisation occurs. Extremely rapid desensitising kinetics is the unique feature of the $\alpha7$ receptor. @@ -96,17 +96,21 @@ Taken together, *Xenopus oocytes* and eukaryotic cell lines can be used as an he Heterologous expression of receptor channels requires appropriate cellular environment to enable receptor maturation and functioning at the cell surface. Expression of nAChRs is a complex process during which individual subunits come together, assemble into correctly folded pentamer and are transported to the plasma membrane where they function. *C.elegans* expresses many proteins involved in these processes. -Identification and heterologous expression of *C. elegans* nAChRs greatly contributed to the understanding of proteins involved in the biogenesis of these ion channels. There are two nAChRs expressed at the NMJ of the body wall muscle. ACR-16 homopentamic receptor and heteropentameric receptor composed of UNC-29, UNC-38, UNC-63, LEV-1 and LEV-8. These receptors are classified based on pharmacology into nicotine- and levamisole- sensitive and named N-type and L-type, respectiely. DEG-3/DES-2 nAChRs are the neuronal receptors [@treinin1998], whereas EAT-2 containing nAChRs are expressed in the pharyngeal muscle [@mckay2004]. +Identification and heterologous expression of *C. elegans* nAChRs greatly contributed to the understanding of proteins involved in the biogenesis of these ion channels. There are two nAChRs expressed at the NMJ of the body wall muscle. ACR-16 homopentamic receptor and heteropentameric receptor composed of UNC-29, UNC-38, UNC-63, LEV-1 and LEV-8. These receptors are classified based on pharmacology into nicotine- and levamisole- sensitive and named N-type and L-type, respectively. DEG-3/DES-2 nAChRs are the neuronal receptors [@treinin1998], whereas EAT-2 containing nAChRs are expressed in the pharyngeal muscle [@mckay2004]. <!-- *C. elegans* is a powerfull tool in which the function and pharmacological properties of proteins can be studied by a combination of genetic, behavioural and cellular approaches (Section \@ref(genmanip) \@ref(analytical_behaviour)). --> #### RIC-3 ####{#ric-3celegans} -RIC-3 is an an ubiquitously expressed in *C. elegans*, as shown by the fluorescence in most (if not all) neurons, pharyngeal and body wall muscle in RIC-3::GFP transgenic worms [@halevi2002]. The predicted topology of *C. elegans* RIC-3 is 2 transmembrane domains and 3 coiled-coils. *C. elegans ric-3* mutant has impaired locomotory behaviour, it is resistant to levamisole [@miller1996] and has impaired responses of nAChs, as measured by electrophysiological recording from the body wall muscle [@halevi2002]. *C. elegans ric-3* mutant has impaired cholinergic nerurotransmission, as shown by the lack of the cholinergic component of the EPG recording resulting in significantly retarded pharyngeal pumping and starved apperance [@halevi2002]. +RIC-3 (resistant to inhibitors of cholinesterase-3) is an evolutionary conserved, ER-residing [@roncarati2006; @alexander2010] transmembrane protein [@wang2009]. In *C. elegans*, it is ubiquitously expressed, as shown by the fluorescence in most (if not all) neurons, pharyngeal and body wall muscle in RIC-3::GFP transgenic worms [@halevi2002]. The predicted topology of *C. elegans* RIC-3 is 2 transmembrane domains and 3 coiled-coils. *C. elegans ric-3* mutant has impaired locomotory behaviour, it is resistant to levamisole [@miller1996] and has impaired responses of nAChs, as measured by electrophysiological recording from the body wall muscle [@halevi2002]. *C. elegans ric-3* mutant has impaired cholinergic nerurotransmission, as shown by the lack of the cholinergic component of the EPG recording resulting in significantly retarded pharyngeal pumping and starved apperance [@halevi2002]. -Heterologous expression of *C. elegans* nAChR in Xenopus oocytes provides evidence for their function in receptor maturation. Choline-evoked currents of neuronal DEG-3/DES-2 recepotors increased by 5-fold upon RIC-3 co-expression [@halevi2002]. *C. elegans* RIC-3 can also promote maturation of mammalian $\alpha-7$ channels. RIC-3 co-expression improved $\alpha-7$ function in *Xenopus oocytes* as shown by enhanced choline- and acetylcholine-evoked currents and cell-surface binding of radiolabelled $\alpha$-Bgtx [@lansdell2005; @williams2005]. RIC-3 also enabled the expression of $\alpha-7$ in otherwise non-permissive insect cell lines [@lansdell2008]. It not only promotes the heterologous cell-surface expression of mammalian, but it also increases the expression of insect chimera nAChRs [@lansdell2012]. +Heterologous expression of *C. elegans* nAChR in Xenopus oocytes provides evidence for their function in receptor maturation. Choline-evoked currents of neuronal DEG-3/DES-2 receptors increased by 5-fold upon RIC-3 co-expression [@halevi2002]. -Successful heterologous expression of L-type *C. elegans* receptor in Xenopus oocytes upon co-expression of RIC-3 and two other proteins, revealed other components important in the process of maturation of nAChRs [@boulin2008]. +This was markedly markedly improved when acr-16 was co-expressed with RIC-3 [@ballivet1996]. The role of RIC-3 in the maturation of this receptor type was also demonstrated in-vivo. The nicotine induced current at the body wall muscle was markedly reduced in ric-3 mutant, in comparison to the wild-type [@halevi2002]. + +*C. elegans* RIC-3 can also promote maturation of mammalian $\alpha-7$ channels. RIC-3 co-expression improved $\alpha-7$ function in *Xenopus oocytes* as shown by enhanced choline- and acetylcholine-evoked currents and cell-surface binding of radiolabelled $\alpha$-Bgtx [@lansdell2005; @williams2005]. RIC-3 also enabled the expression of $\alpha-7$ in otherwise non-permissive insect cell lines [@lansdell2008]. It not only promotes the heterologous cell-surface expression of mammalian, but it also increases the expression of insect chimera nAChRs [@lansdell2012]. + +Successful heterologous expression of L-type *C. elegans* receptor in Xenopus oocytes upon co-expression of RIC-3 and two other proteins, viz. UNC-50 and UNC-74, revealed other components important in the process of maturation of nAChRs [@boulin2008]. #### UNC-50 ####{#unc50} @@ -118,7 +122,7 @@ UNC-74 is closely related to the human TMX3 protein which is thought to be ER-as #### EAT-18 ####{#eat18} -EAT-18 is thought to be required for the function of pharyngeal nAChRs. It consists of a single transmembrane and an extracellular domain. Transgenic worms expressing EAT-18::GFP fusion protein reveal fluorescence in the pharynx with the strongest signal in the muscle, but also in the pharyngeal neuron M5 and unidentified 5 to 6 extrapharyngeal neurons [@mckay2004]. *eat-18* mutants are deficient in pumping and resistant to high concentraton of nicotine, supporting the function of EAT-18 in cholinergic neurotransmission of the pharynx [@raizen1995]. The association of *eat-18* with pharyngeal nAChR was indicated by comparison of the staining in the wild-type and *eat-18* mutant strains. Injection into the pseudocoelom of radiolabelled $\alpha$-bgtx resulted in straining of the pharynx. This was however abolished in the mutant strain [@mckay2004]. In addition, the expression of EAT-2 in *eat-2* was normal, suggesting EAT-18 is not involved in the trafficing of this receptor. It has been proposed that EAT-18 co-assembles with EAT-2 due to their common pharyngeal phenotypes in muntant strains and common cellular localisation in the pharyngeal muscle [@mckay2004]. Recently, successful expression of eat-2 co-assembled with eat-18 shown in Xenopus oocytes (personal comunication). +EAT-18 is thought to be required for the function of pharyngeal nAChRs. It consists of a single transmembrane and an extracellular domain. Transgenic worms expressing EAT-18::GFP fusion protein reveal fluorescence in the pharynx with the strongest signal in the muscle, but also in the pharyngeal neuron M5 and unidentified 5 to 6 extrapharyngeal neurons [@mckay2004]. *eat-18* mutants are deficient in pumping and resistant to high concentraton of nicotine, supporting the function of EAT-18 in cholinergic neurotransmission of the pharynx [@raizen1995]. The association of *eat-18* with pharyngeal nAChR was indicated by comparison of the staining in the wild-type and *eat-18* mutant strains. Injection into the pseudocoelom of radiolabelled $\alpha$-bgtx resulted in straining of the pharynx. This was however abolished in the mutant strain [@mckay2004]. In addition, the expression of EAT-2 in *eat-2* was normal, suggesting EAT-18 is not involved in the trafficing of this receptor. It has been proposed that EAT-18 co-assembles with EAT-2 due to their common pharyngeal phenotypes in mutant strains and common cellular localisation in the pharyngeal muscle [@mckay2004]. Recently, successful expression of eat-2 co-assembled with eat-18 shown in Xenopus oocytes (personal communication). ### Biochemical methods to assess expression of the transgene in *C. elegans* @@ -166,9 +170,9 @@ $\alpha$-Bgtx is used to demonstrate cell surface expression, because it binds t #### *Eat-2* is a suitable genetic background for functional expression -Heterologous proteins expression can have several effects on worm's behaviour (Section \@ref(hetexpeffectsofphysiology)). Pharyngeal pumping, is a measure of the feeding behaviour of the worm, and can be easily quantified in whole organisms or cellular assays. Thus, the activity of the pharynx can be used a platform to investigate the performance and the drug sensitivity of this organ in the wild-type, mutant and transgenic lines. +Many of worm's behaviours are underpinned by the cholinergic neurotransmission (Section \@ref(cholinergicneurotransmissioninworms)). Pharyngeal pumping is a measure of the feeding behaviour of the worm, regulated by acetylcholine. It can be easily quantified in whole organisms or cellular assays. Thus, the activity of the pharynx can be used a platform to investigate the performance and sensitivity of this organ to cholinergic drugs in the wild-type and in strains deficient in cholinergic transmission. -The activity of the pharynx is regulated by acetylcholine, thus this organ can be also suitable for the expression of nAChRs. Acetylcholine acting on EAT-2 containing nAChRs in the pharynx is a main driver of fast pumping (Chapter 3 and @mckay2004). EAT-2 is expressed in pm4 and pm5 muscle cells [@mckay2004], which make synaptic connections with the MC [@albertson1976]. The feeding response is markedly hindered in *eat-2 C. elegans* mutant [@raizen1995; @mckay2004]. Thus, selective expression of nAChRs in the pharyngeal muscle of *eat-2 C. elegans* mutant at the MC synapse should be a suitable platform for functional expression. +The activity of the pharynx is regulated by acetylcholine, thus this organ can be also suitable for the heterologous expression of nAChRs. Acetylcholine acting on EAT-2 containing nAChRs in the pharynx is a main driver of fast pumping (Chapter 3 and @mckay2004). EAT-2 is expressed in pm4 and pm5 muscle cells [@mckay2004], which make synaptic connections with the MC [@albertson1976]. The feeding response is markedly hindered in *eat-2 C. elegans* mutant [@raizen1995; @mckay2004]. Thus, selective expression of nAChRs in the pharyngeal muscle of *eat-2 C. elegans* mutant at the MC synapse should be a suitable platform for functional expression. <!-- *C. elegans* pharynx is an attractive platform for investigation of drug sensitivity due to the availbailabiloty of assays scoring the pharyngeal function and the genetic knowledge of the pharyngeal muscle function. --> @@ -381,7 +385,7 @@ knitr::include_graphics("fig/results4/PNG/rescuechrna7_feeding_2.png") ``` -#### Effects of 5-HT on pharyngeal pumping ####{#5htandtransgenicalpha7} +#### Effects of 5-HT on pharyngeal pumping ####{#htandtransgenicalpha7} The effects of 5-HT on the pharyngeal pumping of wild-type, *eat-* mutant, transgenic and transgenic control worms expressing human receptor was assayed. (Figure \@ref(fig:human-transgenic-rescue-label)). Cut-heads were bathed in 1 $\mu$M 5-HT. 30 minutes later, the effects on pharyngeal pumping were scored. @@ -407,7 +411,7 @@ ggplot(aes(x=Strain, y=mean_pumping)) + ### Pharmacological characterisation of $\alpha$ 7 expressing worms ####{#pharmaalpha7transegnicworms} -The experiments utilizing the pharyngeal pump phenotype on food and in the presence of 5-HT suggest lack of functionality of introduced receptor. However, the experiments that we used may not be sensitive enough to be able to detect functional expression of the $\alpha7$ receptors. Thus, we extended the analysis to investigate the pharmacological sensitivity with the aim of determining if the transgenic lines heterologously expressing $\alpha7$ exhibit known $\alpha7$ pharmacology (Cross ref to intro). +The experiments utilizing the pharyngeal pump phenotype on food and in the presence of 5-HT suggest lack of functionality of introduced receptor. However, the experiments that we used may not be sensitive enough to be able to detect functional expression of the $\alpha7$ receptors. Thus, we extended the analysis to investigate the pharmacological sensitivity with the aim of determining if the transgenic lines heterologously expressing $\alpha7$ exhibit known $\alpha7$ pharmacology. To asses whether the introduction of receptor into the pharynx of wild-type worms imposes $\alpha7$ pharmacology on the pharyngeal system, a series of pharyngeal assays were performed. nAChR agonists were tested to determine if there is a differential sensitivity between the N2 wild-type and transgenic worms. Compounds tested were acetylcholine, nicotine, choline and cytisine. @@ -611,14 +615,14 @@ knitr::include_graphics("fig/results4/PNG/cytisine_cuthead_2.png") <!-- axis.text = element_text(size=12), --> <!-- axis.text.x=element_text(angle=90)) --> <!-- plot12 --> -<!-- ``` --> +<!-- ``` #### $\alpha$-Bgtx staining ####{#bgtxstaining} The work above utilized 3 distinct functional criteria to address the possible expression. Based on phenotypic rescue of the pharmacological sensitivity, there is little indication that the mammalian $\alpha7$ is expressed. However, the cytisine effects hint at change in sensitivity of the system. To better determine if the introduced human receptor is expressed in *C. elegans*, staining of pharynxes with FITC-$\alpha$-Bgtx was carried out. $\alpha$-Bgtx is a high affinity toxin that acts as a selective antagonist of human $\alpha7$ nAChRs and it binds to the extracellular domain of this receptor. $\alpha$-Bgtx conjugated with a fluorescent reagent can be utilized to histologically define expression and resolve sub-cellur localisation of $\alpha7$ receptor in mammalian tissue and *C. elegans* [@barnard1971, @jensen2012]. This technique has been used to shown that $\alpha$-Bgtx binds to receptors at the body wall muscle [@jensen2012] and to the nAChR axillary subunit EAT-18 in the pharynx [@mckay2004]. -<!-- However, it has little antagonistsic effect on the body wall receptors [@boulin2008, @abongwa2016] and on the pharyngeal receptors (preliminary data not shown). --> + However, it has little antagonistsic effect on the body wall receptors [@boulin2008, @abongwa2016] and on the pharyngeal receptors (preliminary data not shown). --> To determine if FITC-$\alpha$-bgtx binds to native nAChRs, an isolated pharynx was used (Section \@ref(fitcmethod) and Figure \@ref(fig:exposed-pharynx-label)). In this preparation, there is no cuticular barrier, therefore, $\alpha$-Bgtx should access to the extracellular nAChR binding sites in the cell membrane of the pharyngeal muscle. Pharynxes were incubated with $\alpha$-Bgtx for 1 hour before being washed to remove unbound toxin. @@ -681,14 +685,13 @@ Overall the intrinsic sensitivity of the pharynx to nAChR agonists confounds thi The lack of significant behavioural and pharmacological differential between the transgenic and control strains suggests lack of functionality of these receptors in the *C. elegans* pharynx, or the inability to resolve the functional human receptor. To independently assess whether $\alpha7$ is expressed, staining of isolated pharynxes with conjugated $\alpha7$ nAChR selective antagonist FITC-$\alpha$-bgtx was carried out. -The lack of intense staining in the wild-type suggest that pharynx does not endogenously express $\alpha7$-Bgtx sensitivity. This is in contrast with the body wall muscle where ACR-16 is readily detected by $\alpha$-bgtx [@jensen2012]. This reinforces the distinct nature of pharyngeal cholinergic receptors. In contrast, the robust detection of $\alpha$-Bgtx-binding in excised transgenic heads was observed. $\alpha$-Bgtx can bind to partially assembled receptors. X-ray crystal structure of human $\alpha1$ shows $\alpha$-Bgtx binding to the extracellular domain of a single subunit, suggesting, a fully assembled receptor is not necessary for the binding of this antagonist [@dellisanti2007]. This may suggest that the expressed $\alpha7$ subunits are monomeric. However, nAChR assembly is strictly regulated in the cell (ref to general intro). Incorrectly assembled receptors are degraded or accumulate in the cytoplasm (ref) and are not expressed on the cell surface. In this study, there was no detergent permeabilization, thus, the robust $\alpha$-Bgtx staining is likely concentrated to extracellular cell surface. This favours the idea that staining is to the cell surface homopentamers. +The lack of intense staining in the wild-type suggest that pharynx does not endogenously express $\alpha7$-Bgtx sensitivity. This is in contrast with the body wall muscle where ACR-16 is readily detected by $\alpha$-bgtx [@jensen2012]. This reinforces the distinct nature of pharyngeal cholinergic receptors. In contrast, the robust detection of $\alpha$-Bgtx-binding in excised transgenic heads was observed. $\alpha$-Bgtx can bind to partially assembled receptors. X-ray crystal structure of human $\alpha1$ shows $\alpha$-Bgtx binding to the extracellular domain of a single subunit, suggesting, a fully assembled receptor is not necessary for the binding of this antagonist [@dellisanti2007]. This may suggest that the expressed $\alpha7$ subunits are monomeric. However, nAChR assembly is strictly regulated in the cell [@crespi2018]. Incorrectly assembled receptors are degraded [@brodsky1999] or accumulate inside the cell [@han2000. In this study, there was no detergent permeabilization, thus, the robust $\alpha$-Bgtx staining is likely concentrated to extracellular cell surface. This favours the idea that staining is to the cell surface homopentamers. -The $\alpha7$ bgtx staining is consistently localised to pm7 and pm8 muscle cells. The receptor expression is driven by the myo-2 promoter, which should result in protein production in all muscle cells of the pharynx, however selectivity has been observed previously (Anna Crisford, personal communication). In the endogenous system, EAT-2 functions at pm4, suggesting eat-2 promoter should be used to avoid restriction of endogenous promoter expression. +The $\alpha$-bgtx staining of $\alpha7$ receptors is consistently localised to pm7 and pm8 muscle cells, and inconsistently in other muscle cells of the pharynx. The receptor expression is driven by the myo-2 promoter, which should result in protein production in all muscle cells of the pharynx [@altun2009a], however selectivity has been observed previously (Anna Crisford, personal communication). In the endogenous system, EAT-2 functions at pm4, suggesting eat-2 promoter should be used to avoid restriction of endogenous promoter expression. -<!-- ### --> <!-- Bgtx-staining and pharyngeal pumping in the presence of cytisine experiments hint at the successful expression and function of endogenous receptor in *C. elegans*. However, it is also possible that $\alpha7$ is expressed in the muscle, but not functional. --> -<!-- <!-- Another chaperon in Nacho which is a NACHO - a TM neuronal ER protein important in receptor folding, assembly, maturation and surface expression - [@gu2016] - (read! Brain a 7 Nicotinic Acetylcholine Receptor Assembly Requires NACHO) --> --> +<!-- <!-- Another chaperon in Nacho which is a NACHO - a TM neuronal ER protein important in receptor folding, assembly, maturation and surface expression - [@gu2016] - (read! Brain a 7 Nicotinic Acetylcholine Receptor Assembly Requires NACHO) --> <!-- <!-- Another possibility is that $\alpha$ 7 interacts with native nAChR subunits to form non-functional complexes [@millar2007]. Indeed, in human cell lines, heterologous expression of recombinant forms of heterometic $\alpha$ 7/$\beta$ 2 was noted, whereas in a native environment $\alpha$ 7 forms homopentameric channels. --> diff --git a/19-discussion.Rmd b/19-discussion.Rmd index 8fe21a9c629bdce6d9c6b91c59ead8933a737375..2d1e026df2bb3c7f3911b0491c4ed69d23654fff 100644 --- a/19-discussion.Rmd +++ b/19-discussion.Rmd @@ -3,13 +3,15 @@ ## Environmental levels of neonicotinoids do not impact on the behavior or development of C. elegans -Increased use of insecticides requires a better understanding of their environmental impact. Therefore, the initial aim of this project was to investigate the effects of neonicotinoid-insecticides on the Nematoda representative *C. elegans*. Neonicotinoids have been introduced to the marked in the 1990s and since have become the most commonly used insecticides worldwide [@jeschke2011]. They have many advantages, including a high potency against wide range pest insects (Section \@ref(potentpests)) and low mammal toxicity. However, neonicotinoids can negatively impair on non-target species. The adverse effects of environmental neonicotinoids on bees have been studied for decades (Section \@ref(sublethalbees)), whereas the effects on other ecologically important species is less understood. +Increased use of insecticides requires a better understanding of their environmental impact. Therefore, the initial aim of this project was to investigate the effects of neonicotinoid-insecticides on the Nematoda representative *C. elegans*. Neonicotinoids have been introduced to the marked in the 1990s and since have become the most commonly used insecticides worldwide [@jeschke2011]. They have many advantages, including a high potency against wide range pest insects (Section \@ref(potentpests)) and low mammalian toxicity. However, neonicotinoids can have significant field effects on non-target species. The adverse effects of environmental neonicotinoids on bees have been studied for decades (Section \@ref(sublethalbees)), whereas the effects on other ecologically important species is less understood but unlikely to have a problem. There are several forms in which neonicotinoids are delivered onto fields including spray and granules, but seed-coating is the most common method [@jeschke2011]. This focused application ensures the presence of drug inside the plant at effective concentrations [@stamm2016], nevertheless neonicotinoids have long half-life and a leeching potential, therefore can reside in soil for prolonged time periods, coming in contact with inhabiting organisms. This leads to potential exposure to soil namatodes and earth worms, two important cultivars of the biomass and nutrient cyclers, that contribute to the soil fertility [@ingham1985; @neher2001]. The lethal dose of neonicotinoids on earths worms and nematodes varies between 2.74 and 62.08 $\mu$M (Table \@ref(tab:toxallanimal)), however neonicotinoids at lower doses can induce sublethal effects (Section \@ref(sublethalsoilworm)). The investigations into their effects on the nematode representative and model organism *C. elegans* were carried using thiacloprid, clothianidin and nitenpyram. -The effects of these three compounds on locomotion in liquid and solid media, egg-laying and egg-hatching of wild-type worm were investigated (Chapter 3 and 4). This study reports low potency of neonicotinoids against wild-type *C. elegans* [@kudelska2017]. When tested against locomotion in liquid, nitenpyram had an inhibitory effect at mM concentrations and the estimated EC50 of 195.8 mM. Thiacloprid and clothianidin had no effect at concentrations up to 1 and 2.5 nM, respectively (Section \@ref(effectsofneonicsonthrashing)). When on solid medium, the locomotion was inhibited by thiacloprid with the estimated EC50 of 3.7 mM but not by nitenpyram at 1 mM or clothianidin at 3.75 mM (Section \@ref(bodybendsneonics)). The low potency of neonicotinoids on intact *C. elegans* is consistent with the literature (Section \@ref(chapter3effectsofneonics)). +The effects of these three compounds on locomotion in liquid and solid media, egg-laying and egg-hatching of wild-type worm were investigated (Chapter 3 and 4). This study reports low potency of neonicotinoids against wild-type *C. elegans* [@kudelska2017]. Neonicotinoids were either not effective, or effective at mM concentrations. -Neonicotinoids had no effects on locomotion, reproduction or feeding, but it is possible that they affect more intricate aspects of worm’s physiology. They impact on learning and plasticity in honeybees [@williamson2013], therefore efforts into determining their effects on the ability to perceive and process information could be made. For example, decision making could be tested in food leaving [@shtonda2006] or chemotaxis assays [@law2004]. +These data suggests that neonicotinoids have minimal, if any, effect on locomotion, reproduction or feeding of *C. elegans*, however it is possible that they affect more intricate aspects of worm’s physiology. They impact on learning and plasticity in honeybees [@williamson2013], therefore efforts into determining their effects on the ability to perceive and process information could be made. For example, decision making could be tested in food leaving [@shtonda2006] or chemotaxis assays [@law2004]. + +<!-- When tested against locomotion in liquid, nitenpyram had an inhibitory effect at mM concentrations and the estimated EC50 of 195.8 mM. Thiacloprid and clothianidin had no effect at concentrations up to 1 and 2.5 nM, respectively (Section \@ref(effectsofneonicsonthrashing)). When on solid medium, the locomotion was inhibited by thiacloprid with the estimated EC50 of 3.7 mM but not by nitenpyram at 1 mM or clothianidin at 3.75 mM (Section \@ref(bodybendsneonics)). The low potency of neonicotinoids on intact *C. elegans* is consistent with the literature (Section \@ref(chapter3effectsofneonics)). --> <!-- It would also be beneficial to perform long-term exposure assay to determine whether neonicotinoids bio-accumulate in worm’s adipose tissue, or are metabolised to toxic chemical species [@suchail2001]. However, experiemnts in which Lastly, these compounds can act on multiple targets and exert effects at a very low and high doses [@pisa2015], therefore it would be beneficial to determine if *C. elegans* exposure to low doses (high nM - low $\mu$M) have an impact on its behavior. --> @@ -18,15 +20,15 @@ Exposure of *C. elegans* mutant with increased cuticle permeability [@xiong2017] The cuticle encapsulates the body of nematodes as well as earthworms. Their structures have several similarities, as revealed by the electron microscopy of redworm *L. terrestris*, greenworm *Allolobophora chlorotica* [@reed1948; @coggeshall1966; @knapp1971] and *C. elegans* preparations [@cox1981]. The main components of the cuticle are the collagen fibrils embedded within the matrix. This relatively thick layer is covered by a much thinner epicuticle, which consists mainly of lipids. In earthworms, the epicuticle is perforated by a coat of outward projections, shorter ellipsoidal bodies and longer microvilli. In *C. elegans* the surface coat consists of the glycoprotein-mesh. Based on the architectural and chemical similarities, it is likely that the cuticle of earthworms may also play a role in drug permeability. This is however poorly investigated. <!-- [@carter2014]. --> -Generally, the concentrations at which neonicotinoids impair on *C. elegans* behaviour are several folds higher than those found in the field [@sanchez-bayo2016] and concentrations effective against insect [@goulson2013]. These data suggests *C. elegans* is not impacted by neonicotinoids in the field. +Generally, the concentrations at which neonicotinoids impair on *C. elegans* behaviour are several folds higher than those found in the field [@sanchez-bayo2016] and concentrations effective against insect [@goulson2013]. These data suggests *C. elegans* is not impacted by neonicotinoids in the field, however no field-studies are available to confirm this. -The sensitivity of *C. elegans* differs from that of parasitic nematodes and earth worms. In *C. elegans* neonicotinoids impact on locomotion at low mM concentrations (Figure \@ref(fig:thrashing-tc-comp-label) and Figure \@ref(fig:BB-plot-label)), but have no effects on reproduction (Figure \@ref(fig:EL-plot-label) and Figure \@ref(EH-plot-label)). In plant parasitic nematode, neonicotinoids are effective at $\mu$M concentrations. The LD50 of thiacloprid is 143.23 $\mu$M [@dong2014], whereas the IC50 from the egg-hatching experiments is 300 $\mu$M [@dong2014; @dong2017]. Earthworms seem to be the most susceptible, with reported toxic lethal doses greater or equal to 2.74 $\mu$M (Table \@ref(tab:toxallanimal)) and doses effective against their reproduction and mobility at 488.85 nM, or higher (Section \@ref(ublethalsoilworm)). Thus, there is a differential neonicotinoid-susceptibility between *C. elegans* and parasitic nematodes and between *C. elegans* and earth worm species. The same is true among the insects, where some species are much more susceptible than others (Section \@ref(toxallanimal)). Therefore, the sensitivity of each species to neonicotinoids should be considered separately when evaluating the environmental impact of these insecticides. This highlights the complexity and difficulty of the neonicotinoids risk characterisation and usage management. +The sensitivity of *C. elegans* to neonicotinoids differs from that of parasitic nematodes and earth worms. In *C. elegans* neonicotinoids impact on locomotion at low mM concentrations (Figure \@ref(fig:thrashing-tc-comp-label) and \@ref(fig:BB-plot-label)), but have no effects on reproduction (Figure \@ref(fig:EL-plot-label) and \@ref(fig:EH-plot-label)). In plant parasitic nematode, neonicotinoids are effective at $\mu$M concentrations. The LD50 of thiacloprid on the root-knot nematode *M. incognita* is 143.23 $\mu$M [@dong2014], whereas the IC50 from the egg-hatching experiments is 300 $\mu$M [@dong2014; @dong2017]. Earthworms seem to be the most susceptible, with reported toxic lethal doses greater or equal to 2.74 $\mu$M (Table \@ref(tab:toxallanimal)) and doses effective against their reproduction and mobility at 488.85 nM, or higher (Section \@ref(sublethalsoilworm)). Thus, there is a differential neonicotinoid-susceptibility between *C. elegans* and parasitic nematodes and between *C. elegans* and earth worm species. The same is true among the insects, where some species are much more susceptible than others (Section \@ref(tab:toxallanimal)). Therefore, the sensitivity of each species to neonicotinoids should be considered separately when evaluating the environmental impact of these insecticides. This highlights the complexity and difficulty of the neonicotinoids risk characterisation and usage management. ## *C. elegans* as a model to study the mode of action of neonicotinoids -The adverse effect of neonicotinoids on biological pollinators and the emerging resistance opposes a threat to the food safety and highlights the need for the synthesis of novel and more selective insecticides. One of the first steps towards the synthesis of new insecticides is the understanding of their mode of action [@metcalf1971]. Neonicotinoids act by targeting insect nAChRs (Section \@ref(neonicstarget)), however their mode of action and receptor specificity differs. They can have agonistic, antagonistic and super-agonistic action, depending on the animal preparation upon which they are applied (Section \@ref(moaneonicsinsects)). In addition, even neonicotinoids sharing the same pharmacophore, target distinct receptors [@thany2009; @moffat2016]. Difficulties in the heterologous expression of insects' receptors hiders their pharmacological characterisation and description of neonicotinoid-receptor specificity (Section \@ref(ric3insect)). +The adverse effect of neonicotinoids on biological pollinators and the emerging resistance (Section \@ref(resgenevidence)) opposes a threat to the food safety and highlights the need for the synthesis of novel and more selective insecticides. One of the first steps towards the synthesis of new insecticides is the understanding of their mode of action [@metcalf1971]. Neonicotinoids act by targeting insect nAChRs (Section \@ref(neonicstarget)), however their mode of action and receptor specificity differs. They can have agonistic, antagonistic and super-agonistic action, depending on the animal preparation upon which they are applied (Section \@ref(moaneonicsinsects)). In addition, even neonicotinoids sharing the same pharmacophore, target distinct receptors [@thany2009; @moffat2016]. Difficulties in the heterologous expression of insects' receptors hiders their pharmacological characterisation and description of neonicotinoid-receptor specificity (Section \@ref(ric3insect)). -Model organism *C. elegans* is an alternative system in which the mode of action of chemical agents can be studied in-vivo [@lewis1987; @lewis1980]. *C. elegans* expresses at least 29 nAChR subunits (Table \@ref(tab:celegans-nachrs)) [@jones2007a] which form receptors at the neuromuscular junction and in the nervous system. Muscle-type receptors are involved in the regulation of locomotion, reproduction and feeding (Section \@ref(pharmacelegans) \@ref(nachrutantfeeding)). Neuronal type receptors are expressed in circuits involved in the sensory processing and chemosensation [@yassin2001]. The suitability of the *C. elegans* system for the mode of action studies was investigated by scoring the sensitivity of native pharyngeal nAChRs receptors to neonicotinoids. +Model organism *C. elegans* is an alternative system in which the mode of action of chemical agents can be studied in-vivo [@lewis1987; @lewis1980]. *C. elegans* expresses at least 29 nAChR subunits (Figure \@ref(fig:seqidentityecd-label)) [@jones2007a] which form receptors at the neuromuscular junction and in the nervous system. Muscle-type receptors are involved in the regulation of locomotion, reproduction and feeding (Section \@ref(pharmacelegans) \@ref(nachrutantfeeding)). Neuronal type receptors are expressed in circuits involved in the sensory processing and chemosensation [@yassin2001]. The suitability of the *C. elegans* system for the mode of action studies was investigated by scoring the sensitivity of native pharyngeal nAChRs receptors to neonicotinoids. Pharynx is a neuromuscular system in which feeding is carried out by a musculature under the influence of the pharyngeal nervous system. In the presence of food, 5-HT is released, which stimulates MC neuron. MC releases acetylcholine which acts directly on EAT-2 containing nAChRs to drive fast pumping. Thus, EAT-2 is a molecular determinant of the fast pharyngeal response. Although EAT-2 is the only nAChR subunit with clearly characterised function, ACR-7 is also expressed in the pharyngeal muscle [@saur2013]. @@ -62,9 +64,11 @@ Low sensitivity of *C. elegans* to nitenpyram, clothianidin and thiacloprid in b Cell lines and Xenopus oocytes are routinely used as biological systems for heterologous nAChR expression (Section \@ref(biologicalsystemfornachrexpression)). Model organism *C. elegans* is an alternative system in which recombinant proteins can be expressed by generation of transgenic worms [@crisford2011; @sloan2015]. In comparison to other systems, *C. elegans* is cheap and easy to maintain, whereas transgenic worms can be preserved for years at - 80 °C. The function of recombinant nAChRs can be studied in-vivo by evaluating their impact on behaviours underpinned by the cholinergic neurotransmission. -Acetylcholine is a major neurotransmitter of the pharynx, released by at least 7 out of 14 neurons (Table \@ref(pharynx-neurons)). It is key and necessary for the induction of fast feeding in response to food (Section \@ref(achpumping)). Its action on the pharynx is mediated by nAChRs, most notably EAT-2 expressed at the NMJ (Section \@ref(nachrinpharynx)). *C. elegans* pharynx does not posses an innate susceptibility to low concentrations of neonicotinoids, creating an appropriate genetic background in which effects of these compounds on recombinantly expressed receptor can be studied. In addition, it expresses an array of chaperon proteins, creating a favorable environment for the maturation and function of these ion channels (Section @\ref(cematnachr)). *C. elegans* pharynx has been successfully used for the heterologous expression of non-native proteins [@crisford2011], including nAChRs [@sloan2015]. +Acetylcholine is a major neurotransmitter of the pharynx, released by at least 7 out of 14 neurons (Table \@ref(tab:pharynx-neurons)). It is key and necessary for the induction of fast feeding in response to food (Section \@ref(achpumping)). Its action on the pharynx is mediated by nAChRs, most notably EAT-2 expressed at the NMJ (Section \@ref(nachrinpharynx)). *C. elegans* pharynx does not posses an innate susceptibility to low concentrations of neonicotinoids, creating an appropriate genetic background in which effects of these compounds on recombinantly expressed receptor can be studied. In addition, it expresses an array of chaperon proteins, creating a favorable environment for the maturation and function of these ion channels (Section \@ref(cematnachr)). *C. elegans* pharynx has been successfully used for the heterologous expression of non-native proteins [@crisford2011], including nAChRs [@sloan2015]. + +EAT-2 is a single nAChR subunit that confers pharyngeal 5-HT sensitivity and feeding response in *C. elegans* [@mckay2004]. We show that *eat-2* mutant is a suitable genetic background, in which the expression of heterologous nAChRs could be scored in behavioural assays. Transgenic line in which *eat-2* is heterologously expressed, rescued the blunted pharyngeal response to food and restored 5-HT resistance of the *eat-2* mutant (Section \@ref(behaviourofeat2rescue)). However, the expression of human $\alpha7$ nAChR in the *C. elegans* mutant pharynx had no observable phenotypical consequences (Section \@ref(feedingalpha7celegans) and Section \@ref(htandtransgenicalpha7)). Similarly, expression of this receptor in the wild-type worm revealed no differences in pharyngeal responses to nAChR agonists nicotine or choline (Section \@ref(pharmaalpha7transegnicworms)). Staining with fluorescently labelled human $\alpha7$ nAChR antagonist $\alpha-Bgtx$, reveled increased fluorescence in the pharyngeal muscle of transgenic, when compared to control worms (Section \@ref(bgtxstaining)). $\alpha$-bgtx binds to the extracellular, domain of the receptor [@dellisanti2007]. This suggests that $\alpha7$ receptor is expressed on the cell surface of the pharyngeal muscle, however due to the lack of phenotype its functionality is unclear. Further pharmacological experiments of transgenic strains (as described in the Discussion of Chapter 6) should be carried out to determine whether $\alpha7$ retains its function upon expression in the pharynx of *C. elegans*. -EAT-2 is a single nAChR subunit that confers pharyngeal 5-HT sensitivity and feeding response in *C. elegans* [@mckay2004]. We show that *eat-2* mutant is a suitable genetic background, in which the expression of heterologous nAChRs could be scored in behavioural assays. Transgenic line in which *eat-2* is heterologously expressed, rescued the blunted pharyngeal response to food and restored 5-HT resistance of the *eat-2* mutant (Section \@ref(behaviourofeat2rescue)). However, the expression of human $\alpha7$ nAChR in the *C. elegans* mutant pharynx had no observable phenotypical consequences (Section \@ref(feedingalpha7celegans) and \@ref(5htandtransgenicalpha7)). Similarly, expression of this receptor in the wild-type worm revealed no differences in pharyngeal responses to nAChR agonists nicotine or choline (Section \@ref(pharmaalpha7transegnicworms)). Staining with fluorescently labelled human $\alpha7$ nAChR antagonist $\alpha-Bgtx$, reveled increased fluorescence in the pharyngeal muscle of transgenic, when compared to control worms (Section \@ref(bgtxstaining)). $\alpha$-bgtx binds to the extracellular, domain of the receptor [@dellisanti2007]. This suggests that $\alpha7$ receptor is expressed on the cell surface of the pharyngeal muscle, however due to the lack of phenotype its functionality is unclear. Further pharmacological experiments of transgenic strains (as described in the Discussion of Chapter 6) should be carried out to determine whether $\alpha7$ retains its function upon expression in the pharynx of *C. elegans*. +The expression of $\alpha7$ was driven a myo-2 promoter, which should drive the expression in all cells of the pharyngeal musculature [@@altun2009a]. However, $\alpha-Bgtx$ staining of transgenic worms was concentrated in pm7 and pm8 muscle cells, suggesting $\alpha7$ is expressed in the terminal bulb, which does not overlap with the localisation of native EAT-2, native protein. Thus, native EAT-2 promoter should be used to ensure correct localisation of the expressed protein. <!-- In dissected animal, in the absence of food pharynx continues to pump. It is myogenic or neurogenic? --> @@ -149,15 +153,15 @@ EAT-2 is a single nAChR subunit that confers pharyngeal 5-HT sensitivity and fee ## *C. elegans* as a model for mammalian toxicity studies -To better understand the pharmacological profile of *C. elegans* nAChRs, the effects of endogenous neurotransmitter acetylcholine as well as agonist nicotine and cytisine were tested on the pharynx. Acetylcholine, nicotine and cytisine were applied on cut-head and the effects on EPG was assayed. All three induced potent and transient stimulation of pumping leading to muscle tetanus (Figure \@ref(fig:epg-nicotine-2-label))). Concentrations effective were in the low $\mu$M range. The order of potency as measured by the EC~50~ was: nicotine > cytisine > acetylcholine. In comparison to human $\alpha7$, effective concentrations were in a similar range [@papke2002]. This suggests the pharmacophore of human $\alpha7$ and pharyngeal nAChRs is conserved. This was confirmed by aligning the sequences of key amino acids forming the nAChR binding pocket. +To better understand the pharmacological profile of *C. elegans* nAChRs, the effects of endogenous neurotransmitter acetylcholine as well as agonist nicotine and cytisine were tested on the pharynx. Acetylcholine, nicotine and cytisine were applied on cut-head and the effects on EPG was assayed. All three induced potent and transient stimulation of pumping leading to muscle tetanus (Figure \@ref(fig:epg-nicotine-2-label))). Concentrations effective were in the low $\mu$M range. The order of potency as measured by the EC~50~ was: nicotine > cytisine > acetylcholine. In comparison to human $\alpha7$, effective concentrations were in a similar range [@papke2002]. In addition, like pharyngeal nAChRs, human $\alpha7$ receptors insensitive to low doses of neonicotinoids with the EC~50~ values of 0.74 mM and 0.73 mM, respectively for clothianidin and imidacloprid, on the heterologously expressed channel [@cartereau2018]. This suggests the pharmacophore of human $\alpha7$ and pharyngeal nAChRs is conserved. This was confirmed by aligning the sequences of key amino acids forming the nAChR binding pocket in $\alpha7$ and two of the pharyngeal nAChRs (Figure \@ref(fig:pharmacophoreceleganspharynxandhumanalpha7-label)). -(ref:pharmacophoreceleganspharynxandhumanalpha7) **Amino acid sequence alignment of human $\alpha7$ and pharyngeal *C. elegans* nAChRs ligand binding pockets.** Amino acid sequences forming nAChR binding pocket were aligned. Amino acids important in agonist binding are highlighted, as in Figure \@ref(fig:binding-pocket-label). Ce = *C. elegans*, Hs = human. Sequence alignment generated with MUSCLE. +(ref:pharmacophoreceleganspharynxandhumanalpha7) **Amino acid sequence alignment of human $\alpha7$ and two of the pharyngeal *C. elegans* nAChRs ligand binding pockets.** Amino acid sequences forming nAChR binding pocket were aligned. Amino acids important in agonist binding are highlighted, as in Figure \@ref(fig:binding-pocket-label). Ce = *C. elegans*, Hs = human. Sequence alignment generated with MUSCLE. ```{r pharmacophoreceleganspharynxandhumanalpha7-label, fig.cap="(ref:pharmacophoreceleganspharynxandhumanalpha7)", fig.scap="Amino acid sequence alignemnt of human $\\alpha7$ and pharyngeal \\textit{C. elegans} nAChRs ligand binding pockets.", fig.align='center', out.width= '150%', echo=FALSE} knitr::include_graphics("fig/gen_discussion/celeganseat2andacr7andhumanalpha7.png") ``` -Comparison of human $\alpha7$ and pharyngeal nAChR subunits EAT-2 and ACR-7 revealed high sequence similarity (Figure \@ref(fig:pharmacophoreceleganspharynxandhumanalpha7-label). Almost all residues forming ligand binding pocket are conserved between these subunits, suggesting pharyngeal nAChR subunits are homologous to human $\alpha7$. Besides pharyngeal nAChR subunits, homologs of over two thirds of human proteins can be found in *C. elegans* [@sonnhammer1997; @lai2000]. The similarities between mammals and *C. elegans* extends beyond genetics. *C. elegans* has conserved synaptic function, due to the presence of almost all vertebrate neurotransmitters and conserved neuronal signalling pathways [@bargmann1998; @kaletta2006]. There are however some differences. *C. elegans* presents expresses inhibitory glutamate-gated chloride channel absent in mammals [@cully1994], but lacks voltage-gated sodium channels which is present in humans [@bargmann1998]. Despite these limitations, *C. elegans* emerges as an attractive an attractive model for toxicity studies [@hunt2017]. +Comparison of human $\alpha7$ and pharyngeal nAChR subunits EAT-2 and ACR-7 revealed high sequence similarity. Almost all residues forming ligand binding pocket are conserved between these subunits, suggesting pharyngeal nAChR subunits are homologous to human $\alpha7$. Besides pharyngeal nAChR subunits, homologs of over two thirds of human proteins can be found in *C. elegans* [@sonnhammer1997; @lai2000]. The similarities between mammals and *C. elegans* extends beyond genetics. *C. elegans* has conserved synaptic function, due to the presence of almost all vertebrate neurotransmitters and conserved neuronal signalling pathways [@bargmann1998; @kaletta2006]. There are however some differences. *C. elegans* presents expresses inhibitory glutamate-gated chloride channel absent in mammals [@cully1994], but lacks voltage-gated sodium channels which is present in humans [@bargmann1998]. Despite these limitations, *C. elegans* emerges as an attractive model for toxicity studies [@hunt2017]. Methods to use *C. elegans* as a model to study acute toxicity as well as developmental and reproductive toxicology have been developed [@boyd2010; @xiong2017]. A good correlation between the rank order of toxicity of many compounds on *C. elegans* and mammals for acute toxicity, growth and reproduction endpoints have been found [@williams1988; @boyd2010]. This includes organophosphates, which act by disrupting cholinergic neurotransmission at the synapse [@chadwick1947]. The rank order of acute toxicity, as measured by LC50, correlated well with the LD50 ranking of these agents in rats and mice [@cole2004]. This highlight the potential suitability of *C. elegans* as a model for toxicity testing of cholinergic and other neurotoxins. Introduction of *C. elegans* into toxicity testing has a potential to reduce the use of conventional mammalian models, resulting in the reduction of cost and duration of such studies [@williams1988]. diff --git a/24-appendix-d.Rmd b/24-appendix-d.Rmd index 4ea3e4af38ba1bbf99895ac1de0acec165d33689..2901f857567055425b2a2c8e168b35fee50264e2 100644 --- a/24-appendix-d.Rmd +++ b/24-appendix-d.Rmd @@ -107,24 +107,26 @@ It needs to be noticed that although this chapter describes the expression of hu Two further ECDs, namely honey bee $\alpha5$ and *C. elegans* ACR-21 subunit were cloned. Their expression was driven from plasmids containing 2GSC, as well as two other proteins: 1VR4 and 2GUV. 1VR4 and 2GUV are bacterial proteins of unknown function, shown to form pentamers in *E. coli*. Out of 9 constructs tested, the results from the $\alpha7$ were the most promising. -```{r tesing-constructs, echo=FALSE} - -testconstructs <- data.frame( - Construct = c("$\\alpha7$-1VR4", "$\\alpha7$2GUV", "ACR21-2GSC", "ACR21-1VR4", "ACR21-2GUV", "$\\alpha5$-2GSC", "$\\alpha5$-1VR4", "$\\alpha5$-2GUV"), - Expression = c("", "~10 % purified. Remainer lost after 1st spin", "", "", "", "", "", ""), - Purification = c("", "", "", "", "", "", "", ""), - Gel = c("ND", "ND", "ND", "ND", "Aggregates", "ND", "ND", "ND") -) - -testconstructs %>% - mutate_all(linebreak) %>% - kable("latex", align = "l", booktabs = TRUE, escape = F, - col.names = linebreak(c("Construct", "Expression", "Purification", "Gel\npurification")), - caption = 'Expression of human, honeybee and C. elegans nAChR extracellular domains in E. coli', - ) %>% - kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") +<!-- ```{r tesing-constructs, echo=FALSE} --> +<!-- library(kableExtra) --> +<!-- library(dplyr) --> + +<!-- testconstructs <- data.frame( --> +<!-- Construct = c("$\\alpha7$-1VR4", "$\\alpha7$2GUV", "ACR21-2GSC", "ACR21-1VR4", "ACR21-2GUV", "$\\alpha5$-2GSC", "$\\alpha5$-1VR4", "$\\alpha5$-2GUV"), --> +<!-- Expression = c("", "~10 % purified. Remainer lost after 1st spin", "", "", "", "", "", ""), --> +<!-- Purification = c("", "", "", "", "", "", "", ""), --> +<!-- Gel = c("ND", "ND", "ND", "ND", "Aggregates", "ND", "ND", "ND") --> +<!-- ) --> + +<!-- testconstructs %>% --> +<!-- mutate_all(linebreak) %>% --> +<!-- kable("latex", align = "l", booktabs = TRUE, escape = F, --> +<!-- col.names = linebreak(c("Construct", "Expression", "Purification", "Gel\npurification")), --> +<!-- caption = 'Expression of human, honeybee and C. elegans nAChR extracellular domains in E. coli', --> +<!-- ) %>% --> +<!-- kable_styling(position = "center", full_width = FALSE, latex_options = "hold_position") --> -``` +<!-- ``` --> \newpage @@ -170,7 +172,7 @@ Western Blot was examined closely to establish which condition resulted in the p knitr::include_graphics("fig/results5/png/induction-of-hua7-2gsc-WB-and-SDS.png") ``` -Following overnight protein expression at 18 °C, induced by 0.2 mM IPTG, and 6-hour expression at 37 °C induced with 0.5 mM IPTG, the protein was purified. (Section \@ref:(purification-general-methods)). At each stage of purification the samples were collected to run them on the SDS-PAGE gel. Briefly, purification was done is a three-step process. The cells were precipitated and broken down by sonication to release their content. Homogenised cells were then spun down (low speed spin) to remove the unbroken cells, nucleic acids, organelles and large insoluble cellular particles, such as inclusion bodies (precipant was colected as a Whole Cell sample). The supernatant from this low speed spin was then spun at 100 000g to precipitate cellular organelles. $\alpha7$ ECD in the 100 000g soluble fraction was subsequently resolved using solid phase Ni^2+^-NTA IMAC purification (Section \@ref(his)). Briefly, the soluble fraction was incubated with Ni2+-NTA resin for 2 hours at 4 &dec;C to allow binding of the expressed HIS-tagged $\alpha7$ ECD chimera to beads. The mixture was decanted into the chromatography column. The unbound proteins were collected in the flow-through, before the the beads were washed three times. The wash fractions were pooled and run as “Wash” on the gel. The resin-bound protein was then eluted by washing the column with 5mL of 0.2 mM imidazole, to displace the HIS-tagged protein from the imobilized Nickel by competion. The eluted proteins were collected in two eluate fractions (Eluate 1 and 2). +Following overnight protein expression at 18 °C, induced by 0.2 mM IPTG, and 6-hour expression at 37 °C induced with 0.5 mM IPTG, the protein was purified. (Section \@ref:(purification-general-methods)). At each stage of purification the samples were collected to run them on the SDS-PAGE gel. Briefly, purification was done is a three-step process. The cells were precipitated and broken down by sonication to release their content. Homogenised cells were then spun down (low speed spin) to remove the unbroken cells, nucleic acids, organelles and large insoluble cellular particles, such as inclusion bodies (precipant was colected as a Whole Cell sample). The supernatant from this low speed spin was then spun at 100 000g to precipitate cellular organelles. $\alpha7$ ECD in the 100 000g soluble fraction was subsequently resolved using solid phase Ni^2+^-NTA IMAC purification (Section \@ref(his)). Briefly, the soluble fraction was incubated with Ni2+-NTA resin for 2 hours at 4 $^\circ$C to allow binding of the expressed HIS-tagged $\alpha7$ ECD chimera to beads. The mixture was decanted into the chromatography column. The unbound proteins were collected in the flow-through, before the the beads were washed three times. The wash fractions were pooled and run as “Wash” on the gel. The resin-bound protein was then eluted by washing the column with 5mL of 0.2 mM imidazole, to displace the HIS-tagged protein from the imobilized Nickel by competion. The eluted proteins were collected in two eluate fractions (Eluate 1 and 2). Representative samples from each of the fractions indicated above were resolved on the SDS-PAGE gel (Figure \@ref(fig:expression-conditions-test-label)) and the presence of recombinant protein was detected by Western Blot with anti-HIS-tag antibodies (Figure \@ref(fig:expression-conditions-test-label) b). Since most of the purification features are common following expression at 18 and 37 °C, some general comments are be made first. Then the comparison between the total purified protein will be made between the two. @@ -237,7 +239,7 @@ knitr::include_graphics("fig/results5/png/standard_curve.png") To prepare samples, protein was expressed in 1 L of the growth medium and purified using optimized protocol. Eluate samples collected following Ni^2+^-NTA IMAC were pooled and concentrated to 500 $\mu$L. The final concentration of the sample was 3 mg / mL, as measured by spectoscropy. This sample was run on the SDS-PAGE gel (Figure \@ref(fig:gel-filtration-eluate-label) a). -(ref:filtration-gel) **Expression and purification of $\alpha7$ ECD chimera for size-exclusion chromatography**. SDS-PAGE gel of samples collected during protein expression and purification. +(ref:filtration-gel) **Expression and purification of $\alpha7$ ECD chimera for size-exclusion chromatography**. SDS-PAGE gel of samples collected during protein expression and purification. ```{r filtration-gel-label, fig.cap="(ref: filtration-gel)", fig.scap="Expression and purification of $\\alpha7$ ECD chimera for size-exclusion chromatography", fig.align='center', echo=FALSE} knitr::include_graphics("fig/results5/png/160512_SDS_purification_ACR21-2GUV.png") @@ -290,7 +292,7 @@ In adition, to the band representing $\alpha7$ LBD - chimera there was also an i Western Blot with anti-HIS antibodies detected the presence of HIS-tagged proteins with immunoreactivity consistent with the expressed size of $\alpha7$ ECD - chimera. However, purification results showed that the proportion of induced protein availble for binding was disappointing. The expressed protein was lost during the purifcation procedure, some was precipitated following centrifugation of sonicated cells (Figure \@ref(fig:expression-conditions-test-label) Whole Cell sample), suggesting the formation of inclusion bodies. In addition, some expressed protein failed to bind to the nickel resin, potentially due to misfolding or aggregation. The expression of remaining contstruct was even more challenging, with a smaller proportion of the ECD - chimera purified. -### Analysis of canbdiate expressed protein quaternary structure. +### Analysis of the quaternary structure. To determine whether the protein was purified as a pentamer, Native-PAGE gel was run, which enables separation of folded and assembled proteins on the gel. Two samples were prepared: one containing denatured by boiling proteins and the other containing non-denatured, un-boiled proteins. A clear staining of high molecular weight proteins was observed in the un-boiled sample, but not in the boiled sample, suggesting purification of multimeric proteins. The presence of high molecular weight protein was not confirmed by the gel filtration. Therefore further experiments are needed to investigate whether expressed $\alpha7$ ECD chimera forms pentameric structures. This could include binding of radio labelled ligands, such as $\alpha-bgtx$ [@barnard1971; @carbonetto1979; @clarke1985]. diff --git a/25-appendix-e.Rmd b/25-appendix-e.Rmd index 4a00eab9358bdbce86420462c08da8da19c79502..8582ec530f85d1c59f5b95cccb5060be324ee964 100644 --- a/25-appendix-e.Rmd +++ b/25-appendix-e.Rmd @@ -2,6 +2,6 @@ (ref:appd) **Structures of soluble homopentameric soluble domains**. Single subunits are color coded and the termini of a single subunits (in purple) are shown. 2GUV and 1VR4 subunts were used as C-terminal tags of nAChR expressed in *E. coli* to prompte pentamerisation. Images generated in USCF Chimera (PDB codes: 2GUV and 1VR4). -```{r eppd-label, fig.cap="(ref:appd)", fig.scap="Structures of soluble homopentameric soluble domains", fig.align='center', echo=FALSE} +```{r appd-label, fig.cap="(ref:appd)", fig.scap="Structures of soluble homopentameric soluble domains", fig.align='center', echo=FALSE} knitr::include_graphics("fig/results5/png/HPSD.png") ``` \ No newline at end of file diff --git a/_book/Kudelska_Monika_PhD_thesis.pdf b/_book/Kudelska_Monika_PhD_thesis.pdf new file mode 100644 index 0000000000000000000000000000000000000000..fecb54660c9f5be702b5b66b63189a86bcacb221 Binary files /dev/null and b/_book/Kudelska_Monika_PhD_thesis.pdf differ diff --git a/_book/thesis-dissertaion.pdf b/_book/thesis-dissertaion.pdf index da4e0a0e46f6f95649f09bc59a99a57dc455d50e..01d1ff1ab8a94a0bc7f385c628cea1499812b696 100644 Binary files a/_book/thesis-dissertaion.pdf and b/_book/thesis-dissertaion.pdf differ diff --git a/_bookdown.yml b/_bookdown.yml index de4147c4d96a5a5d37206a3a2cad62cb67d601f4..b7bd468c000e4b0e7a8bd94351442c873a5f1783 100644 --- a/_bookdown.yml +++ b/_bookdown.yml @@ -1,6 +1,6 @@ book_filename: "thesis-dissertaion" # Change this to the actual title delete_merged_file: true -rmd_files: ["index.Rmd","00-preface.Rmd", "01-intro.Rmd","02-methods.Rmd", "03-results-01.Rmd", "04-results-02.Rmd", "05-results-03.Rmd", "06-results-04.Rmd", "19-discussion.Rmd", "20-appendix.Rmd","21-appendix-a.Rmd","22-appendix-b.Rmd", "23-appendix-c.Rmd", "24-appendix-d.Rmd", "25-appendix-e.Rmd", "26-appendix-f.Rmd", "99-references.Rmd"] +rmd_files: ["index.Rmd","00-preface.Rmd", "01-intro_2.Rmd","02-methods.Rmd", "03-results-01.Rmd", "04-results-02.Rmd", "05-results-03.Rmd", "06-results-04.Rmd", "19-discussion.Rmd", "20-appendix.Rmd", "21-appendix-a.Rmd", "22-appendix-b.Rmd", "23-appendix-c.Rmd", "24-appendix-d.Rmd", "25-appendix-e.Rmd", "26-appendix-f.Rmd", "99-references.Rmd"] #rmd_files: ["index.Rmd","00-preface.Rmd", 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J. and Dutzler, R.}, + author = {Hilf, R. J. C. and Dutzler, R.}, title = {Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel}, journal = {Nature}, year = {2009}, @@ -1749,8 +1749,8 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf}, issn = {1476-4687 (Electronic) 0028-0836 (Linking)}, doi = {10.1038/nature07461}, - type = {Journal Article}, url = {http://www.ncbi.nlm.nih.gov/pubmed/18987630}, + type = {Journal Article}, } @Article{hille1978, @@ -1818,7 +1818,7 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf}, } @Article{huang1999, - author = {Huang, Y. and Williamson, M. S. and Devonshire, A. L. and Windass, J. D. and Lansdell, S. J. and Millar, N. S.}, + author = {Huang, Y. and Williamson, M. and Devonshire, A. L. and Windass, J. D. and Lansdell, S. J. and Millar, N. S.}, title = {Molecular characterization and imidacloprid selectivity of nicotinic acetylcholine receptor subunits from the peach-potato aphid Myzus persicae}, journal = {Journal of Neurochemistry}, year = {1999}, @@ -4014,9 +4014,8 @@ http://www.nature.com/nature/journal/v423/n6943/pdf/nature01748.pdf}, pages = {2017--23}, issn = {0261-4189 (Print) 0261-4189 (Linking)}, + url = {http://www.ncbi.nlm.nih.gov/pmc/articles/PMC556666/pdf/emboj00091-0029.pdf}, type = {Journal Article}, - url = {http://www.ncbi.nlm.nih.gov/pubmed/1376242 -http://www.ncbi.nlm.nih.gov/pmc/articles/PMC556666/pdf/emboj00091-0029.pdf}, } @Article{sims1994, @@ -4674,9 +4673,8 @@ http://jcb.rupress.org/content/111/6/2623.full.pdf}, pages = {1101--24}, issn = {0022-2836 (Print) 0022-2836 (Linking)}, + url = {http://www.sciencedirect.com/science/article/pii/S0022283683711071}, type = {Journal Article}, - url = {http://www.ncbi.nlm.nih.gov/pubmed/8445638 -http://www.sciencedirect.com/science/article/pii/S0022283683711071}, } @Article{unwin1995, @@ -8002,17 +8000,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, publisher = {Elsevier}, } -@Article{jones2007b, - author = {Jones, A. K. and Davis, P. and Hodgkin, J. and Sattelle, D. B.}, - title = {The nicotinic acetylcholine receptor gene family of the nematode Caenorhabditis elegans: an update on nomenclature}, - journal = {Invertebrate Neuroscience}, - year = {2007}, - volume = {7}, - number = {2}, - pages = {129--131}, - publisher = {Springer}, -} - @Article{taylor1978, author = {Taylor, A. L. and Sasser, J. N.}, title = {Biology, identification and control of root-knot nematodes}, @@ -11049,17 +11036,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, publisher = {Rockefeller University Press}, } -@Article{hilf2008a, - author = {Hilf, Ricarda JC and Dutzler, Raimund}, - title = {X-ray structure of a prokaryotic pentameric ligand-gated ion channel}, - journal = {Nature}, - year = {2008}, - volume = {452}, - number = {7185}, - pages = {375}, - publisher = {Nature Publishing Group}, -} - @Article{tamkun1986, author = {Tamkun, John W and DeSimone, Douglas W and Fonda, Deborah and Patel, Ramila S and Buck, Clayton and Horwitz, Alan F and Hynes, Richard O}, title = {Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin}, @@ -12620,7 +12596,7 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, } @Article{alkondon2000, - author = {Alkondon, M and Pereira, E F and Eisenberg, H M and Albuquerque, E X}, + author = {Alkondon, M. and Pereira, E. F. and Eisenberg, H. M. and Albuquerque, E. X.}, title = {Nicotinic receptor activation in human cerebral cortical interneurons: a mechanism for inhibition and disinhibition of neuronal networks.}, journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, year = {2000}, @@ -14835,7 +14811,7 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, } @Online{eu2019a, - author = {The European Commission}, + author = {The European Commission.}, title = {EU Pesticides database. Entry for Sulfoxaflor.}, year = {Accessed 01 Sep 2019}, date = {2019}, @@ -16488,7 +16464,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, pages = {173--179}, issn = {0006-8993}, doi = {10.1016/0006-8993(87)91234-0}, - __markedentry = {[monik:]}, abstract = {Immunohistochemistry of the locust central nervous system with antibody to choline acetyltransferase (ChAT) purified from the same species shows: first, there are relatively few immunoreactive cell bodies in the CNS; and second, sensory neuropiles, such as the ventral association centre and the ventral VAC (vVAC), the anterior ring tract, the tritocerebrum and the antennal lobe, are immunoreactive. That ChAT is contained in sensory neurones is suggested by immunoreactivity found in peripheral neurone cell bodies. These results indicate that acetylcholine serves primarily as a sensory transmitter in the locust.}, chemicals = {Choline O-Acetyltransferase}, citation-subset = {IM}, @@ -16526,7 +16501,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, pages = {533--543}, issn = {0021-9967}, doi = {10.1002/cne.902800404}, - __markedentry = {[monik:6]}, abstract = {In situ hybridization with radiolabeled complementary RNA (cRNA) probes was used to determine the location of the messenger RNA (mRNA) encoding choline acetyltransferase (ChAT) in Drosophila nervous system. Areas in the cell-rich cortical regions of the cerebrum and optic lobes hybridized with substantial concentrations of the probe. This contrasted with the cell-sparse neuropil areas where no significant concentrations of probe were observed. Although most of the cortical regions were substantially labeled, there were regions within all of the areas where labeling was sparse or nonexistent. For example in the lamina, even though the monopolar cell layer appeared to be heavily labeled, there were some neuronal profiles that were not associated with the probe. Moreover, the epithelial glia that form an arch of cell profiles subjacent to the monopolar cells were not labeled, nor were amacrine neurons in the apex of the lamina near the external optic chiasma. The highest concentration of probe (approximately 140 grains/400 microns2) was observed in the laminar monopolar cell region and the cerebral cortical rind. The next most heavily labeled region (approximately 90 grains/400 microns2) occurred over cortical cells of the medulla-lobula. In the peripheral nervous system, label over the antennal sensory neurons amounted to about 75 grains/400 microns2, and the retinular cell layer of the compound eye exhibited about 60 grains/400 microns2. The control probe did not hybridize in significant quantities in either cellular or noncellular regions. This study presents evidence that large numbers of Drosophila cortical and primary sensory neurons contain the messenger RNA necessary for the production of ChAT, the acetylcholine-synthesizing enzyme. Further, our findings provide baseline information for use in ontogenetic studies of cholinergic neurons in Drosophila, and they also provide normative data for studying the effects of mutant alleles at the Cha or Ace loci upon the transcription of ChAT messenger RNA.}, chemicals = {RNA, Messenger, Choline O-Acetyltransferase}, citation-subset = {IM}, @@ -16542,8 +16516,8 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, revised = {2007-11-14}, } -@Article{yasuyama 1999, - author = {Yasuyama K,. Salvaterra P. M.}, +@Article{yasuyama1999, + author = {Yasuyama, K. Salvaterra, P. M.}, title = {Localization of choline acetyltransferase-expressing neurons in Drosophila nervous system.}, journal = {Microsc Res Tech}, date = {1999}, @@ -16553,4 +16527,838 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, pages = {65-79}, } +@Article{hill1910, + author = {Hill, A. V.}, + title = {The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves}, + journal = {Journal of Physiology}, + date = {1910}, + volume = {40}, + pages = {4-7}, +} + +@Article{hall1976, + author = {Hall, J. C. and Kankel, D. R.}, + title = {Genetics of acetylcholinesterase in Drosophila melanogaster.}, + journal = {Genetics}, + year = {1976}, + volume = {83}, + issue = {3 PT.2}, + month = jul, + pages = {517--535}, + issn = {0016-6731}, + abstract = {Genes in Drosophila melanogaster that control acetylcholinesterase (AChE) were searched for by segmental aneuploidy techniques. Homogenates of flies containing duplications or deletions for different segments were assayed for enzyme activity. A region on the third chromosome was found for which flies having one dose consistently gave lower AChE activity than euploid flies, which in turn had lower activity than flies with three doses. The activity differences were in the approximate ratio 1:2:3. Fine structure deletion mapping within this region revealed a very small segment for which one-dose flies have approximately half-normal activity. To obtain putative AchE-null mutations, lethal mutations within this region were assayed. Four allelic lethals have approximately half-normal activity in heterozygous condition. These lethals probably define the structural locus (symbol: Ace) for AchE.}, + chemicals = {Acetylcholinesterase}, + citation-subset = {IM}, + completed = {1976-10-20}, + country = {United States}, + issn-linking = {0016-6731}, + keywords = {Acetylcholinesterase, metabolism; Aneuploidy; Animals; Chromosome Aberrations; Drosophila melanogaster, enzymology; Genes; Genes, Lethal; Genes, Recessive; Genotype; Phenotype}, + nlm-id = {0374636}, + owner = {NLM}, + pmc = {PMC1213530}, + pmid = {821817}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{greenspan1980, + author = {Greenspan, R. J. and Finn, J. A. and Hall, J. C.}, + title = {Acetylcholinesterase mutants in Drosophila and their effects on the structure and function of the central nervous system.}, + journal = {The Journal of comparative neurology}, + year = {1980}, + volume = {189}, + issue = {4}, + month = feb, + pages = {741--774}, + issn = {0021-9967}, + doi = {10.1002/cne.901890409}, + abstract = {Mutations that eliminate acetylcholinesterase (AChE) activity were used to study the effects of disrupted acetylcholine metabolism on the form and function of the central nervous system in Drosophila melanogaster. Mutants in the Ace gene, which have no AChE activity, usually die in early development, but the postembryonic effects of this lesion can be studied in genetic mosaics, or with conditional mutants. Adult mosaics, which expressed Ace mutations in part of their CNS, exhibited morphological defects in any ganglionic neuropile whose cells were mutant. The defects included reduction in ganglionic volume, a condensed appearance, and for a very large clone, degeneration. Examination of many such mosaics indicated that small clones restricted to one side of the CNS were not usually lethal. However, mosaics with large clones, with clones on either side of the posterior slope of the protocerebrum, or with clones encompassing symmetrical structures on both sides of the CNS rarely survived to adulthood. Mosaics with AChE-null tissue on either side of the optic lobes or the posterior-inferior protocerebrum had marked deficits in optomotor behavior, although they were outwardly normal in their movement and posture. Mosaics with Ace mutant tissue in the first-order optic lobe, the lamina, lacked a synaptic component of the electroretinogram, the "off" transient. Tests of courtship behavior revealed that AChE mosaics with mutant clones in the superior protocerebrum were often capable of demonstrating male courtship. However, their behavior was quantitatively and perhaps qualitatively deficient. In order to study critical periods for the effects of mutant AChE, temperature-sensitive mutations of the Ace gene were isolated. Flies bearing certain of these new mutations produced AchE activity that was thermolabile in vivo and in vitro. The critical period during which the mutants were most susceptible to conditional lethality was late in embryogenesis.}, + chemicals = {Acetylcholinesterase}, + citation-subset = {IM}, + completed = {1980-08-15}, + country = {United States}, + issn-linking = {0021-9967}, + keywords = {Acetylcholinesterase, deficiency, genetics, physiology; Animals; Drosophila melanogaster, physiology; Electroretinography; Female; Genes, Lethal; Male; Mosaicism; Movement; Mutation; Nervous System, enzymology; Retina, physiology; Sexual Behavior, Animal, physiology; Temperature}, + nlm-id = {0406041}, + owner = {NLM}, + pmid = {6769980}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2006-11-15}, +} + +@Article{slemmon1982, + author = {Slemmon, J. R. and Salvaterra, P. M. and Crawford, G. D. and Roberts, E.}, + title = {Purification of choline acetyltransferase from Drosophila melanogaster.}, + journal = {The Journal of biological chemistry}, + year = {1982}, + volume = {257}, + issue = {7}, + month = apr, + pages = {3847--3852}, + issn = {0021-9258}, + abstract = {Choline acetyltransferase (EC 2.3.1.6) from Drosophila melanogaster (Canton S, wild type) was purified 12,500-fold to a final specific activity of 500 mumol min-1 mg protein-1. The purification used homogenized fly heads and consisted of polyethylene glycol precipitation, DEAE-Bio-Gel A chromatography, Octyl-Sepharose chromatography, and affinity chromatography using solid phase Green A-agarose. The molecular weight of the native enzyme, as determined by molecular exclusion chromatography, was approximately 67,000 daltons. The final enzyme preparation showed two major protein bands at 67,000 and 54,000 daltons on polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS). After molecular exclusion chromatography, both SDS gel bands were present in the single symmetrical peak that contained the enzyme activity. Two-dimensional tryptic peptide maps prepared from the individual SDS gel bands indicated that they have very similar primary structures. Both SDS gel bands were precipitated by two different monoclonal antibodies derived against Drosophila choline acetyltransferase activity. The structural and immunological relatedness of the two SDS gel bands indicates that the enzyme is essentially homogeneous and that, in the native state, it may consist of more than one polypeptide chain.}, + chemicals = {Antigen-Antibody Complex, Immune Sera, Peptide Fragments, Choline O-Acetyltransferase, Trypsin}, + citation-subset = {IM}, + completed = {1982-05-27}, + country = {United States}, + issn-linking = {0021-9258}, + keywords = {Amino Acid Sequence; Animals; Antigen-Antibody Complex; Choline O-Acetyltransferase, isolation & purification, metabolism; Drosophila melanogaster, enzymology; Immune Sera; Kinetics; Molecular Weight; Peptide Fragments, analysis; Trypsin}, + nlm-id = {2985121R}, + owner = {NLM}, + pmid = {6801053}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{Driskell1978, + author = {Driskell, W J and Weber, B H and Roberts, E}, + title = {Purification of choline acetyltransferase from Drosophila melanogaster.}, + journal = {Journal of neurochemistry}, + year = {1978}, + volume = {30}, + issue = {5}, + month = may, + pages = {1135--1141}, + issn = {0022-3042}, + doi = {10.1111/j.1471-4159.1978.tb12408.x}, + chemicals = {Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1978-08-28}, + country = {England}, + issn-linking = {0022-3042}, + keywords = {Animals; Choline O-Acetyltransferase, isolation & purification; Drosophila melanogaster, enzymology; Drug Stability; Kinetics}, + nlm-id = {2985190R}, + owner = {NLM}, + pmid = {96214}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-30}, +} + +@Article{chao1980, + author = {Chao, L P}, + title = {Choline acetyltransferase: purification and characterization.}, + journal = {Journal of neuroscience research}, + year = {1980}, + volume = {5}, + issue = {2}, + pages = {85--115}, + issn = {0360-4012}, + doi = {10.1002/jnr.490050202}, + chemicals = {Isoenzymes, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1980-10-24}, + country = {United States}, + issn-linking = {0360-4012}, + keywords = {Animals; Brain, enzymology; Cattle; Chemical Phenomena; Chemistry; Choline O-Acetyltransferase, antagonists & inhibitors, immunology, isolation & purification; Cockroaches, enzymology; Decapodiformes, enzymology; Drosophila melanogaster, enzymology; Enzyme Activation; Female; Fishes, metabolism; Horseshoe Crabs, enzymology; Humans; Isoenzymes, isolation & purification; Kinetics; Methods; Mice; Placenta, enzymology; Pregnancy; Rats; Snails, enzymology}, + nlm-id = {7600111}, + owner = {NLM}, + pmid = {6772798}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2008-11-21}, +} + +@Article{Tellam2003, + author = {Tellam, R L and Vuocolo, T and Eisemann, C and Briscoe, S and Riding, G and Elvin, C and Pearson, R}, + title = {Identification of an immuno-protective mucin-like protein, peritrophin-55, from the peritrophic matrix of Lucilia cuprina larvae.}, + journal = {Insect biochemistry and molecular biology}, + year = {2003}, + volume = {33}, + issue = {2}, + month = feb, + pages = {239--252}, + issn = {0965-1748}, + abstract = {A mucin-like glycoprotein, peritrophin-55 was isolated and purified from the peritrophic matrix of Lucilia cuprina larvae. When injected into sheep, peritrophin-55 induced an immune response that inhibited larval growth by 51-66% when larvae subsequently fed on sera from the vaccinated sheep. The protein may have potential use as an immunogen probably accompanying other antigens to protect sheep from the cutaneous myiasis caused by these larvae. Peritrophin-55 was uniformly distributed throughout the peritrophic matrix where it probably lubricates the surface of the peritrophic matrix and protects the midgut from invasion by bacteria. The protein consists of an 8-cysteine amino-terminal domain (peritrophin-B domain) and a carboxy-terminal proline and threonine-rich domain with high probability for extensive O-linked glycosylation. The gene consists of two exons separated by a small intron. Peritrophin-55 mRNA was only detected in the larval cardia and midgut and to a minor extent in the hindgut. Sequence upstream of the transcriptional start site contained a putative promoter region, sequence similar to an ecdysone response element, sequence related to the Drosophila transposon S element and a tetranucleotide repeat region. A putative Drosophila melanogaster ortholog or paralog of peritrophin-55 (CG7714) was located within a 3458 bp intron of the Cha gene (choline-O-acetyltransferase), but on the opposite strand. Comparison of the putative promoter regions of the peritrophin-55 and CG7714 genes revealed little similarity except for a small semi-conserved sequence that is suggestive of a common transcription factor-binding site possibly contributing to the highly restricted developmental and tissue-specific expression patterns of these genes.}, + chemicals = {Insect Proteins, Membrane Glycoproteins, Mucins, Peptide Fragments, peritrophin-55 protein, Lucilia cuprina}, + citation-subset = {IM}, + completed = {2003-04-17}, + country = {England}, + issn-linking = {0965-1748}, + keywords = {Amino Acid Sequence; Animals; Base Sequence; Diptera, immunology; Insect Proteins, chemistry, genetics, isolation & purification; Larva; Membrane Glycoproteins, chemistry, genetics, isolation & purification; Molecular Sequence Data; Mucins, isolation & purification; Peptide Fragments, chemistry; Reverse Transcriptase Polymerase Chain Reaction}, + nlm-id = {9207282}, + owner = {NLM}, + pii = {S0965174802002084}, + pmid = {12535682}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2006-11-15}, +} + +@Article{hsiao2004, + author = {Hsiao, Y. and Lai, J. and Liao, Hsiu-Y. and Feng, Hai-T.}, + title = {Purification and characterization of acetylcholinesterase from oriental fruit fly [Bactrocera dorsalis (Hendel)](Diptera: Tephritidae)}, + journal = {Journal of agricultural and food chemistry}, + year = {2004}, + volume = {52}, + number = {17}, + pages = {5340--5346}, + publisher = {ACS Publications}, +} + +@Article{harel2000, + author = {Harel, M. and Kryger, G. and Rosenberry, T. L. and Mallender, W. D. and Lewis, T. and Fletcher, R. J. and Guss, J. M. and Silman, I. and Sussman, J. L.}, + title = {Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors}, + journal = {Protein Science}, + year = {2000}, + volume = {9}, + number = {6}, + pages = {1063--1072}, + publisher = {Cambridge University Press}, +} + +@Article{kerkut1970, + author = {Kerkut, G. A. and Oliver, G. W. O. and Rick, J. T. and Walker, R. J.}, + title = {The effects of drugs on learning in a simple preparation}, + journal = {Comparative and general pharmacology}, + year = {1970}, + volume = {1}, + number = {4}, + pages = {437--484}, + publisher = {Elsevier}, +} + +@Article{carlyle1963, + author = {Carlyle, R. F.}, + title = {The mode of action of neostigmine and physostigmine on the guinea-pig trachealis muscle}, + journal = {British journal of pharmacology and chemotherapy}, + year = {1963}, + volume = {21}, + number = {1}, + pages = {137--149}, + publisher = {Wiley Online Library}, +} + +@Article{greenspan1980b, + author = {Greenspan, R. J.}, + title = {Mutations of choline acetyltransferase and associated neural defects}, + journal = {Journal of comparative physiology}, + year = {1980}, + volume = {137}, + number = {1}, + pages = {83--92}, + publisher = {Springer}, +} + +@Article{pahud1998, + author = {Pahud, G. and Salem, N. and Van De Goor, J. and Medilanski, J. and Pellegrinelli, N. and Eder-Colli, L.}, + title = {Study of subcellular localization of membrane-bound choline acetyltransferase in Drosophila central nervous system and its association with membranes}, + journal = {European Journal of Neuroscience}, + year = {1998}, + volume = {10}, + number = {5}, + pages = {1644--1653}, + publisher = {Wiley Online Library}, +} + +@Article{lutz1988, + author = {Lutz, E. M. and Lloyd, S. J. and Tyrer, N. M.}, + title = {Purification of choline acetyltransferase from the locust Schistocerca gregaria and production of serum antibodies to this enzyme}, + journal = {Journal of neurochemistry}, + year = {1988}, + volume = {50}, + number = {1}, + pages = {82--89}, + publisher = {Wiley Online Library}, +} + +@Article{fabian1997, + author = {Fabian, R. and Seyfarth, Ernst-A.}, + title = {Acetylcholine and histamine are transmitter candidates in identifiable mechanosensitive neurons of the spider Cupiennius salei: an immunocytochemical study}, + journal = {Cell and tissue research}, + year = {1997}, + volume = {287}, + number = {2}, + pages = {413--423}, + publisher = {Springer}, +} + +@Article{kitamoto1998, + author = {Kitamoto, T. and Wang, W. and Salvaterra, P. M.}, + title = {Structure and organization of the Drosophila cholinergic locus.}, + journal = {The Journal of biological chemistry}, + year = {1998}, + volume = {273}, + issue = {5}, + month = jan, + pages = {2706--2713}, + issn = {0021-9258}, + doi = {10.1074/jbc.273.5.2706}, + abstract = {The Drosophila cholinergic locus is composed of two distinct genetic functions: choline acetyltransferase (ChAT; EC 2.3.1.6), the enzyme catalyzing biosynthesis of neurotransmitter acetylcholine (ACh), and the vesicular ACh transporter (VAChT), the synaptic vesicle membrane protein which pumps transmitter into vesicles. Both genes share a common first exon and the remainder of the VAChT gene contains a single coding exon residing entirely within the first intron of ChAT. RNase protection analysis indicates that all Drosophila VAChT specific transcripts contain the shared first exon and suggests common transcriptional control for ChAT and VAChT. Similar types of genomic organization have been evolutionarily conserved for cholinergic loci in nematodes and vertebrates, and may operate to ensure coordinate expression of these functionally related genes in the same cells. The relative levels of Drosophila ChAT and VAChT mRNA differ, however, in different tissues or in Cha mutants, indicating that independent regulation of ChAT and VAChT transcripts may occur post-transcriptionally. The predicted Drosophila VAChT protein is composed of 578 amino acids and contains 12 conserved putative transmembrane domains. Full-length VAChT cDNA is 7.2 kilobase long and has unusually long 5'- and 3'-untranslated regions (UTR). The 5'-UTR contains a GTG ChAT translational initiation codon along with three other potential ATG initiation codons. These features of the VAChT 5'-UTR region suggest that a ribosome scanning model may not be used for VAChT translation initiation.}, + chemicals = {Carrier Proteins, DNA, Complementary, Drosophila Proteins, Membrane Transport Proteins, Nerve Tissue Proteins, RNA Precursors, VAChT protein, Drosophila, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1998-02-23}, + country = {United States}, + issn-linking = {0021-9258}, + keywords = {Amino Acid Sequence; Animals; Base Sequence; Carrier Proteins, biosynthesis, genetics; Choline O-Acetyltransferase, biosynthesis, genetics; Cholinergic Fibers; DNA, Complementary, genetics; Drosophila Proteins; Drosophila melanogaster, genetics; Exons; Genomic Library; Introns; Membrane Transport Proteins; Molecular Sequence Data; Nerve Tissue Proteins, biosynthesis, genetics; Nucleic Acid Conformation; Protein Conformation; RNA Precursors, chemistry, genetics; RNA Processing, Post-Transcriptional; Sequence Homology, Amino Acid; Species Specificity; Transcription, Genetic; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins}, + nlm-id = {2985121R}, + owner = {NLM}, + pmid = {9446576}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-08}, +} + +@Article{song1997, + author = {Song, H. and Ming, G. and Fon, E. and Bellocchio, E. and Edwards, R. H. and Poo, M.}, + title = {Expression of a putative vesicular acetylcholine transporter facilitates quantal transmitter packaging.}, + journal = {Neuron}, + year = {1997}, + volume = {18}, + issue = {5}, + month = may, + pages = {815--826}, + issn = {0896-6273}, + doi = {10.1016/s0896-6273(00)80320-7}, + abstract = {A putative vesicular acetylcholine transporter (VAChT) was overexpressed in developing Xenopus spinal neurons by injection of rat VAChT cDNA or synthetic mRNA into Xenopus embryos. This resulted in a marked increase in the amplitude and frequency of miniature excitatory postsynaptic currents at neuromuscular synapses, reflecting an over 10-fold increase in the vesicular packaging of acetylcholine (ACh). The effect appeared in developing neurons even before synaptogenesis and was blocked by L-vesamicol, a specific blocker of ACh uptake into synaptic vesicles. Mutational studies showed that two highly conserved aspartate residues within putative transmembrane domains 4 and 10 are essential for the transport activity. These results provide direct evidence for the physiological function of a putative VAChT and demonstrate that quantal size can be regulated by changes in vesicular transporter activity.}, + chemicals = {Carrier Proteins, Membrane Transport Proteins, Neuromuscular Depolarizing Agents, Piperidines, Slc18a3 protein, rat, Synaptophysin, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Aspartic Acid, vesamicol, Acetylcholine}, + citation-subset = {IM}, + completed = {1997-06-30}, + country = {United States}, + issn-linking = {0896-6273}, + keywords = {Acetylcholine, metabolism; Animals; Aspartic Acid, genetics; Blastomeres; Carrier Proteins, analysis, genetics, metabolism; Cells, Cultured; Embryo, Nonmammalian, chemistry, physiology; Female; Gene Expression Regulation, Developmental, physiology; Membrane Transport Proteins; Microinjections; Muscles, cytology; Mutagenesis, physiology; Nervous System, cytology; Neuromuscular Depolarizing Agents, pharmacology; Neurons, chemistry, physiology, ultrastructure; Patch-Clamp Techniques; Piperidines, pharmacology; Rats; Synapses, chemistry, physiology; Synaptic Transmission, drug effects, physiology; Synaptophysin, analysis; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins; Xenopus laevis}, + nlm-id = {8809320}, + owner = {NLM}, + pii = {S0896-6273(00)80320-7}, + pmid = {9182805}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-08-22}, +} + +@Article{varoqui1996, + author = {Varoqui, H. and Erickson, J. D.}, + title = {Active transport of acetylcholine by the human vesicular acetylcholine transporter.}, + journal = {The Journal of biological chemistry}, + year = {1996}, + volume = {271}, + issue = {44}, + month = nov, + pages = {27229--27232}, + issn = {0021-9258}, + doi = {10.1074/jbc.271.44.27229}, + abstract = {The characteristics of ATP-dependent transport of acetylcholine (ACh) in homogenates of pheochromocytoma (PC-12) cells stably transfected with the human vesicular acetylcholine transporter (VAChT) cDNA are described. The human VAChT protein was abundantly expressed in this line and appeared as a diffuse band with a molecular mass of approximately 75 kDa on Western blots. Vesicular [3H]ACh accumulation increased approximately 20 times over levels attained by the endogenous rat VAChT, expressed at low levels in control PC-12 cells. The transport of [3H]ACh by human VAChT was dependent upon the addition of exogenous ATP at 37 degrees C. Uptake was abolished by low temperature (4 degrees C), the proton ionophore carbonyl cyanide p-trifluoromethoxyphenylhydrazone (2.5 microM) and bafilomycin A1 (1 microM), a specific inhibitor of the vesicular H+-ATPase. The kinetics of [3H]ACh uptake by human VAChT were saturable, exhibiting an apparent Km of 0.97 +/- 0.1 mM and Vmax of 0.58 +/- 0.04 nmol/min/mg. Maximal steady-state levels of vesicular [3H]ACh accumulation were directly proportional to the concentration of substrate present in the medium with saturation occurring at approximately 4 mM. Uptake was stereospecifically inhibited by L-vesamicol with an IC50 of 14.7 +/- 1.5 nM. The apparent affinity (Kd) of [3H]vesamicol for human VAChT was 4.1 +/- 0.5 nM, and the Bmax was 8.9 +/- 0.6 pmol/mg. The turnover (Vmax/Bmax) of the human VAChT was approximately 65/min. This expression system should prove useful for the structure/function analysis of VAChT.}, + chemicals = {Carrier Proteins, Membrane Transport Proteins, Neuromuscular Depolarizing Agents, Piperidines, Recombinant Proteins, SLC18A3 protein, human, Slc18a3 protein, rat, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, vesamicol, Acetylcholine, Tetrabenazine}, + citation-subset = {IM}, + completed = {1996-12-26}, + country = {United States}, + issn-linking = {0021-9258}, + keywords = {Acetylcholine, metabolism; Adrenal Gland Neoplasms; Animals; Biological Transport, Active, drug effects; Carrier Proteins, biosynthesis, metabolism; Cytosol, metabolism; Humans; Kinetics; Membrane Transport Proteins; Neuromuscular Depolarizing Agents, metabolism, pharmacology; PC12 Cells; Pheochromocytoma; Piperidines, metabolism, pharmacology; Rats; Recombinant Proteins, biosynthesis, metabolism; Substrate Specificity; Tetrabenazine, metabolism, pharmacology; Transfection; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins}, + nlm-id = {2985121R}, + owner = {NLM}, + pmid = {8910293}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-08}, +} + +@Article{kitamoto2000, + author = {Kitamoto, T and Xie, X and Wu, C F and Salvaterra, P M}, + title = {Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster.}, + journal = {Journal of neurobiology}, + year = {2000}, + volume = {42}, + issue = {2}, + month = feb, + pages = {161--171}, + issn = {0022-3034}, + abstract = {The Drosophila vesicular acetylcholine transporter gene (Vacht) is nested within the first intron of the choline acetyltransferase gene (Cha). To isolate Vacht mutants, we performed an F(2) genetic screen and identified mutations that failed to complement Df(3R)Cha(5), a deletion lacking Cha and the surrounding genes. Of these mutations, three mapped to a small genomic region where Cha resides. Complementation tests with a Cha mutant allele and rescue experiments using a transgenic Vacht minigene have revealed that two of these three mutations are nonconditional lethal alleles of Vacht (Vacht(1) and Vacht(2) ). The other is a new temperature-sensitive allele of Cha (Cha(ts3) ). Newly isolated Vacht mutants were used to reexamine the existing Cha mutations. We found that all deficiencies uncovering Cha also lack Vacht function, reflecting the nested organization of the two genes. The effective lethal phase for Vacht(1) is the embryonic stage, whereas that for Vacht(2) is the larval stage. Viable first-instar larvae homozygous for Vacht(2) showed reduced motility. Adult flies heterozygous for Vacht mutations were found to have defective responses in the dorsal longitudinal muscles following high-frequency brain stimulation. Since cholinergic synapses have been shown to be involved in the giant fiber pathway that mediates this response, the result suggested that reduction in the Vacht activity to 50% causes an abnormality in cholinergic transmission when stressed by a high-frequency stimulus.}, + chemicals = {Carrier Proteins, Drosophila Proteins, Membrane Transport Proteins, VAChT protein, Drosophila, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {2000-02-08}, + country = {United States}, + issn-linking = {0022-3034}, + keywords = {Alleles; Animals; Blotting, Western; Brain, enzymology; Carrier Proteins, genetics, physiology; Choline O-Acetyltransferase, metabolism; Drosophila Proteins; Drosophila melanogaster, genetics, physiology; Electrophysiology; Female; Genes, Lethal; Heterozygote; Larva, genetics, physiology; Male; Membrane Transport Proteins; Motor Activity, genetics; Muscles, enzymology; Mutagenesis; Nerve Fibers, enzymology, physiology; Synapses, genetics, physiology; Temperature; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins}, + nlm-id = {0213640}, + owner = {NLM}, + pii = {10.1002/(SICI)1097-4695(20000205)42:2<161::AID-NEU1>3.0.CO;2-P}, + pmid = {10640324}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{karnovsky1964, + author = {Karnovsky, M. J. and Roots, L.}, + title = {A "direct-coloring thiocholine method for cholinesterase".}, + journal = {The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society}, + year = {1964}, + volume = {12}, + month = mar, + pages = {219--221}, + issn = {0022-1554}, + doi = {10.1177/12.3.219}, + chemicals = {Coloring Agents, Thiocholine, Copper, Cholinesterases, Choline}, + citation-subset = {OM}, + completed = {1996-12-01}, + country = {United States}, + issn-linking = {0022-1554}, + keywords = {Choline; Cholinesterases; Color; Coloring Agents; Copper; Histocytochemistry; Research; Staining and Labeling; Thiocholine; CHOLINE; CHOLINESTERASE; COPPER; EXPERIMENTAL LAB STUDY; HISTOCYTOCHEMISTRY; STAINS AND STAINING}, + nlm-id = {9815334}, + owner = {NLM}, + pmid = {14187330}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2018-12-01}, +} + +@Article{gorczyca1987, + author = {Gorczyca, M. G. and Hall, J. C.}, + title = {Immunohistochemical localization of choline acetyltransferase during development and in Chats mutants of Drosophila melanogaster.}, + journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, + year = {1987}, + volume = {7}, + issue = {5}, + month = may, + pages = {1361--1369}, + issn = {0270-6474}, + abstract = {The distribution of choline acetyltransferase (CAT) in the nervous system of Drosophila melanogaster was determined by indirect immunohistochemical procedures using a monoclonal antibody specific to the enzyme. Immunoreactivity was first detected in the nervous system of 16 hr embryos, and increased considerably by the end of embryogenesis. Neuropil was preferentially stained, though cell bodies could also be observed. Staining was prominent in the CNS of all 3 larval instars but decreased substantially during the mid-pupal stage. Prior to eclosion, the level of immunoreactivity increased and the adult staining pattern became discernible. In the adult brain, staining was extensive, with numerous structures, such as the optic lobes and mushroom bodies, staining strongly. The adult thoracic ganglia were also moderately immunoreactive. These results imply a wide distribution of cholinergic neurons in the CNS of Drosophila. Immunoreactivity was also determined for 2 temperature-sensitive CAT mutants, Chats1 and Chats2. These files exhibit reduced CAT activity at permissive temperature, 18 degrees C, which eventually falls to undetectable levels after incubation at nonpermissive temperature, 30 degrees C. Chats2 mutants, after incubation at either 18 or 30 degrees C displayed virtually no staining. This result indicated that the immunoreactivity observed in wild-type flies was specifically associated with the enzyme encoded by the Cha gene. The intensity of staining in Chats1 mutants incubated at 18 degrees C appeared greater than in control flies, even though CAT enzyme activity in Chats1 is lower. This suggests that the enzyme molecule itself is structurally altered in Chats1 mutants. After incubation at 30 degrees C, staining in Chats1 flies decreased but did not disappear.}, + chemicals = {Horseradish Peroxidase, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1987-06-25}, + country = {United States}, + issn-linking = {0270-6474}, + keywords = {Animals; Central Nervous System, enzymology; Choline O-Acetyltransferase, analysis; Drosophila melanogaster, enzymology, genetics; Embryo, Nonmammalian; Histocytochemistry; Horseradish Peroxidase; Immunologic Techniques; Larva; Mutation; Neurons, enzymology; Pupa; Temperature}, + nlm-id = {8102140}, + owner = {NLM}, + pmid = {3106590}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{sattelle1983, + author = {Sattelle, D. B. and Harrow, I. D. and Hue, B. and Pelhate, M. and Gepner, J. I. and Hall, L. M.}, + title = {$\alpha$-Bungarotoxin Blocks excitatory synaptic transmission between cercal sensory neurones and Giant Interneurone 2 of the cockroach, Peripianeta americana}, + journal = {Journal of experimental biology}, + year = {1983}, + volume = {107}, + number = {1}, + pages = {473--489}, + publisher = {The Company of Biologists Ltd}, +} + +@Article{daley1988, + author = {Daley, D. L. and Camhi, J. M.}, + title = {Connectivity pattern of the cercal-to-giant interneuron system of the American cockroach}, + journal = {Journal of neurophysiology}, + year = {1988}, + volume = {60}, + number = {4}, + pages = {1350--1368}, + publisher = {American Physiological Society Bethesda, MD}, +} + +@Article{scheidler1990, + author = {Scheidler, A. and Kaulen, P. and Briining, G. and Erber, J.}, + title = {Quantitative autoradiographic localization of [125I]α-bungarotoxin binding sites in the honeybee brain.}, + journal = {Brain Research}, + date = {1990}, + volume = {534}, + pages = {332-335}, +} + +@Article{schmidt-nielsen1977, + author = {Schmidt-Nielsen, B. K. and Gepner, J. I. and Teng, N. N. and Hall, L. M.}, + title = {Characterization of an alpha-bungarotoxin binding component from Drosophila melanogaster.}, + journal = {Journal of neurochemistry}, + year = {1977}, + volume = {29}, + issue = {6}, + month = dec, + pages = {1013--1029}, + issn = {0022-3042}, + doi = {10.1111/j.1471-4159.1977.tb06505.x}, + chemicals = {Bungarotoxins, Receptors, Cholinergic, Acetylcholine}, + citation-subset = {IM}, + completed = {1978-03-21}, + country = {England}, + issn-linking = {0022-3042}, + keywords = {Acetylcholine, pharmacology; Animals; Binding Sites; Brain Chemistry; Bungarotoxins, antagonists & inhibitors, metabolism; Dose-Response Relationship, Drug; Drosophila melanogaster; Kinetics; Methods; Receptors, Cholinergic, analysis; Synapses, analysis; Time Factors}, + nlm-id = {2985190R}, + owner = {NLM}, + pmid = {413880}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-30}, +} + +@Article{hildebrand1979, + author = {Hildebrand, J. G. and Hall, L. M. and Osmond, B. C.}, + title = {Distribution of binding sites for 125I-labeled alpha-bungarotoxin in normal and deafferented antennal lobes of Manduca sexta.}, + journal = {Proceedings of the National Academy of Sciences of the United States of America}, + year = {1979}, + volume = {76}, + issue = {1}, + month = jan, + pages = {499--503}, + issn = {0027-8424}, + doi = {10.1073/pnas.76.1.499}, + abstract = {125I-Labeled alpha-bungarotoxin has been used to determine the distribution of putative acetylcholine receptors in normal and chronically deafferented antennal lobes in the brain of the moth Manduca sexta. Toxin-binding sites are confined to synaptic regions in deafferented lobes. These findings suggest that receptors can develop in the insect central nervous system independently of normal synaptic influences.}, + chemicals = {Bungarotoxins, Receptors, Cholinergic}, + citation-subset = {IM}, + completed = {1979-05-26}, + country = {United States}, + issn-linking = {0027-8424}, + keywords = {Afferent Pathways; Animals; Brain, cytology, metabolism; Bungarotoxins, metabolism; Denervation; Lepidoptera, metabolism; Moths, metabolism; Receptors, Cholinergic, metabolism; Synapses, metabolism}, + nlm-id = {7505876}, + owner = {NLM}, + pmc = {PMC382969}, + pmid = {284367}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-01}, +} + +@Article{meyer1985, + author = {Meyer, M. R. and Reddy, G. R.}, + title = {Muscarinic and nicotinic cholinergic binding sites in the terminal abdominal ganglion of the cricket (Acheta domesticus).}, + journal = {Journal of neurochemistry}, + year = {1985}, + volume = {45}, + issue = {4}, + month = oct, + pages = {1101--1112}, + issn = {0022-3042}, + doi = {10.1111/j.1471-4159.1985.tb05529.x}, + abstract = {Cricket (Acheta domesticus) terminal abdominal ganglia (TG) contain high concentrations (approximately 2 pmol/mg protein) of muscarinic and nicotinic cholinergic binding sites, based on the capacity of TG to bind specifically the labelled ligands L-[3H]quinuclidinyl benzilate ([3H]QNB) and [125I]alpha-bungarotoxin ([125I]alpha-BGT) with high affinity. For both ligands, binding is saturable and reversible. Competitive displacement experiments indicate that the [3H]QNB and [125I]alpha-BGT binding sites probably represent pharmacologically distinct classes of putative TG acetylcholine receptors (AChRs). Results from physiological recording and autoradiographic localization experiments demonstrate that a portion of the putative nicotinic AChRs is localized in synaptic regions of the well-characterized cercal sensory-giant interneuron pathway in the TG, where they are likely to serve as functional synaptic AChRs. Unlike nicotinic ligands, muscarinic agents do not appear to be pharmacologically active in this pathway. Therefore, in the insect CNS, putative muscarinic and nicotinic AChRs coexist at high density, but can be pharmacologically distinguished from one another on the basis of criteria derived from both ligand binding and physiological methods.}, + chemicals = {Bungarotoxins, Receptors, Muscarinic, Receptors, Nicotinic, Quinuclidinyl Benzilate, Tubocurarine}, + citation-subset = {IM}, + completed = {1985-10-11}, + country = {England}, + issn-linking = {0022-3042}, + keywords = {Animals; Autoradiography; Binding, Competitive; Bungarotoxins, metabolism; Evoked Potentials; Ganglia, metabolism; Kinetics; Orthoptera; Quinuclidinyl Benzilate, metabolism; Receptors, Muscarinic, metabolism; Receptors, Nicotinic, metabolism; Synaptic Transmission; Tubocurarine, pharmacology}, + nlm-id = {2985190R}, + owner = {NLM}, + pmid = {2993520}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-30}, +} + +@Article{orr1990, + author = {Orr, G. L. and Orr, N. and Hollingworth, R. M.}, + title = {Localization and pharmacological characterization of nicotinic-cholinergic binding sites in cockroach brain using α- and neuronal bungarotoxin}, + journal = {Insect Biochemistry}, + date = {1990}, + volume = {20}, + issue = {6}, + pages = {557-566}, +} + +@Article{kerkut1969, + author = {Kerkut, G. A. and Pitman, R. M. and Walker, R. J.}, + title = {Iontophoretic application of acetylcholine and gaba onto insect central neurones.}, + journal = {Comparative Biochemistry and Physiology}, + date = {1969}, + volume = {31}, + issue = {4}, + pages = {611-612}, +} + +@Article{barbara2005, + author = {Barbara, Guillaume Stephane and Zube, Christina and Rybak, Jürgen and Gauthier, Monique and Grünewald, Bernd}, + title = {Acetylcholine, GABA and glutamate induce ionic currents in cultured antennal lobe neurons of the honeybee, Apis mellifera.}, + journal = {Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology}, + year = {2005}, + volume = {191}, + issue = {9}, + month = sep, + pages = {823--836}, + issn = {0340-7594}, + doi = {10.1007/s00359-005-0007-3}, + abstract = {The honeybee, Apis mellifera, is a valuable model system for the study of olfactory coding and its learning and memory capabilities. In order to understand the synaptic organisation of olfactory information processing, the transmitter receptors of the antennal lobe need to be characterized. Using whole-cell patch-clamp recordings, we analysed the ligand-gated ionic currents of antennal lobe neurons in primary cell culture. Pressure applications of acetylcholine (ACh), gamma-amino butyric acid (GABA) or glutamate induced rapidly activating ionic currents. The ACh-induced current flows through a cation-selective ionotropic receptor with a nicotinic profile. The ACh-induced current is partially blocked by alpha-bungarotoxin. Epibatidine and imidacloprid are partial agonists. Our data indicate the existence of an ionotropic GABA receptor which is permeable to chloride ions and sensitive to picrotoxin (PTX) and the insecticide fipronil. We also identified the existence of a chloride current activated by pressure applications of glutamate. The glutamate-induced current is sensitive to PTX. Thus, within the honeybee antennal lobe, an excitatory cholinergic transmitter system and two inhibitory networks that use GABA or glutamate as their neurotransmitter were identified.}, + chemicals = {Excitatory Amino Acid Agonists, Excitatory Amino Acid Antagonists, GABA Agonists, GABA Antagonists, Ion Channels, Nicotinic Agonists, Nicotinic Antagonists, Glutamic Acid, gamma-Aminobutyric Acid, Histamine, Acetylcholine, Epinephrine}, + citation-subset = {IM}, + completed = {2005-12-15}, + country = {Germany}, + issn-linking = {0340-7594}, + keywords = {Acetylcholine, pharmacology; Animals; Bees; Cells, Cultured; Dose-Response Relationship, Drug; Drug Interactions; Epinephrine, pharmacology; Excitatory Amino Acid Agonists, pharmacology; Excitatory Amino Acid Antagonists, pharmacology; GABA Agonists, pharmacology; GABA Antagonists; Glutamic Acid, pharmacology; Histamine, pharmacology; Ion Channels, physiology; Membrane Potentials, drug effects; Models, Neurological; Neurons, Afferent, drug effects, physiology; Nicotinic Agonists, pharmacology; Nicotinic Antagonists, pharmacology; Olfactory Pathways, cytology; Patch-Clamp Techniques, methods; Pupa; gamma-Aminobutyric Acid, pharmacology}, + nlm-id = {101141792}, + owner = {NLM}, + pmid = {16044331}, + pubmodel = {Print-Electronic}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{pumphrey1937, + author = {Pumphrey, R. J. and Rawdon-Smith, A. F.}, + title = {Synaptic transmission of nervous impulses through the last abdominal ganglion of the cockroach}, + journal = {Proceedings of the Royal Society of London. Series B-Biological Sciences}, + year = {1937}, + volume = {122}, + number = {826}, + pages = {106--118}, + publisher = {The Royal Society London}, +} + +@Article{Hoskins1940, + author = {Hoskins, W and others}, + title = {Recent contributions of insect physiology to insect toxicology and control}, + journal = {Hilgardia}, + year = {1940}, + volume = {13}, + number = {6}, + pages = {307--386}, + publisher = {University of California, Agriculture and Natural Resources}, +} + +@Article{Mongeau2015, + author = {Mongeau, Jean-Michel and Sponberg, Simon N and Miller, John P and Full, Robert J}, + title = {Sensory processing within cockroach antenna enables rapid implementation of feedback control for high-speed running maneuvers}, + journal = {Journal of Experimental Biology}, + year = {2015}, + volume = {218}, + number = {15}, + pages = {2344--2354}, + publisher = {The Company of Biologists Ltd}, +} + +@Article{sattelle1976, + author = {Sattelle, D. B. and McClay, A. S. and Dowson, R. J. and Callec, J. J.}, + title = {The pharmacology of an insect ganglion: actions of carbamylcholine and acetylcholine.}, + journal = {The Journal of experimental biology}, + year = {1976}, + volume = {64}, + issue = {1}, + month = feb, + pages = {13--23}, + issn = {0022-0949}, + abstract = {1. Methods for presenting dose-response data for the ganglionic actions of cholinergic agonists (e.g. carbamylcholine) are compared, using the mannitol-gap technique for electrophysiological recording of synaptic events at the cercal nerve, giant fibre synapse of the sixth abdominal ganglion of the cockroach Periplaneta americana. 2. At concentrations around 10(-5)M, carbamylcholine has no effect on ganglionic polarization but potentiates the monosynaptic EPSP. At 10(-4)M and higher concentrations, ganglionic depolarization is accompanied by a reduction of EPSP. 3. Pretreatment with eserine (10(-6) M) considerably shifts the dose-response curve for acetylcholine so that synaptic transmission is consistently sensitive to 10(-6) M acetylcholine.}, + chemicals = {Receptors, Cholinergic, Carbachol, Physostigmine, Acetylcholine}, + citation-subset = {IM}, + completed = {1976-08-02}, + country = {England}, + issn-linking = {0022-0949}, + keywords = {Acetylcholine, pharmacology; Animals; Carbachol, pharmacology; Dose-Response Relationship, Drug; Drug Interactions; Ganglia, drug effects, physiology; In Vitro Techniques; Membrane Potentials, drug effects; Periplaneta; Physostigmine, pharmacology; Receptors, Cholinergic; Synaptic Transmission}, + nlm-id = {0243705}, + owner = {NLM}, + pmid = {178820}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2015-11-19}, +} + +@Article{callec1973, + author = {Callec, J. J. and Sattelle, D. B.}, + title = {A simple technique for monitoring the synaptic actions of pharmacological agents.}, + journal = {The Journal of experimental biology}, + year = {1973}, + volume = {59}, + issue = {3}, + month = dec, + pages = {725--738}, + issn = {0022-0949}, + chemicals = {Acetylcholine}, + citation-subset = {IM}, + completed = {1974-02-22}, + country = {England}, + issn-linking = {0022-0949}, + keywords = {Acetylcholine, pharmacology; Action Potentials, drug effects; Animals; Axons, physiology; Cockroaches; Dose-Response Relationship, Drug; Electric Stimulation; Evoked Potentials, drug effects; Ganglia, drug effects, physiology; Methods; Perfusion; Sensory Receptor Cells, drug effects, physiology; Synapses, drug effects, physiology; Synaptic Transmission, drug effects}, + nlm-id = {0243705}, + owner = {NLM}, + pmid = {4357996}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2013-11-21}, +} + +@Article{goldberg1999, + author = {Goldberg, F. and Grünewald, B. and Rosenboom, H. and Menzel, R.}, + title = {Nicotinic acetylcholine currents of cultured Kkenyon cells from the mushroom bodies of the honey bee Aapis mellifera.}, + journal = {The Journal of physiology}, + year = {1999}, + volume = {514 ( Pt 3)}, + month = feb, + pages = {759--768}, + issn = {0022-3751}, + doi = {10.1111/j.1469-7793.1999.759ad.x}, + abstract = {1. Acetylcholine-induced currents of mushroom body Kenyon cells from the honey bee Apis mellifera were studied using the whole-cell configuration of the patch clamp technique. Pressure application of 1 mM acetylcholine (ACh) induced inward currents with amplitudes between -5 and -500 pA. 2. The cholinergic agonists ACh and carbamylcholine had almost equal potencies of current activation at concentrations between 0.01 and 1 mM; nicotine was less potent. The muscarinic agonist oxotremorine did not elicit any currents. 3. Approximately 80 % of the ACh-induced current was irreversibly blocked by 1 microM alpha-bungarotoxin. Atropine (1 mM) did not block the ACh-induced current. 4. Upon prolonged ACh application the current desensitized with a time course that could be approximated by the sum of two exponentials (tau1 = 276 +/- 45 ms (mean +/- s.e.m. ) for the fast component and tau2 = 2.4 +/- 0.7 s for the slow component). 5. Noise analyses of whole-cell currents yielded elementary conductances of 19.5 +/- 2.4 pS for ACh and 23.7 +/- 5.0 pS for nicotine. The channel lifetimes, calculated from the frequency spectra, were tauo = 1.8 ms for ACh and tauo = 2.5 ms for nicotine. 6. Raising the external calcium concentration from 5 to 50 mM shifted the reversal potential of the ACh-induced current from +4. 6 +/- 0.9 to +37.3 +/- 1.3 mV. The calcium-to-sodium permeability ratio (PCa : PNa) was 6.4. 7. In high external calcium solution (50 mM) the ACh-induced current rectified in an outward direction at positive membrane potentials. 8. We conclude that Kenyon cells express nicotinic ACh receptors with functional profiles reminiscent of the vertebrate neuronal nicotinic ACh receptor subtype.}, + chemicals = {Cholinergic Agonists, Nicotinic Agonists, Receptors, Nicotinic, Carbachol, Sodium, Calcium}, + citation-subset = {IM}, + completed = {1999-03-26}, + country = {England}, + issn-linking = {0022-3751}, + keywords = {Animals; Bees, metabolism; Calcium, metabolism; Carbachol, pharmacology; Cell Membrane, drug effects, metabolism; Cells, Cultured; Cholinergic Agonists, pharmacology; Electric Stimulation; Electrophysiology; Membrane Potentials, physiology; Nicotinic Agonists, pharmacology; Patch-Clamp Techniques; Receptors, Nicotinic, drug effects, metabolism; Sodium, metabolism}, + nlm-id = {0266262}, + owner = {NLM}, + pmc = {PMC2269090}, + pmid = {9882748}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-12}, +} + +@Article{albert1993, + author = {Albert, J. L. and Lingle, C. J.}, + title = {Activation of nicotinic acetylcholine receptors on cultured Drosophila and other insect neurones.}, + journal = {The Journal of physiology}, + year = {1993}, + volume = {463}, + month = apr, + pages = {605--630}, + issn = {0022-3751}, + doi = {10.1113/jphysiol.1993.sp019613}, + abstract = {1. Using whole-cell and single channel recordings, we have examined the properties of acetylcholine (ACh)-activated currents in neurones from larval and pupal Drosophila melanogaster (fruit fly), larval and embryonic Musca domestica (house fly), and nymphal Schistocerca gregaria (locust). 2. In all preparations, single channel recordings revealed two major classes of ACh-activated channels, with average conductances of approximately 32 and 59 pS. 3. At ACh concentrations from 1 to 10 microM, channel activity in Drosophila larval neurones occurs in bursts with an average of 1-2 openings. Open times and burst durations are described by one or two exponentials. Burst durations for the 32 pS channel (approximately 3 ms, slow component) were longer than those for the 59 pS channel (approximately 1.0 ms). The mean open interval duration for the 32 pS channel (slow component) was also longer than that of the 59 pS channel. 4. At high ACh (20-200 microM) concentrations, bursts of the smaller conductance channel occur in clusters separated by long-lived periods without channel activity. Considerable kinetic heterogeneity was observed among clusters. 5. The whole-cell dose-response curve suggests that activation of current by ACh increases up to at least 100 microM and that multiple ligand binding steps are involved. 6. Drosophila and Musca larval neuronal ACh-activated channels show some unique features in their cholinergic pharmacological properties: (a) they are only weakly activated by the potent neuromuscular nicotinic agonist suberyldicholine, (b) hexamethonium and decamethonium are weak, but approximately equi-effective blockers, and (c) alpha- and kappa-bungarotoxin (BTX) both blocked reversibly, though alpha-BTX appears to be the more potent inhibitor.}, + chemicals = {Decamethonium Compounds, Hexamethonium Compounds, Ion Channels, Receptors, Nicotinic, Tetrodotoxin, Mecamylamine, Trimethaphan, Chlorisondamine, Acetylcholine}, + citation-subset = {IM}, + completed = {1993-12-30}, + country = {England}, + issn-linking = {0022-3751}, + keywords = {Acetylcholine, pharmacology; Animals; Cells, Cultured; Chlorisondamine, pharmacology; Decamethonium Compounds, pharmacology; Drosophila melanogaster, metabolism; Grasshoppers; Hexamethonium Compounds, pharmacology; Houseflies; Insecta, metabolism; Ion Channels, drug effects, metabolism; Kinetics; Larva; Mecamylamine, pharmacology; Neurons, drug effects, metabolism; Pupa; Receptors, Nicotinic, drug effects, metabolism; Tetrodotoxin, pharmacology; Trimethaphan, pharmacology}, + nlm-id = {0266262}, + owner = {NLM}, + pmc = {PMC1175362}, + pmid = {7504110}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-12}, +} + +@Article{morales-perez2016, + author = {Morales-Perez, C. L. and Noviello, C. M. and Hibbs, R. E.}, + title = {X-ray structure of the human α4β2 nicotinic receptor.}, + journal = {Nature}, + year = {2016}, + volume = {538}, + issue = {7625}, + month = oct, + pages = {411--415}, + issn = {1476-4687}, + doi = {10.1038/nature19785}, + abstract = {Nicotinic acetylcholine receptors are ligand-gated ion channels that mediate fast chemical neurotransmission at the neuromuscular junction and have diverse signalling roles in the central nervous system. The nicotinic receptor has been a model system for cell-surface receptors, and specifically for ligand-gated ion channels, for well over a century. In addition to the receptors' prominent roles in the development of the fields of pharmacology and neurobiology, nicotinic receptors are important therapeutic targets for neuromuscular disease, addiction, epilepsy and for neuromuscular blocking agents used during surgery. The overall architecture of the receptor was described in landmark studies of the nicotinic receptor isolated from the electric organ of Torpedo marmorata. Structures of a soluble ligand-binding domain have provided atomic-scale insights into receptor-ligand interactions, while high-resolution structures of other members of the pentameric receptor superfamily provide touchstones for an emerging allosteric gating mechanism. All available high-resolution structures are of homopentameric receptors. However, the vast majority of pentameric receptors (called Cys-loop receptors in eukaryotes) present physiologically are heteromeric. Here we present the X-ray crystallographic structure of the human α4β2 nicotinic receptor, the most abundant nicotinic subtype in the brain. This structure provides insights into the architectural principles governing ligand recognition, heteromer assembly, ion permeation and desensitization in this prototypical receptor class.}, + chemicals = {Bridged Bicyclo Compounds, Heterocyclic, Ligands, Neurotransmitter Agents, Nicotinic Agonists, Pyridines, Receptors, Nicotinic, nicotinic receptor alpha4beta2, epibatidine}, + citation-subset = {IM}, + completed = {2017-03-07}, + country = {England}, + issn-linking = {0028-0836}, + keywords = {Binding Sites; Bridged Bicyclo Compounds, Heterocyclic, chemistry, metabolism; Crystallography, X-Ray; Humans; Ion Transport; Ligands; Models, Molecular; Neurotransmitter Agents, chemistry, metabolism; Nicotinic Agonists, chemistry, metabolism; Protein Structure, Quaternary; Pyridines, chemistry, metabolism; Receptors, Nicotinic, chemistry, metabolism}, + mid = {NIHMS812379}, + nlm-id = {0410462}, + owner = {NLM}, + pii = {nature19785}, + pmc = {PMC5161573}, + pmid = {27698419}, + pubmodel = {Print-Electronic}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{althoff2014, + author = {Althoff, T. and Hibbs, R. E. and Banerjee, S. and Gouaux, E.}, + title = {X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors.}, + journal = {Nature}, + year = {2014}, + volume = {512}, + issue = {7514}, + month = aug, + pages = {333--337}, + issn = {1476-4687}, + doi = {10.1038/nature13669}, + abstract = {Cys-loop receptors are neurotransmitter-gated ion channels that are essential mediators of fast chemical neurotransmission and are associated with a large number of neurological diseases and disorders, as well as parasitic infections. Members of this ion channel superfamily mediate excitatory or inhibitory neurotransmission depending on their ligand and ion selectivity. Structural information for Cys-loop receptors comes from several sources including electron microscopic studies of the nicotinic acetylcholine receptor, high-resolution X-ray structures of extracellular domains and X-ray structures of bacterial orthologues. In 2011 our group published structures of the Caenorhabditis elegans glutamate-gated chloride channel (GluCl) in complex with the allosteric partial agonist ivermectin, which provided insights into the structure of a possibly open state of a eukaryotic Cys-loop receptor, the basis for anion selectivity and channel block, and the mechanism by which ivermectin and related molecules stabilize the open state and potentiate neurotransmitter binding. However, there remain unanswered questions about the mechanism of channel opening and closing, the location and nature of the shut ion channel gate, the transitions between the closed/resting, open/activated and closed/desensitized states, and the mechanism by which conformational changes are coupled between the extracellular, orthosteric agonist binding domain and the transmembrane, ion channel domain. Here we present two conformationally distinct structures of C. elegans GluCl in the absence of ivermectin. Structural comparisons reveal a quaternary activation mechanism arising from rigid-body movements between the extracellular and transmembrane domains and a mechanism for modulation of the receptor by phospholipids. }, + chemicals = {Apoproteins, Chloride Channels, Cysteine Loop Ligand-Gated Ion Channel Receptors, Ligands, Phosphatidylcholines, glutamate-gated chloride channels, Glutamic Acid, Ivermectin, 1-palmitoyl-2-oleoylphosphatidylcholine}, + citation-subset = {IM}, + completed = {2014-09-15}, + country = {England}, + issn-linking = {0028-0836}, + keywords = {Allosteric Regulation, drug effects; Animals; Apoproteins, chemistry, metabolism; Binding Sites; Binding, Competitive, drug effects; Caenorhabditis elegans, chemistry; Cell Membrane, metabolism; Chloride Channels, chemistry, metabolism; Crystallography, X-Ray; Cysteine Loop Ligand-Gated Ion Channel Receptors, chemistry, metabolism; Drug Partial Agonism; Glutamic Acid, metabolism; Ion Channel Gating; Ivermectin, chemistry, metabolism, pharmacology; Ligands; Models, Molecular; Movement, drug effects; Phosphatidylcholines, chemistry, metabolism, pharmacology; Protein Binding; Protein Multimerization, drug effects; Protein Structure, Tertiary, drug effects; Structure-Activity Relationship}, + mid = {NIHMS634520}, + nlm-id = {0410462}, + owner = {NLM}, + pii = {nature13669}, + pmc = {PMC4255919}, + pmid = {25143115}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-01-08}, +} + +@Article{du2015, + author = {Du, J. and Lü, W. and Wu, S. and Cheng, Y. and Gouaux, E.}, + title = {Glycine receptor mechanism elucidated by electron cryo-microscopy.}, + journal = {Nature}, + year = {2015}, + volume = {526}, + issue = {7572}, + month = oct, + pages = {224--229}, + issn = {1476-4687}, + doi = {10.1038/nature14853}, + abstract = {The strychnine-sensitive glycine receptor (GlyR) mediates inhibitory synaptic transmission in the spinal cord and brainstem and is linked to neurological disorders, including autism and hyperekplexia. Understanding of molecular mechanisms and pharmacology of glycine receptors has been hindered by a lack of high-resolution structures. Here we report electron cryo-microscopy structures of the zebrafish α1 GlyR with strychnine, glycine, or glycine and ivermectin (glycine/ivermectin). Strychnine arrests the receptor in an antagonist-bound closed ion channel state, glycine stabilizes the receptor in an agonist-bound open channel state, and the glycine/ivermectin complex adopts a potentially desensitized or partially open state. Relative to the glycine-bound state, strychnine expands the agonist-binding pocket via outward movement of the C loop, promotes rearrangement of the extracellular and transmembrane domain 'wrist' interface, and leads to rotation of the transmembrane domain towards the pore axis, occluding the ion conduction pathway. These structures illuminate the GlyR mechanism and define a rubric to interpret structures of Cys-loop receptors. }, + chemicals = {Neurotransmitter Agents, Protein Subunits, Receptors, Glycine, glycine receptor alpha1, Ivermectin, Strychnine, Glycine}, + citation-subset = {IM}, + completed = {2016-03-30}, + country = {England}, + issn-linking = {0028-0836}, + keywords = {Allosteric Regulation; Animals; Binding Sites; Cryoelectron Microscopy; Glycine, metabolism, pharmacology; Ion Channel Gating, drug effects; Ivermectin, metabolism, pharmacology; Models, Molecular; Neurotransmitter Agents, metabolism, pharmacology; Protein Conformation, drug effects; Protein Subunits, chemistry, drug effects, metabolism; Receptors, Glycine, agonists, antagonists & inhibitors, metabolism, ultrastructure; Rotation; Signal Transduction; Strychnine, metabolism, pharmacology; Zebrafish}, + mid = {NIHMS727941}, + nlm-id = {0410462}, + owner = {NLM}, + pii = {nature14853}, + pmc = {PMC4659708}, + pmid = {26344198}, + pubmodel = {Print-Electronic}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{monod1965, + author = {Monod, J. and Wyman, J. and Changeux, Jean-P.}, + title = {On the nature of allosteric transitions: a plausible model}, + journal = {J Mol Biol}, + year = {1965}, + volume = {12}, + number = {1}, + pages = {88--118}, +} + +@Article{lindblom2006, + author = {Lindblom, T. H. and Dodd, A. K.}, + title = {Xenobiotic detoxification in the nematode Caenorhabditis elegans}, + journal = {Journal of Experimental Zoology Part A: Comparative Experimental Biology}, + year = {2006}, + volume = {305}, + number = {9}, + pages = {720--730}, + publisher = {Wiley Online Library}, +} + +@InCollection{dalliere2017, + author = {Dalli{\`e}re, N. and Holden-Dye, L. and Dillon, J. and O'Connor, V. and Walker, R. J.}, + title = {Caenorhabditis elegans Feeding Behaviors}, + booktitle = {Oxford Research Encyclopedia of Neuroscience}, + year = {2017}, + __markedentry = {[monik:]}, +} + +\begin{filecontents}{\august.bib} + +@IEEEtranBSTCTL{IEEEexample:BSTcontrol, + ctldash_repeated_names = {no}, +} + +@Article{han2000, + author = {Han, H. and Yang, Shi-H. and Phillips, W. D.}, + title = {Overexpression of rapsyn modifies the intracellular trafficking of acetylcholine receptors}, + journal = {Journal of neuroscience research}, + year = {2000}, + volume = {60}, + number = {2}, + pages = {155--163}, + __markedentry = {[monik:6]}, + publisher = {Wiley Online Library}, +} + +@MastersThesis{Visvanathan2015, + author = {Visvanathan, Archunan}, + title = {The influence of the MuSK system and the L25 transgene on the Neuromuscular Junction}, + year = {2015}, + __markedentry = {[monik:6]}, + school = {University of Sydney}, +} + @Comment{jabref-meta: databaseType:biblatex;} diff --git a/bib/august.bib.bak b/bib/august.bib.bak index 2c09bedac69798f2df8affdb3de0c1f1ce606e78..02739d2ec70e3fb6add90486c197aaf50e58bc55 100644 --- a/bib/august.bib.bak +++ b/bib/august.bib.bak @@ -1739,7 +1739,7 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf}, } @Article{hilf2009, - author = {Hilf, R. J. and Dutzler, R.}, + author = {Hilf, R. J. C. and Dutzler, R.}, title = {Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel}, journal = {Nature}, year = {2009}, @@ -1749,8 +1749,8 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf}, issn = {1476-4687 (Electronic) 0028-0836 (Linking)}, doi = {10.1038/nature07461}, - type = {Journal Article}, url = {http://www.ncbi.nlm.nih.gov/pubmed/18987630}, + type = {Journal Article}, } @Article{hille1978, @@ -1818,7 +1818,7 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf}, } @Article{huang1999, - author = {Huang, Y. and Williamson, M. S. and Devonshire, A. L. and Windass, J. D. and Lansdell, S. J. and Millar, N. S.}, + author = {Huang, Y. and Williamson, M. and Devonshire, A. L. and Windass, J. D. and Lansdell, S. J. and Millar, N. S.}, title = {Molecular characterization and imidacloprid selectivity of nicotinic acetylcholine receptor subunits from the peach-potato aphid Myzus persicae}, journal = {Journal of Neurochemistry}, year = {1999}, @@ -4014,9 +4014,8 @@ http://www.nature.com/nature/journal/v423/n6943/pdf/nature01748.pdf}, pages = {2017--23}, issn = {0261-4189 (Print) 0261-4189 (Linking)}, + url = {http://www.ncbi.nlm.nih.gov/pmc/articles/PMC556666/pdf/emboj00091-0029.pdf}, type = {Journal Article}, - url = {http://www.ncbi.nlm.nih.gov/pubmed/1376242 -http://www.ncbi.nlm.nih.gov/pmc/articles/PMC556666/pdf/emboj00091-0029.pdf}, } @Article{sims1994, @@ -4674,9 +4673,8 @@ http://jcb.rupress.org/content/111/6/2623.full.pdf}, pages = {1101--24}, issn = {0022-2836 (Print) 0022-2836 (Linking)}, + url = {http://www.sciencedirect.com/science/article/pii/S0022283683711071}, type = {Journal Article}, - url = {http://www.ncbi.nlm.nih.gov/pubmed/8445638 -http://www.sciencedirect.com/science/article/pii/S0022283683711071}, } @Article{unwin1995, @@ -8002,17 +8000,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, publisher = {Elsevier}, } -@Article{jones2007b, - author = {Jones, A. K. and Davis, P. and Hodgkin, J. and Sattelle, D. B.}, - title = {The nicotinic acetylcholine receptor gene family of the nematode Caenorhabditis elegans: an update on nomenclature}, - journal = {Invertebrate Neuroscience}, - year = {2007}, - volume = {7}, - number = {2}, - pages = {129--131}, - publisher = {Springer}, -} - @Article{taylor1978, author = {Taylor, A. L. and Sasser, J. N.}, title = {Biology, identification and control of root-knot nematodes}, @@ -11049,17 +11036,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, publisher = {Rockefeller University Press}, } -@Article{hilf2008a, - author = {Hilf, Ricarda JC and Dutzler, Raimund}, - title = {X-ray structure of a prokaryotic pentameric ligand-gated ion channel}, - journal = {Nature}, - year = {2008}, - volume = {452}, - number = {7185}, - pages = {375}, - publisher = {Nature Publishing Group}, -} - @Article{tamkun1986, author = {Tamkun, John W and DeSimone, Douglas W and Fonda, Deborah and Patel, Ramila S and Buck, Clayton and Horwitz, Alan F and Hynes, Richard O}, title = {Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin}, @@ -12620,7 +12596,7 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, } @Article{alkondon2000, - author = {Alkondon, M and Pereira, E F and Eisenberg, H M and Albuquerque, E X}, + author = {Alkondon, M. and Pereira, E. F. and Eisenberg, H. M. and Albuquerque, E. X.}, title = {Nicotinic receptor activation in human cerebral cortical interneurons: a mechanism for inhibition and disinhibition of neuronal networks.}, journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, year = {2000}, @@ -14835,7 +14811,7 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, } @Online{eu2019a, - author = {The European Commission}, + author = {The European Commission.}, title = {EU Pesticides database. Entry for Sulfoxaflor.}, year = {Accessed 01 Sep 2019}, date = {2019}, @@ -16406,7 +16382,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, pages = {469--478}, issn = {0748-2337}, doi = {10.1177/074823378800400406}, - __markedentry = {[monik:]}, abstract = {The acute lethality of the salts of eight metals--HgCl2, BeSO4.4H2O, Al(NO3)3.9H2O, CuCl2.2H2O, ZnCl2, Pb(NO3)2, CdCl2, and Sr(NO3)2--was determined using a type of free-living nematode, Caenorhabditis elegans. The LC50 values were compared to the published mammalian oral LD50 values for salts of the same metals. Within this set of chemicals, C. elegans was found to be a predictor of mammalian acute lethality, generating LC50 values parallel to the rat and mouse LD50 values. The total expenses for this testing are about 10% of the cost for mammalian acute lethality testing. The method is considered to have great promise, but further study is needed.}, chemicals = {Metals}, citation-subset = {IM}, @@ -16433,7 +16408,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, pages = {248--256}, issn = {0041-008X}, doi = {10.1016/j.taap.2003.09.013}, - __markedentry = {[monik:6]}, abstract = {Fifteen organic phosphate pesticides were tested by computer tracking for their acute behavioral toxicity with the nematode Caenorhabditis elegans. Thirteen of these 15 chemicals are used as insecticides and are anticholesterase agents. The other two chemicals are used as herbicides. EC50 values for each chemical were compared to the corresponding LD50 acute lethality value in rats and mice. Order of toxicity was found to be significantly correlated in comparisons of C. elegans to both rats and mice. Mechanistic investigations were conducted by assaying 8 of the 15 chemicals for anticholinesterase activity in C. elegans. Significant cholinesterase inhibition was confirmed for five chemicals that had displayed high behavioral toxicity, while three chemicals of low behavioral toxicity showed no significant decrease in cholinesterase activity. Toxicity for two chemicals that do not inhibit cholinesterase in mammals was linked to pH effects. Detailed comparison of individual chemicals and metabolic issues are discussed. These results have positive implications for the use of C. elegans as a mammalian neurological model and support the use of C. elegans in early rounds of chemical toxicity screening.}, chemicals = {Cholinesterase Inhibitors, Insecticides, Organophosphorus Compounds, Cholinesterases}, citation-subset = {IM}, @@ -16450,4 +16424,922 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf}, revised = {2006-11-15}, } +@Article{buchner1986, + author = {Buchner, E. and Buchner, S. and Crawford, G. and Mason, W. T. and Salvaterra, P. M. and Sattelle, D. B.}, + title = {Choline acetyltransferase-like immunoreactivity in the brain of Drosophila melanogaster}, + journal = {Cell and Tissue Research}, + year = {1986}, + date = {1986-10-01}, + volume = {246}, + number = {1}, + month = oct, + pages = {57}, + issn = {1432-0878}, + doi = {10.1007/BF00218999}, + url = {http://dx.doi.org/10.1007/BF00218999}, + abstract = {SummaryUsing a monoclonal antibody selective for the acetylcholine (ACh)-synthesizing enzyme choline acetyltransferase (ChAT) of Drosophila melanogaster we find ChAT-like immunoreactivity in specific synaptic regions throughout the brain of Drosophila melanogaster apart from the lobes and the peduncle of the mushroom body and most of the first visual neuropile (lamina). Several anatomically well-defined central brain structures exhibit particularly strong binding. Characteristic differential staining patterns are observed for each of the four neuromeres of the optic lobes. Cell bodies appear not to bind this antibody. The prominent features of the distribution of ChAT-like immunoreactivity are paralleled by the distribution of acetylcholine hydrolyzing enzymatic activity as revealed by histochemical staining for acetylcholine esterase (AChE). These results are discussed in comparison with published data on enzyme distribution, choline uptake and ACh receptor binding in the nervous system of Drosophila melanogaster.}, + publisher = {Springer}, +} + +@Article{geffard1985, + author = {Geffard, M. and Vieillemaringe, J. and Heinrich-Rock, A. M. and Duris, P.}, + title = {Anti-acetylcholine antibodies and first immunocytochemical application in insect brain.}, + journal = {Neurosci Lett}, + year = {1985}, + date = {1985}, + volume = {4}, + number = {57}, + issue = {1}, + pages = {1-6}, +} + +@Article{lutz1987, + author = {Lutz, E. M. and Tyrer, N. M.}, + title = {Immunohistochemical localization of choline acetyltransferase in the central nervous system of the locust.}, + journal = {Brain research}, + year = {1987}, + volume = {407}, + issue = {1}, + month = mar, + pages = {173--179}, + issn = {0006-8993}, + doi = {10.1016/0006-8993(87)91234-0}, + abstract = {Immunohistochemistry of the locust central nervous system with antibody to choline acetyltransferase (ChAT) purified from the same species shows: first, there are relatively few immunoreactive cell bodies in the CNS; and second, sensory neuropiles, such as the ventral association centre and the ventral VAC (vVAC), the anterior ring tract, the tritocerebrum and the antennal lobe, are immunoreactive. That ChAT is contained in sensory neurones is suggested by immunoreactivity found in peripheral neurone cell bodies. These results indicate that acetylcholine serves primarily as a sensory transmitter in the locust.}, + chemicals = {Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1987-07-14}, + country = {Netherlands}, + issn-linking = {0006-8993}, + keywords = {Animals; Central Nervous System, enzymology; Choline O-Acetyltransferase, analysis; Ganglia, enzymology; Grasshoppers, enzymology; Histocytochemistry; Immunoenzyme Techniques; Interneurons, enzymology; Neurons, Afferent, enzymology}, + nlm-id = {0045503}, + owner = {NLM}, + pii = {0006-8993(87)91234-0}, + pmid = {3555698}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-14}, +} + +@Article{ellman1961, + author = {Ellman, G. L. and Featherstone, R. M.}, + title = {A new and rapid colorimetric determination of acetylcholinesterase activity}, + journal = {Biochemical Pharmacology}, + date = {1961}, + volume = {7}, + issue = {2}, + pages = {88-90}, +} + +@Article{barber1989, + author = {Barber, R. P. and Sugihara, H. and Lee, M. and Vaughn, J. E. and Salvaterra, P. M.}, + title = {Localization of Drosophila neurons that contain choline acetyltransferase messenger RNA: an in situ hybridization study.}, + journal = {The Journal of comparative neurology}, + year = {1989}, + volume = {280}, + issue = {4}, + month = feb, + pages = {533--543}, + issn = {0021-9967}, + doi = {10.1002/cne.902800404}, + abstract = {In situ hybridization with radiolabeled complementary RNA (cRNA) probes was used to determine the location of the messenger RNA (mRNA) encoding choline acetyltransferase (ChAT) in Drosophila nervous system. Areas in the cell-rich cortical regions of the cerebrum and optic lobes hybridized with substantial concentrations of the probe. This contrasted with the cell-sparse neuropil areas where no significant concentrations of probe were observed. Although most of the cortical regions were substantially labeled, there were regions within all of the areas where labeling was sparse or nonexistent. For example in the lamina, even though the monopolar cell layer appeared to be heavily labeled, there were some neuronal profiles that were not associated with the probe. Moreover, the epithelial glia that form an arch of cell profiles subjacent to the monopolar cells were not labeled, nor were amacrine neurons in the apex of the lamina near the external optic chiasma. The highest concentration of probe (approximately 140 grains/400 microns2) was observed in the laminar monopolar cell region and the cerebral cortical rind. The next most heavily labeled region (approximately 90 grains/400 microns2) occurred over cortical cells of the medulla-lobula. In the peripheral nervous system, label over the antennal sensory neurons amounted to about 75 grains/400 microns2, and the retinular cell layer of the compound eye exhibited about 60 grains/400 microns2. The control probe did not hybridize in significant quantities in either cellular or noncellular regions. This study presents evidence that large numbers of Drosophila cortical and primary sensory neurons contain the messenger RNA necessary for the production of ChAT, the acetylcholine-synthesizing enzyme. Further, our findings provide baseline information for use in ontogenetic studies of cholinergic neurons in Drosophila, and they also provide normative data for studying the effects of mutant alleles at the Cha or Ace loci upon the transcription of ChAT messenger RNA.}, + chemicals = {RNA, Messenger, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1989-06-02}, + country = {United States}, + issn-linking = {0021-9967}, + keywords = {Animals; Choline O-Acetyltransferase, metabolism; Cholinergic Fibers, cytology, metabolism; Drosophila melanogaster, anatomy & histology, metabolism; Nervous System, cytology, metabolism; Nucleic Acid Hybridization; RNA, Messenger, metabolism}, + nlm-id = {0406041}, + owner = {NLM}, + pmid = {2496152}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{yasuyama1999, + author = {Yasuyama, K. Salvaterra, P. M.}, + title = {Localization of choline acetyltransferase-expressing neurons in Drosophila nervous system.}, + journal = {Microsc Res Tech}, + date = {1999}, + volume = {15}, + number = {45}, + issue = {2}, + pages = {65-79}, +} + +@Article{hill1910, + author = {Hill, A. V.}, + title = {The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves}, + journal = {Journal of Physiology}, + date = {1910}, + volume = {40}, + pages = {4-7}, +} + +@Article{hall1976, + author = {Hall, J. C. and Kankel, D. R.}, + title = {Genetics of acetylcholinesterase in Drosophila melanogaster.}, + journal = {Genetics}, + year = {1976}, + volume = {83}, + issue = {3 PT.2}, + month = jul, + pages = {517--535}, + issn = {0016-6731}, + abstract = {Genes in Drosophila melanogaster that control acetylcholinesterase (AChE) were searched for by segmental aneuploidy techniques. Homogenates of flies containing duplications or deletions for different segments were assayed for enzyme activity. A region on the third chromosome was found for which flies having one dose consistently gave lower AChE activity than euploid flies, which in turn had lower activity than flies with three doses. The activity differences were in the approximate ratio 1:2:3. Fine structure deletion mapping within this region revealed a very small segment for which one-dose flies have approximately half-normal activity. To obtain putative AchE-null mutations, lethal mutations within this region were assayed. Four allelic lethals have approximately half-normal activity in heterozygous condition. These lethals probably define the structural locus (symbol: Ace) for AchE.}, + chemicals = {Acetylcholinesterase}, + citation-subset = {IM}, + completed = {1976-10-20}, + country = {United States}, + issn-linking = {0016-6731}, + keywords = {Acetylcholinesterase, metabolism; Aneuploidy; Animals; Chromosome Aberrations; Drosophila melanogaster, enzymology; Genes; Genes, Lethal; Genes, Recessive; Genotype; Phenotype}, + nlm-id = {0374636}, + owner = {NLM}, + pmc = {PMC1213530}, + pmid = {821817}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{greenspan1980, + author = {Greenspan, R. J. and Finn, J. A. and Hall, J. C.}, + title = {Acetylcholinesterase mutants in Drosophila and their effects on the structure and function of the central nervous system.}, + journal = {The Journal of comparative neurology}, + year = {1980}, + volume = {189}, + issue = {4}, + month = feb, + pages = {741--774}, + issn = {0021-9967}, + doi = {10.1002/cne.901890409}, + abstract = {Mutations that eliminate acetylcholinesterase (AChE) activity were used to study the effects of disrupted acetylcholine metabolism on the form and function of the central nervous system in Drosophila melanogaster. Mutants in the Ace gene, which have no AChE activity, usually die in early development, but the postembryonic effects of this lesion can be studied in genetic mosaics, or with conditional mutants. Adult mosaics, which expressed Ace mutations in part of their CNS, exhibited morphological defects in any ganglionic neuropile whose cells were mutant. The defects included reduction in ganglionic volume, a condensed appearance, and for a very large clone, degeneration. Examination of many such mosaics indicated that small clones restricted to one side of the CNS were not usually lethal. However, mosaics with large clones, with clones on either side of the posterior slope of the protocerebrum, or with clones encompassing symmetrical structures on both sides of the CNS rarely survived to adulthood. Mosaics with AChE-null tissue on either side of the optic lobes or the posterior-inferior protocerebrum had marked deficits in optomotor behavior, although they were outwardly normal in their movement and posture. Mosaics with Ace mutant tissue in the first-order optic lobe, the lamina, lacked a synaptic component of the electroretinogram, the "off" transient. Tests of courtship behavior revealed that AChE mosaics with mutant clones in the superior protocerebrum were often capable of demonstrating male courtship. However, their behavior was quantitatively and perhaps qualitatively deficient. In order to study critical periods for the effects of mutant AChE, temperature-sensitive mutations of the Ace gene were isolated. Flies bearing certain of these new mutations produced AchE activity that was thermolabile in vivo and in vitro. The critical period during which the mutants were most susceptible to conditional lethality was late in embryogenesis.}, + chemicals = {Acetylcholinesterase}, + citation-subset = {IM}, + completed = {1980-08-15}, + country = {United States}, + issn-linking = {0021-9967}, + keywords = {Acetylcholinesterase, deficiency, genetics, physiology; Animals; Drosophila melanogaster, physiology; Electroretinography; Female; Genes, Lethal; Male; Mosaicism; Movement; Mutation; Nervous System, enzymology; Retina, physiology; Sexual Behavior, Animal, physiology; Temperature}, + nlm-id = {0406041}, + owner = {NLM}, + pmid = {6769980}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2006-11-15}, +} + +@Article{slemmon1982, + author = {Slemmon, J. R. and Salvaterra, P. M. and Crawford, G. D. and Roberts, E.}, + title = {Purification of choline acetyltransferase from Drosophila melanogaster.}, + journal = {The Journal of biological chemistry}, + year = {1982}, + volume = {257}, + issue = {7}, + month = apr, + pages = {3847--3852}, + issn = {0021-9258}, + abstract = {Choline acetyltransferase (EC 2.3.1.6) from Drosophila melanogaster (Canton S, wild type) was purified 12,500-fold to a final specific activity of 500 mumol min-1 mg protein-1. The purification used homogenized fly heads and consisted of polyethylene glycol precipitation, DEAE-Bio-Gel A chromatography, Octyl-Sepharose chromatography, and affinity chromatography using solid phase Green A-agarose. The molecular weight of the native enzyme, as determined by molecular exclusion chromatography, was approximately 67,000 daltons. The final enzyme preparation showed two major protein bands at 67,000 and 54,000 daltons on polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS). After molecular exclusion chromatography, both SDS gel bands were present in the single symmetrical peak that contained the enzyme activity. Two-dimensional tryptic peptide maps prepared from the individual SDS gel bands indicated that they have very similar primary structures. Both SDS gel bands were precipitated by two different monoclonal antibodies derived against Drosophila choline acetyltransferase activity. The structural and immunological relatedness of the two SDS gel bands indicates that the enzyme is essentially homogeneous and that, in the native state, it may consist of more than one polypeptide chain.}, + chemicals = {Antigen-Antibody Complex, Immune Sera, Peptide Fragments, Choline O-Acetyltransferase, Trypsin}, + citation-subset = {IM}, + completed = {1982-05-27}, + country = {United States}, + issn-linking = {0021-9258}, + keywords = {Amino Acid Sequence; Animals; Antigen-Antibody Complex; Choline O-Acetyltransferase, isolation & purification, metabolism; Drosophila melanogaster, enzymology; Immune Sera; Kinetics; Molecular Weight; Peptide Fragments, analysis; Trypsin}, + nlm-id = {2985121R}, + owner = {NLM}, + pmid = {6801053}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{Driskell1978, + author = {Driskell, W J and Weber, B H and Roberts, E}, + title = {Purification of choline acetyltransferase from Drosophila melanogaster.}, + journal = {Journal of neurochemistry}, + year = {1978}, + volume = {30}, + issue = {5}, + month = may, + pages = {1135--1141}, + issn = {0022-3042}, + doi = {10.1111/j.1471-4159.1978.tb12408.x}, + chemicals = {Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1978-08-28}, + country = {England}, + issn-linking = {0022-3042}, + keywords = {Animals; Choline O-Acetyltransferase, isolation & purification; Drosophila melanogaster, enzymology; Drug Stability; Kinetics}, + nlm-id = {2985190R}, + owner = {NLM}, + pmid = {96214}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-30}, +} + +@Article{chao1980, + author = {Chao, L P}, + title = {Choline acetyltransferase: purification and characterization.}, + journal = {Journal of neuroscience research}, + year = {1980}, + volume = {5}, + issue = {2}, + pages = {85--115}, + issn = {0360-4012}, + doi = {10.1002/jnr.490050202}, + chemicals = {Isoenzymes, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1980-10-24}, + country = {United States}, + issn-linking = {0360-4012}, + keywords = {Animals; Brain, enzymology; Cattle; Chemical Phenomena; Chemistry; Choline O-Acetyltransferase, antagonists & inhibitors, immunology, isolation & purification; Cockroaches, enzymology; Decapodiformes, enzymology; Drosophila melanogaster, enzymology; Enzyme Activation; Female; Fishes, metabolism; Horseshoe Crabs, enzymology; Humans; Isoenzymes, isolation & purification; Kinetics; Methods; Mice; Placenta, enzymology; Pregnancy; Rats; Snails, enzymology}, + nlm-id = {7600111}, + owner = {NLM}, + pmid = {6772798}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2008-11-21}, +} + +@Article{Tellam2003, + author = {Tellam, R L and Vuocolo, T and Eisemann, C and Briscoe, S and Riding, G and Elvin, C and Pearson, R}, + title = {Identification of an immuno-protective mucin-like protein, peritrophin-55, from the peritrophic matrix of Lucilia cuprina larvae.}, + journal = {Insect biochemistry and molecular biology}, + year = {2003}, + volume = {33}, + issue = {2}, + month = feb, + pages = {239--252}, + issn = {0965-1748}, + abstract = {A mucin-like glycoprotein, peritrophin-55 was isolated and purified from the peritrophic matrix of Lucilia cuprina larvae. When injected into sheep, peritrophin-55 induced an immune response that inhibited larval growth by 51-66% when larvae subsequently fed on sera from the vaccinated sheep. The protein may have potential use as an immunogen probably accompanying other antigens to protect sheep from the cutaneous myiasis caused by these larvae. Peritrophin-55 was uniformly distributed throughout the peritrophic matrix where it probably lubricates the surface of the peritrophic matrix and protects the midgut from invasion by bacteria. The protein consists of an 8-cysteine amino-terminal domain (peritrophin-B domain) and a carboxy-terminal proline and threonine-rich domain with high probability for extensive O-linked glycosylation. The gene consists of two exons separated by a small intron. Peritrophin-55 mRNA was only detected in the larval cardia and midgut and to a minor extent in the hindgut. Sequence upstream of the transcriptional start site contained a putative promoter region, sequence similar to an ecdysone response element, sequence related to the Drosophila transposon S element and a tetranucleotide repeat region. A putative Drosophila melanogaster ortholog or paralog of peritrophin-55 (CG7714) was located within a 3458 bp intron of the Cha gene (choline-O-acetyltransferase), but on the opposite strand. Comparison of the putative promoter regions of the peritrophin-55 and CG7714 genes revealed little similarity except for a small semi-conserved sequence that is suggestive of a common transcription factor-binding site possibly contributing to the highly restricted developmental and tissue-specific expression patterns of these genes.}, + chemicals = {Insect Proteins, Membrane Glycoproteins, Mucins, Peptide Fragments, peritrophin-55 protein, Lucilia cuprina}, + citation-subset = {IM}, + completed = {2003-04-17}, + country = {England}, + issn-linking = {0965-1748}, + keywords = {Amino Acid Sequence; Animals; Base Sequence; Diptera, immunology; Insect Proteins, chemistry, genetics, isolation & purification; Larva; Membrane Glycoproteins, chemistry, genetics, isolation & purification; Molecular Sequence Data; Mucins, isolation & purification; Peptide Fragments, chemistry; Reverse Transcriptase Polymerase Chain Reaction}, + nlm-id = {9207282}, + owner = {NLM}, + pii = {S0965174802002084}, + pmid = {12535682}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2006-11-15}, +} + +@Article{hsiao2004, + author = {Hsiao, Y. and Lai, J. and Liao, Hsiu-Y. and Feng, Hai-T.}, + title = {Purification and characterization of acetylcholinesterase from oriental fruit fly [Bactrocera dorsalis (Hendel)](Diptera: Tephritidae)}, + journal = {Journal of agricultural and food chemistry}, + year = {2004}, + volume = {52}, + number = {17}, + pages = {5340--5346}, + publisher = {ACS Publications}, +} + +@Article{harel2000, + author = {Harel, M. and Kryger, G. and Rosenberry, T. L. and Mallender, W. D. and Lewis, T. and Fletcher, R. J. and Guss, J. M. and Silman, I. and Sussman, J. L.}, + title = {Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors}, + journal = {Protein Science}, + year = {2000}, + volume = {9}, + number = {6}, + pages = {1063--1072}, + publisher = {Cambridge University Press}, +} + +@Article{kerkut1970, + author = {Kerkut, G. A. and Oliver, G. W. O. and Rick, J. T. and Walker, R. J.}, + title = {The effects of drugs on learning in a simple preparation}, + journal = {Comparative and general pharmacology}, + year = {1970}, + volume = {1}, + number = {4}, + pages = {437--484}, + publisher = {Elsevier}, +} + +@Article{carlyle1963, + author = {Carlyle, R. F.}, + title = {The mode of action of neostigmine and physostigmine on the guinea-pig trachealis muscle}, + journal = {British journal of pharmacology and chemotherapy}, + year = {1963}, + volume = {21}, + number = {1}, + pages = {137--149}, + publisher = {Wiley Online Library}, +} + +@Article{greenspan1980b, + author = {Greenspan, R. J.}, + title = {Mutations of choline acetyltransferase and associated neural defects}, + journal = {Journal of comparative physiology}, + year = {1980}, + volume = {137}, + number = {1}, + pages = {83--92}, + publisher = {Springer}, +} + +@Article{pahud1998, + author = {Pahud, G. and Salem, N. and Van De Goor, J. and Medilanski, J. and Pellegrinelli, N. and Eder-Colli, L.}, + title = {Study of subcellular localization of membrane-bound choline acetyltransferase in Drosophila central nervous system and its association with membranes}, + journal = {European Journal of Neuroscience}, + year = {1998}, + volume = {10}, + number = {5}, + pages = {1644--1653}, + publisher = {Wiley Online Library}, +} + +@Article{lutz1988, + author = {Lutz, E. M. and Lloyd, S. J. and Tyrer, N. M.}, + title = {Purification of choline acetyltransferase from the locust Schistocerca gregaria and production of serum antibodies to this enzyme}, + journal = {Journal of neurochemistry}, + year = {1988}, + volume = {50}, + number = {1}, + pages = {82--89}, + publisher = {Wiley Online Library}, +} + +@Article{fabian1997, + author = {Fabian, R. and Seyfarth, Ernst-A.}, + title = {Acetylcholine and histamine are transmitter candidates in identifiable mechanosensitive neurons of the spider Cupiennius salei: an immunocytochemical study}, + journal = {Cell and tissue research}, + year = {1997}, + volume = {287}, + number = {2}, + pages = {413--423}, + publisher = {Springer}, +} + +@Article{kitamoto1998, + author = {Kitamoto, T. and Wang, W. and Salvaterra, P. M.}, + title = {Structure and organization of the Drosophila cholinergic locus.}, + journal = {The Journal of biological chemistry}, + year = {1998}, + volume = {273}, + issue = {5}, + month = jan, + pages = {2706--2713}, + issn = {0021-9258}, + doi = {10.1074/jbc.273.5.2706}, + abstract = {The Drosophila cholinergic locus is composed of two distinct genetic functions: choline acetyltransferase (ChAT; EC 2.3.1.6), the enzyme catalyzing biosynthesis of neurotransmitter acetylcholine (ACh), and the vesicular ACh transporter (VAChT), the synaptic vesicle membrane protein which pumps transmitter into vesicles. Both genes share a common first exon and the remainder of the VAChT gene contains a single coding exon residing entirely within the first intron of ChAT. RNase protection analysis indicates that all Drosophila VAChT specific transcripts contain the shared first exon and suggests common transcriptional control for ChAT and VAChT. Similar types of genomic organization have been evolutionarily conserved for cholinergic loci in nematodes and vertebrates, and may operate to ensure coordinate expression of these functionally related genes in the same cells. The relative levels of Drosophila ChAT and VAChT mRNA differ, however, in different tissues or in Cha mutants, indicating that independent regulation of ChAT and VAChT transcripts may occur post-transcriptionally. The predicted Drosophila VAChT protein is composed of 578 amino acids and contains 12 conserved putative transmembrane domains. Full-length VAChT cDNA is 7.2 kilobase long and has unusually long 5'- and 3'-untranslated regions (UTR). The 5'-UTR contains a GTG ChAT translational initiation codon along with three other potential ATG initiation codons. These features of the VAChT 5'-UTR region suggest that a ribosome scanning model may not be used for VAChT translation initiation.}, + chemicals = {Carrier Proteins, DNA, Complementary, Drosophila Proteins, Membrane Transport Proteins, Nerve Tissue Proteins, RNA Precursors, VAChT protein, Drosophila, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1998-02-23}, + country = {United States}, + issn-linking = {0021-9258}, + keywords = {Amino Acid Sequence; Animals; Base Sequence; Carrier Proteins, biosynthesis, genetics; Choline O-Acetyltransferase, biosynthesis, genetics; Cholinergic Fibers; DNA, Complementary, genetics; Drosophila Proteins; Drosophila melanogaster, genetics; Exons; Genomic Library; Introns; Membrane Transport Proteins; Molecular Sequence Data; Nerve Tissue Proteins, biosynthesis, genetics; Nucleic Acid Conformation; Protein Conformation; RNA Precursors, chemistry, genetics; RNA Processing, Post-Transcriptional; Sequence Homology, Amino Acid; Species Specificity; Transcription, Genetic; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins}, + nlm-id = {2985121R}, + owner = {NLM}, + pmid = {9446576}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-08}, +} + +@Article{song1997, + author = {Song, H. and Ming, G. and Fon, E. and Bellocchio, E. and Edwards, R. H. and Poo, M.}, + title = {Expression of a putative vesicular acetylcholine transporter facilitates quantal transmitter packaging.}, + journal = {Neuron}, + year = {1997}, + volume = {18}, + issue = {5}, + month = may, + pages = {815--826}, + issn = {0896-6273}, + doi = {10.1016/s0896-6273(00)80320-7}, + abstract = {A putative vesicular acetylcholine transporter (VAChT) was overexpressed in developing Xenopus spinal neurons by injection of rat VAChT cDNA or synthetic mRNA into Xenopus embryos. This resulted in a marked increase in the amplitude and frequency of miniature excitatory postsynaptic currents at neuromuscular synapses, reflecting an over 10-fold increase in the vesicular packaging of acetylcholine (ACh). The effect appeared in developing neurons even before synaptogenesis and was blocked by L-vesamicol, a specific blocker of ACh uptake into synaptic vesicles. Mutational studies showed that two highly conserved aspartate residues within putative transmembrane domains 4 and 10 are essential for the transport activity. These results provide direct evidence for the physiological function of a putative VAChT and demonstrate that quantal size can be regulated by changes in vesicular transporter activity.}, + chemicals = {Carrier Proteins, Membrane Transport Proteins, Neuromuscular Depolarizing Agents, Piperidines, Slc18a3 protein, rat, Synaptophysin, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Aspartic Acid, vesamicol, Acetylcholine}, + citation-subset = {IM}, + completed = {1997-06-30}, + country = {United States}, + issn-linking = {0896-6273}, + keywords = {Acetylcholine, metabolism; Animals; Aspartic Acid, genetics; Blastomeres; Carrier Proteins, analysis, genetics, metabolism; Cells, Cultured; Embryo, Nonmammalian, chemistry, physiology; Female; Gene Expression Regulation, Developmental, physiology; Membrane Transport Proteins; Microinjections; Muscles, cytology; Mutagenesis, physiology; Nervous System, cytology; Neuromuscular Depolarizing Agents, pharmacology; Neurons, chemistry, physiology, ultrastructure; Patch-Clamp Techniques; Piperidines, pharmacology; Rats; Synapses, chemistry, physiology; Synaptic Transmission, drug effects, physiology; Synaptophysin, analysis; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins; Xenopus laevis}, + nlm-id = {8809320}, + owner = {NLM}, + pii = {S0896-6273(00)80320-7}, + pmid = {9182805}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-08-22}, +} + +@Article{varoqui1996, + author = {Varoqui, H. and Erickson, J. D.}, + title = {Active transport of acetylcholine by the human vesicular acetylcholine transporter.}, + journal = {The Journal of biological chemistry}, + year = {1996}, + volume = {271}, + issue = {44}, + month = nov, + pages = {27229--27232}, + issn = {0021-9258}, + doi = {10.1074/jbc.271.44.27229}, + abstract = {The characteristics of ATP-dependent transport of acetylcholine (ACh) in homogenates of pheochromocytoma (PC-12) cells stably transfected with the human vesicular acetylcholine transporter (VAChT) cDNA are described. The human VAChT protein was abundantly expressed in this line and appeared as a diffuse band with a molecular mass of approximately 75 kDa on Western blots. Vesicular [3H]ACh accumulation increased approximately 20 times over levels attained by the endogenous rat VAChT, expressed at low levels in control PC-12 cells. The transport of [3H]ACh by human VAChT was dependent upon the addition of exogenous ATP at 37 degrees C. Uptake was abolished by low temperature (4 degrees C), the proton ionophore carbonyl cyanide p-trifluoromethoxyphenylhydrazone (2.5 microM) and bafilomycin A1 (1 microM), a specific inhibitor of the vesicular H+-ATPase. The kinetics of [3H]ACh uptake by human VAChT were saturable, exhibiting an apparent Km of 0.97 +/- 0.1 mM and Vmax of 0.58 +/- 0.04 nmol/min/mg. Maximal steady-state levels of vesicular [3H]ACh accumulation were directly proportional to the concentration of substrate present in the medium with saturation occurring at approximately 4 mM. Uptake was stereospecifically inhibited by L-vesamicol with an IC50 of 14.7 +/- 1.5 nM. The apparent affinity (Kd) of [3H]vesamicol for human VAChT was 4.1 +/- 0.5 nM, and the Bmax was 8.9 +/- 0.6 pmol/mg. The turnover (Vmax/Bmax) of the human VAChT was approximately 65/min. This expression system should prove useful for the structure/function analysis of VAChT.}, + chemicals = {Carrier Proteins, Membrane Transport Proteins, Neuromuscular Depolarizing Agents, Piperidines, Recombinant Proteins, SLC18A3 protein, human, Slc18a3 protein, rat, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, vesamicol, Acetylcholine, Tetrabenazine}, + citation-subset = {IM}, + completed = {1996-12-26}, + country = {United States}, + issn-linking = {0021-9258}, + keywords = {Acetylcholine, metabolism; Adrenal Gland Neoplasms; Animals; Biological Transport, Active, drug effects; Carrier Proteins, biosynthesis, metabolism; Cytosol, metabolism; Humans; Kinetics; Membrane Transport Proteins; Neuromuscular Depolarizing Agents, metabolism, pharmacology; PC12 Cells; Pheochromocytoma; Piperidines, metabolism, pharmacology; Rats; Recombinant Proteins, biosynthesis, metabolism; Substrate Specificity; Tetrabenazine, metabolism, pharmacology; Transfection; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins}, + nlm-id = {2985121R}, + owner = {NLM}, + pmid = {8910293}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-08}, +} + +@Article{kitamoto2000, + author = {Kitamoto, T and Xie, X and Wu, C F and Salvaterra, P M}, + title = {Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster.}, + journal = {Journal of neurobiology}, + year = {2000}, + volume = {42}, + issue = {2}, + month = feb, + pages = {161--171}, + issn = {0022-3034}, + abstract = {The Drosophila vesicular acetylcholine transporter gene (Vacht) is nested within the first intron of the choline acetyltransferase gene (Cha). To isolate Vacht mutants, we performed an F(2) genetic screen and identified mutations that failed to complement Df(3R)Cha(5), a deletion lacking Cha and the surrounding genes. Of these mutations, three mapped to a small genomic region where Cha resides. Complementation tests with a Cha mutant allele and rescue experiments using a transgenic Vacht minigene have revealed that two of these three mutations are nonconditional lethal alleles of Vacht (Vacht(1) and Vacht(2) ). The other is a new temperature-sensitive allele of Cha (Cha(ts3) ). Newly isolated Vacht mutants were used to reexamine the existing Cha mutations. We found that all deficiencies uncovering Cha also lack Vacht function, reflecting the nested organization of the two genes. The effective lethal phase for Vacht(1) is the embryonic stage, whereas that for Vacht(2) is the larval stage. Viable first-instar larvae homozygous for Vacht(2) showed reduced motility. Adult flies heterozygous for Vacht mutations were found to have defective responses in the dorsal longitudinal muscles following high-frequency brain stimulation. Since cholinergic synapses have been shown to be involved in the giant fiber pathway that mediates this response, the result suggested that reduction in the Vacht activity to 50% causes an abnormality in cholinergic transmission when stressed by a high-frequency stimulus.}, + chemicals = {Carrier Proteins, Drosophila Proteins, Membrane Transport Proteins, VAChT protein, Drosophila, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {2000-02-08}, + country = {United States}, + issn-linking = {0022-3034}, + keywords = {Alleles; Animals; Blotting, Western; Brain, enzymology; Carrier Proteins, genetics, physiology; Choline O-Acetyltransferase, metabolism; Drosophila Proteins; Drosophila melanogaster, genetics, physiology; Electrophysiology; Female; Genes, Lethal; Heterozygote; Larva, genetics, physiology; Male; Membrane Transport Proteins; Motor Activity, genetics; Muscles, enzymology; Mutagenesis; Nerve Fibers, enzymology, physiology; Synapses, genetics, physiology; Temperature; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins}, + nlm-id = {0213640}, + owner = {NLM}, + pii = {10.1002/(SICI)1097-4695(20000205)42:2<161::AID-NEU1>3.0.CO;2-P}, + pmid = {10640324}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{karnovsky1964, + author = {Karnovsky, M. J. and Roots, L.}, + title = {A "direct-coloring thiocholine method for cholinesterase".}, + journal = {The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society}, + year = {1964}, + volume = {12}, + month = mar, + pages = {219--221}, + issn = {0022-1554}, + doi = {10.1177/12.3.219}, + chemicals = {Coloring Agents, Thiocholine, Copper, Cholinesterases, Choline}, + citation-subset = {OM}, + completed = {1996-12-01}, + country = {United States}, + issn-linking = {0022-1554}, + keywords = {Choline; Cholinesterases; Color; Coloring Agents; Copper; Histocytochemistry; Research; Staining and Labeling; Thiocholine; CHOLINE; CHOLINESTERASE; COPPER; EXPERIMENTAL LAB STUDY; HISTOCYTOCHEMISTRY; STAINS AND STAINING}, + nlm-id = {9815334}, + owner = {NLM}, + pmid = {14187330}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2018-12-01}, +} + +@Article{gorczyca1987, + author = {Gorczyca, M. G. and Hall, J. C.}, + title = {Immunohistochemical localization of choline acetyltransferase during development and in Chats mutants of Drosophila melanogaster.}, + journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, + year = {1987}, + volume = {7}, + issue = {5}, + month = may, + pages = {1361--1369}, + issn = {0270-6474}, + abstract = {The distribution of choline acetyltransferase (CAT) in the nervous system of Drosophila melanogaster was determined by indirect immunohistochemical procedures using a monoclonal antibody specific to the enzyme. Immunoreactivity was first detected in the nervous system of 16 hr embryos, and increased considerably by the end of embryogenesis. Neuropil was preferentially stained, though cell bodies could also be observed. Staining was prominent in the CNS of all 3 larval instars but decreased substantially during the mid-pupal stage. Prior to eclosion, the level of immunoreactivity increased and the adult staining pattern became discernible. In the adult brain, staining was extensive, with numerous structures, such as the optic lobes and mushroom bodies, staining strongly. The adult thoracic ganglia were also moderately immunoreactive. These results imply a wide distribution of cholinergic neurons in the CNS of Drosophila. Immunoreactivity was also determined for 2 temperature-sensitive CAT mutants, Chats1 and Chats2. These files exhibit reduced CAT activity at permissive temperature, 18 degrees C, which eventually falls to undetectable levels after incubation at nonpermissive temperature, 30 degrees C. Chats2 mutants, after incubation at either 18 or 30 degrees C displayed virtually no staining. This result indicated that the immunoreactivity observed in wild-type flies was specifically associated with the enzyme encoded by the Cha gene. The intensity of staining in Chats1 mutants incubated at 18 degrees C appeared greater than in control flies, even though CAT enzyme activity in Chats1 is lower. This suggests that the enzyme molecule itself is structurally altered in Chats1 mutants. After incubation at 30 degrees C, staining in Chats1 flies decreased but did not disappear.}, + chemicals = {Horseradish Peroxidase, Choline O-Acetyltransferase}, + citation-subset = {IM}, + completed = {1987-06-25}, + country = {United States}, + issn-linking = {0270-6474}, + keywords = {Animals; Central Nervous System, enzymology; Choline O-Acetyltransferase, analysis; Drosophila melanogaster, enzymology, genetics; Embryo, Nonmammalian; Histocytochemistry; Horseradish Peroxidase; Immunologic Techniques; Larva; Mutation; Neurons, enzymology; Pupa; Temperature}, + nlm-id = {8102140}, + owner = {NLM}, + pmid = {3106590}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2007-11-14}, +} + +@Article{sattelle1983, + author = {Sattelle, D. B. and Harrow, I. D. and Hue, B. and Pelhate, M. and Gepner, J. I. and Hall, L. M.}, + title = {$\alpha$-Bungarotoxin Blocks excitatory synaptic transmission between cercal sensory neurones and Giant Interneurone 2 of the cockroach, Peripianeta americana}, + journal = {Journal of experimental biology}, + year = {1983}, + volume = {107}, + number = {1}, + pages = {473--489}, + publisher = {The Company of Biologists Ltd}, +} + +@Article{daley1988, + author = {Daley, D. L. and Camhi, J. M.}, + title = {Connectivity pattern of the cercal-to-giant interneuron system of the American cockroach}, + journal = {Journal of neurophysiology}, + year = {1988}, + volume = {60}, + number = {4}, + pages = {1350--1368}, + publisher = {American Physiological Society Bethesda, MD}, +} + +@Article{scheidler1990, + author = {Scheidler, A. and Kaulen, P. and Briining, G. and Erber, J.}, + title = {Quantitative autoradiographic localization of [125I]α-bungarotoxin binding sites in the honeybee brain.}, + journal = {Brain Research}, + date = {1990}, + volume = {534}, + pages = {332-335}, +} + +@Article{schmidt-nielsen1977, + author = {Schmidt-Nielsen, B. K. and Gepner, J. I. and Teng, N. N. and Hall, L. M.}, + title = {Characterization of an alpha-bungarotoxin binding component from Drosophila melanogaster.}, + journal = {Journal of neurochemistry}, + year = {1977}, + volume = {29}, + issue = {6}, + month = dec, + pages = {1013--1029}, + issn = {0022-3042}, + doi = {10.1111/j.1471-4159.1977.tb06505.x}, + chemicals = {Bungarotoxins, Receptors, Cholinergic, Acetylcholine}, + citation-subset = {IM}, + completed = {1978-03-21}, + country = {England}, + issn-linking = {0022-3042}, + keywords = {Acetylcholine, pharmacology; Animals; Binding Sites; Brain Chemistry; Bungarotoxins, antagonists & inhibitors, metabolism; Dose-Response Relationship, Drug; Drosophila melanogaster; Kinetics; Methods; Receptors, Cholinergic, analysis; Synapses, analysis; Time Factors}, + nlm-id = {2985190R}, + owner = {NLM}, + pmid = {413880}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-30}, +} + +@Article{hildebrand1979, + author = {Hildebrand, J. G. and Hall, L. M. and Osmond, B. C.}, + title = {Distribution of binding sites for 125I-labeled alpha-bungarotoxin in normal and deafferented antennal lobes of Manduca sexta.}, + journal = {Proceedings of the National Academy of Sciences of the United States of America}, + year = {1979}, + volume = {76}, + issue = {1}, + month = jan, + pages = {499--503}, + issn = {0027-8424}, + doi = {10.1073/pnas.76.1.499}, + abstract = {125I-Labeled alpha-bungarotoxin has been used to determine the distribution of putative acetylcholine receptors in normal and chronically deafferented antennal lobes in the brain of the moth Manduca sexta. Toxin-binding sites are confined to synaptic regions in deafferented lobes. These findings suggest that receptors can develop in the insect central nervous system independently of normal synaptic influences.}, + chemicals = {Bungarotoxins, Receptors, Cholinergic}, + citation-subset = {IM}, + completed = {1979-05-26}, + country = {United States}, + issn-linking = {0027-8424}, + keywords = {Afferent Pathways; Animals; Brain, cytology, metabolism; Bungarotoxins, metabolism; Denervation; Lepidoptera, metabolism; Moths, metabolism; Receptors, Cholinergic, metabolism; Synapses, metabolism}, + nlm-id = {7505876}, + owner = {NLM}, + pmc = {PMC382969}, + pmid = {284367}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-01}, +} + +@Article{meyer1985, + author = {Meyer, M. R. and Reddy, G. R.}, + title = {Muscarinic and nicotinic cholinergic binding sites in the terminal abdominal ganglion of the cricket (Acheta domesticus).}, + journal = {Journal of neurochemistry}, + year = {1985}, + volume = {45}, + issue = {4}, + month = oct, + pages = {1101--1112}, + issn = {0022-3042}, + doi = {10.1111/j.1471-4159.1985.tb05529.x}, + abstract = {Cricket (Acheta domesticus) terminal abdominal ganglia (TG) contain high concentrations (approximately 2 pmol/mg protein) of muscarinic and nicotinic cholinergic binding sites, based on the capacity of TG to bind specifically the labelled ligands L-[3H]quinuclidinyl benzilate ([3H]QNB) and [125I]alpha-bungarotoxin ([125I]alpha-BGT) with high affinity. For both ligands, binding is saturable and reversible. Competitive displacement experiments indicate that the [3H]QNB and [125I]alpha-BGT binding sites probably represent pharmacologically distinct classes of putative TG acetylcholine receptors (AChRs). Results from physiological recording and autoradiographic localization experiments demonstrate that a portion of the putative nicotinic AChRs is localized in synaptic regions of the well-characterized cercal sensory-giant interneuron pathway in the TG, where they are likely to serve as functional synaptic AChRs. Unlike nicotinic ligands, muscarinic agents do not appear to be pharmacologically active in this pathway. Therefore, in the insect CNS, putative muscarinic and nicotinic AChRs coexist at high density, but can be pharmacologically distinguished from one another on the basis of criteria derived from both ligand binding and physiological methods.}, + chemicals = {Bungarotoxins, Receptors, Muscarinic, Receptors, Nicotinic, Quinuclidinyl Benzilate, Tubocurarine}, + citation-subset = {IM}, + completed = {1985-10-11}, + country = {England}, + issn-linking = {0022-3042}, + keywords = {Animals; Autoradiography; Binding, Competitive; Bungarotoxins, metabolism; Evoked Potentials; Ganglia, metabolism; Kinetics; Orthoptera; Quinuclidinyl Benzilate, metabolism; Receptors, Muscarinic, metabolism; Receptors, Nicotinic, metabolism; Synaptic Transmission; Tubocurarine, pharmacology}, + nlm-id = {2985190R}, + owner = {NLM}, + pmid = {2993520}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-06-30}, +} + +@Article{orr1990, + author = {Orr, G. L. and Orr, N. and Hollingworth, R. M.}, + title = {Localization and pharmacological characterization of nicotinic-cholinergic binding sites in cockroach brain using α- and neuronal bungarotoxin}, + journal = {Insect Biochemistry}, + date = {1990}, + volume = {20}, + issue = {6}, + pages = {557-566}, +} + +@Article{kerkut1969, + author = {Kerkut, G. A. and Pitman, R. M. and Walker, R. J.}, + title = {Iontophoretic application of acetylcholine and gaba onto insect central neurones.}, + journal = {Comparative Biochemistry and Physiology}, + date = {1969}, + volume = {31}, + issue = {4}, + pages = {611-612}, +} + +@Article{barbara2005, + author = {Barbara, Guillaume Stephane and Zube, Christina and Rybak, Jürgen and Gauthier, Monique and Grünewald, Bernd}, + title = {Acetylcholine, GABA and glutamate induce ionic currents in cultured antennal lobe neurons of the honeybee, Apis mellifera.}, + journal = {Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology}, + year = {2005}, + volume = {191}, + issue = {9}, + month = sep, + pages = {823--836}, + issn = {0340-7594}, + doi = {10.1007/s00359-005-0007-3}, + abstract = {The honeybee, Apis mellifera, is a valuable model system for the study of olfactory coding and its learning and memory capabilities. In order to understand the synaptic organisation of olfactory information processing, the transmitter receptors of the antennal lobe need to be characterized. Using whole-cell patch-clamp recordings, we analysed the ligand-gated ionic currents of antennal lobe neurons in primary cell culture. Pressure applications of acetylcholine (ACh), gamma-amino butyric acid (GABA) or glutamate induced rapidly activating ionic currents. The ACh-induced current flows through a cation-selective ionotropic receptor with a nicotinic profile. The ACh-induced current is partially blocked by alpha-bungarotoxin. Epibatidine and imidacloprid are partial agonists. Our data indicate the existence of an ionotropic GABA receptor which is permeable to chloride ions and sensitive to picrotoxin (PTX) and the insecticide fipronil. We also identified the existence of a chloride current activated by pressure applications of glutamate. The glutamate-induced current is sensitive to PTX. Thus, within the honeybee antennal lobe, an excitatory cholinergic transmitter system and two inhibitory networks that use GABA or glutamate as their neurotransmitter were identified.}, + chemicals = {Excitatory Amino Acid Agonists, Excitatory Amino Acid Antagonists, GABA Agonists, GABA Antagonists, Ion Channels, Nicotinic Agonists, Nicotinic Antagonists, Glutamic Acid, gamma-Aminobutyric Acid, Histamine, Acetylcholine, Epinephrine}, + citation-subset = {IM}, + completed = {2005-12-15}, + country = {Germany}, + issn-linking = {0340-7594}, + keywords = {Acetylcholine, pharmacology; Animals; Bees; Cells, Cultured; Dose-Response Relationship, Drug; Drug Interactions; Epinephrine, pharmacology; Excitatory Amino Acid Agonists, pharmacology; Excitatory Amino Acid Antagonists, pharmacology; GABA Agonists, pharmacology; GABA Antagonists; Glutamic Acid, pharmacology; Histamine, pharmacology; Ion Channels, physiology; Membrane Potentials, drug effects; Models, Neurological; Neurons, Afferent, drug effects, physiology; Nicotinic Agonists, pharmacology; Nicotinic Antagonists, pharmacology; Olfactory Pathways, cytology; Patch-Clamp Techniques, methods; Pupa; gamma-Aminobutyric Acid, pharmacology}, + nlm-id = {101141792}, + owner = {NLM}, + pmid = {16044331}, + pubmodel = {Print-Electronic}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{pumphrey1937, + author = {Pumphrey, R. J. and Rawdon-Smith, A. F.}, + title = {Synaptic transmission of nervous impulses through the last abdominal ganglion of the cockroach}, + journal = {Proceedings of the Royal Society of London. Series B-Biological Sciences}, + year = {1937}, + volume = {122}, + number = {826}, + pages = {106--118}, + publisher = {The Royal Society London}, +} + +@Article{Hoskins1940, + author = {Hoskins, W and others}, + title = {Recent contributions of insect physiology to insect toxicology and control}, + journal = {Hilgardia}, + year = {1940}, + volume = {13}, + number = {6}, + pages = {307--386}, + publisher = {University of California, Agriculture and Natural Resources}, +} + +@Article{Mongeau2015, + author = {Mongeau, Jean-Michel and Sponberg, Simon N and Miller, John P and Full, Robert J}, + title = {Sensory processing within cockroach antenna enables rapid implementation of feedback control for high-speed running maneuvers}, + journal = {Journal of Experimental Biology}, + year = {2015}, + volume = {218}, + number = {15}, + pages = {2344--2354}, + publisher = {The Company of Biologists Ltd}, +} + +@Article{sattelle1976, + author = {Sattelle, D. B. and McClay, A. S. and Dowson, R. J. and Callec, J. J.}, + title = {The pharmacology of an insect ganglion: actions of carbamylcholine and acetylcholine.}, + journal = {The Journal of experimental biology}, + year = {1976}, + volume = {64}, + issue = {1}, + month = feb, + pages = {13--23}, + issn = {0022-0949}, + abstract = {1. Methods for presenting dose-response data for the ganglionic actions of cholinergic agonists (e.g. carbamylcholine) are compared, using the mannitol-gap technique for electrophysiological recording of synaptic events at the cercal nerve, giant fibre synapse of the sixth abdominal ganglion of the cockroach Periplaneta americana. 2. At concentrations around 10(-5)M, carbamylcholine has no effect on ganglionic polarization but potentiates the monosynaptic EPSP. At 10(-4)M and higher concentrations, ganglionic depolarization is accompanied by a reduction of EPSP. 3. Pretreatment with eserine (10(-6) M) considerably shifts the dose-response curve for acetylcholine so that synaptic transmission is consistently sensitive to 10(-6) M acetylcholine.}, + chemicals = {Receptors, Cholinergic, Carbachol, Physostigmine, Acetylcholine}, + citation-subset = {IM}, + completed = {1976-08-02}, + country = {England}, + issn-linking = {0022-0949}, + keywords = {Acetylcholine, pharmacology; Animals; Carbachol, pharmacology; Dose-Response Relationship, Drug; Drug Interactions; Ganglia, drug effects, physiology; In Vitro Techniques; Membrane Potentials, drug effects; Periplaneta; Physostigmine, pharmacology; Receptors, Cholinergic; Synaptic Transmission}, + nlm-id = {0243705}, + owner = {NLM}, + pmid = {178820}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2015-11-19}, +} + +@Article{callec1973, + author = {Callec, J. J. and Sattelle, D. B.}, + title = {A simple technique for monitoring the synaptic actions of pharmacological agents.}, + journal = {The Journal of experimental biology}, + year = {1973}, + volume = {59}, + issue = {3}, + month = dec, + pages = {725--738}, + issn = {0022-0949}, + chemicals = {Acetylcholine}, + citation-subset = {IM}, + completed = {1974-02-22}, + country = {England}, + issn-linking = {0022-0949}, + keywords = {Acetylcholine, pharmacology; Action Potentials, drug effects; Animals; Axons, physiology; Cockroaches; Dose-Response Relationship, Drug; Electric Stimulation; Evoked Potentials, drug effects; Ganglia, drug effects, physiology; Methods; Perfusion; Sensory Receptor Cells, drug effects, physiology; Synapses, drug effects, physiology; Synaptic Transmission, drug effects}, + nlm-id = {0243705}, + owner = {NLM}, + pmid = {4357996}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2013-11-21}, +} + +@Article{goldberg1999, + author = {Goldberg, F. and Grünewald, B. and Rosenboom, H. and Menzel, R.}, + title = {Nicotinic acetylcholine currents of cultured Kkenyon cells from the mushroom bodies of the honey bee Aapis mellifera.}, + journal = {The Journal of physiology}, + year = {1999}, + volume = {514 ( Pt 3)}, + month = feb, + pages = {759--768}, + issn = {0022-3751}, + doi = {10.1111/j.1469-7793.1999.759ad.x}, + abstract = {1. Acetylcholine-induced currents of mushroom body Kenyon cells from the honey bee Apis mellifera were studied using the whole-cell configuration of the patch clamp technique. Pressure application of 1 mM acetylcholine (ACh) induced inward currents with amplitudes between -5 and -500 pA. 2. The cholinergic agonists ACh and carbamylcholine had almost equal potencies of current activation at concentrations between 0.01 and 1 mM; nicotine was less potent. The muscarinic agonist oxotremorine did not elicit any currents. 3. Approximately 80 % of the ACh-induced current was irreversibly blocked by 1 microM alpha-bungarotoxin. Atropine (1 mM) did not block the ACh-induced current. 4. Upon prolonged ACh application the current desensitized with a time course that could be approximated by the sum of two exponentials (tau1 = 276 +/- 45 ms (mean +/- s.e.m. ) for the fast component and tau2 = 2.4 +/- 0.7 s for the slow component). 5. Noise analyses of whole-cell currents yielded elementary conductances of 19.5 +/- 2.4 pS for ACh and 23.7 +/- 5.0 pS for nicotine. The channel lifetimes, calculated from the frequency spectra, were tauo = 1.8 ms for ACh and tauo = 2.5 ms for nicotine. 6. Raising the external calcium concentration from 5 to 50 mM shifted the reversal potential of the ACh-induced current from +4. 6 +/- 0.9 to +37.3 +/- 1.3 mV. The calcium-to-sodium permeability ratio (PCa : PNa) was 6.4. 7. In high external calcium solution (50 mM) the ACh-induced current rectified in an outward direction at positive membrane potentials. 8. We conclude that Kenyon cells express nicotinic ACh receptors with functional profiles reminiscent of the vertebrate neuronal nicotinic ACh receptor subtype.}, + chemicals = {Cholinergic Agonists, Nicotinic Agonists, Receptors, Nicotinic, Carbachol, Sodium, Calcium}, + citation-subset = {IM}, + completed = {1999-03-26}, + country = {England}, + issn-linking = {0022-3751}, + keywords = {Animals; Bees, metabolism; Calcium, metabolism; Carbachol, pharmacology; Cell Membrane, drug effects, metabolism; Cells, Cultured; Cholinergic Agonists, pharmacology; Electric Stimulation; Electrophysiology; Membrane Potentials, physiology; Nicotinic Agonists, pharmacology; Patch-Clamp Techniques; Receptors, Nicotinic, drug effects, metabolism; Sodium, metabolism}, + nlm-id = {0266262}, + owner = {NLM}, + pmc = {PMC2269090}, + pmid = {9882748}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-12}, +} + +@Article{albert1993, + author = {Albert, J. L. and Lingle, C. J.}, + title = {Activation of nicotinic acetylcholine receptors on cultured Drosophila and other insect neurones.}, + journal = {The Journal of physiology}, + year = {1993}, + volume = {463}, + month = apr, + pages = {605--630}, + issn = {0022-3751}, + doi = {10.1113/jphysiol.1993.sp019613}, + abstract = {1. Using whole-cell and single channel recordings, we have examined the properties of acetylcholine (ACh)-activated currents in neurones from larval and pupal Drosophila melanogaster (fruit fly), larval and embryonic Musca domestica (house fly), and nymphal Schistocerca gregaria (locust). 2. In all preparations, single channel recordings revealed two major classes of ACh-activated channels, with average conductances of approximately 32 and 59 pS. 3. At ACh concentrations from 1 to 10 microM, channel activity in Drosophila larval neurones occurs in bursts with an average of 1-2 openings. Open times and burst durations are described by one or two exponentials. Burst durations for the 32 pS channel (approximately 3 ms, slow component) were longer than those for the 59 pS channel (approximately 1.0 ms). The mean open interval duration for the 32 pS channel (slow component) was also longer than that of the 59 pS channel. 4. At high ACh (20-200 microM) concentrations, bursts of the smaller conductance channel occur in clusters separated by long-lived periods without channel activity. Considerable kinetic heterogeneity was observed among clusters. 5. The whole-cell dose-response curve suggests that activation of current by ACh increases up to at least 100 microM and that multiple ligand binding steps are involved. 6. Drosophila and Musca larval neuronal ACh-activated channels show some unique features in their cholinergic pharmacological properties: (a) they are only weakly activated by the potent neuromuscular nicotinic agonist suberyldicholine, (b) hexamethonium and decamethonium are weak, but approximately equi-effective blockers, and (c) alpha- and kappa-bungarotoxin (BTX) both blocked reversibly, though alpha-BTX appears to be the more potent inhibitor.}, + chemicals = {Decamethonium Compounds, Hexamethonium Compounds, Ion Channels, Receptors, Nicotinic, Tetrodotoxin, Mecamylamine, Trimethaphan, Chlorisondamine, Acetylcholine}, + citation-subset = {IM}, + completed = {1993-12-30}, + country = {England}, + issn-linking = {0022-3751}, + keywords = {Acetylcholine, pharmacology; Animals; Cells, Cultured; Chlorisondamine, pharmacology; Decamethonium Compounds, pharmacology; Drosophila melanogaster, metabolism; Grasshoppers; Hexamethonium Compounds, pharmacology; Houseflies; Insecta, metabolism; Ion Channels, drug effects, metabolism; Kinetics; Larva; Mecamylamine, pharmacology; Neurons, drug effects, metabolism; Pupa; Receptors, Nicotinic, drug effects, metabolism; Tetrodotoxin, pharmacology; Trimethaphan, pharmacology}, + nlm-id = {0266262}, + owner = {NLM}, + pmc = {PMC1175362}, + pmid = {7504110}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-05-12}, +} + +@Article{morales-perez2016, + author = {Morales-Perez, C. L. and Noviello, C. M. and Hibbs, R. E.}, + title = {X-ray structure of the human α4β2 nicotinic receptor.}, + journal = {Nature}, + year = {2016}, + volume = {538}, + issue = {7625}, + month = oct, + pages = {411--415}, + issn = {1476-4687}, + doi = {10.1038/nature19785}, + abstract = {Nicotinic acetylcholine receptors are ligand-gated ion channels that mediate fast chemical neurotransmission at the neuromuscular junction and have diverse signalling roles in the central nervous system. The nicotinic receptor has been a model system for cell-surface receptors, and specifically for ligand-gated ion channels, for well over a century. In addition to the receptors' prominent roles in the development of the fields of pharmacology and neurobiology, nicotinic receptors are important therapeutic targets for neuromuscular disease, addiction, epilepsy and for neuromuscular blocking agents used during surgery. The overall architecture of the receptor was described in landmark studies of the nicotinic receptor isolated from the electric organ of Torpedo marmorata. Structures of a soluble ligand-binding domain have provided atomic-scale insights into receptor-ligand interactions, while high-resolution structures of other members of the pentameric receptor superfamily provide touchstones for an emerging allosteric gating mechanism. All available high-resolution structures are of homopentameric receptors. However, the vast majority of pentameric receptors (called Cys-loop receptors in eukaryotes) present physiologically are heteromeric. Here we present the X-ray crystallographic structure of the human α4β2 nicotinic receptor, the most abundant nicotinic subtype in the brain. This structure provides insights into the architectural principles governing ligand recognition, heteromer assembly, ion permeation and desensitization in this prototypical receptor class.}, + chemicals = {Bridged Bicyclo Compounds, Heterocyclic, Ligands, Neurotransmitter Agents, Nicotinic Agonists, Pyridines, Receptors, Nicotinic, nicotinic receptor alpha4beta2, epibatidine}, + citation-subset = {IM}, + completed = {2017-03-07}, + country = {England}, + issn-linking = {0028-0836}, + keywords = {Binding Sites; Bridged Bicyclo Compounds, Heterocyclic, chemistry, metabolism; Crystallography, X-Ray; Humans; Ion Transport; Ligands; Models, Molecular; Neurotransmitter Agents, chemistry, metabolism; Nicotinic Agonists, chemistry, metabolism; Protein Structure, Quaternary; Pyridines, chemistry, metabolism; Receptors, Nicotinic, chemistry, metabolism}, + mid = {NIHMS812379}, + nlm-id = {0410462}, + owner = {NLM}, + pii = {nature19785}, + pmc = {PMC5161573}, + pmid = {27698419}, + pubmodel = {Print-Electronic}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{althoff2014, + author = {Althoff, T. and Hibbs, R. E. and Banerjee, S. and Gouaux, E.}, + title = {X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors.}, + journal = {Nature}, + year = {2014}, + volume = {512}, + issue = {7514}, + month = aug, + pages = {333--337}, + issn = {1476-4687}, + doi = {10.1038/nature13669}, + abstract = {Cys-loop receptors are neurotransmitter-gated ion channels that are essential mediators of fast chemical neurotransmission and are associated with a large number of neurological diseases and disorders, as well as parasitic infections. Members of this ion channel superfamily mediate excitatory or inhibitory neurotransmission depending on their ligand and ion selectivity. Structural information for Cys-loop receptors comes from several sources including electron microscopic studies of the nicotinic acetylcholine receptor, high-resolution X-ray structures of extracellular domains and X-ray structures of bacterial orthologues. In 2011 our group published structures of the Caenorhabditis elegans glutamate-gated chloride channel (GluCl) in complex with the allosteric partial agonist ivermectin, which provided insights into the structure of a possibly open state of a eukaryotic Cys-loop receptor, the basis for anion selectivity and channel block, and the mechanism by which ivermectin and related molecules stabilize the open state and potentiate neurotransmitter binding. However, there remain unanswered questions about the mechanism of channel opening and closing, the location and nature of the shut ion channel gate, the transitions between the closed/resting, open/activated and closed/desensitized states, and the mechanism by which conformational changes are coupled between the extracellular, orthosteric agonist binding domain and the transmembrane, ion channel domain. Here we present two conformationally distinct structures of C. elegans GluCl in the absence of ivermectin. Structural comparisons reveal a quaternary activation mechanism arising from rigid-body movements between the extracellular and transmembrane domains and a mechanism for modulation of the receptor by phospholipids. }, + chemicals = {Apoproteins, Chloride Channels, Cysteine Loop Ligand-Gated Ion Channel Receptors, Ligands, Phosphatidylcholines, glutamate-gated chloride channels, Glutamic Acid, Ivermectin, 1-palmitoyl-2-oleoylphosphatidylcholine}, + citation-subset = {IM}, + completed = {2014-09-15}, + country = {England}, + issn-linking = {0028-0836}, + keywords = {Allosteric Regulation, drug effects; Animals; Apoproteins, chemistry, metabolism; Binding Sites; Binding, Competitive, drug effects; Caenorhabditis elegans, chemistry; Cell Membrane, metabolism; Chloride Channels, chemistry, metabolism; Crystallography, X-Ray; Cysteine Loop Ligand-Gated Ion Channel Receptors, chemistry, metabolism; Drug Partial Agonism; Glutamic Acid, metabolism; Ion Channel Gating; Ivermectin, chemistry, metabolism, pharmacology; Ligands; Models, Molecular; Movement, drug effects; Phosphatidylcholines, chemistry, metabolism, pharmacology; Protein Binding; Protein Multimerization, drug effects; Protein Structure, Tertiary, drug effects; Structure-Activity Relationship}, + mid = {NIHMS634520}, + nlm-id = {0410462}, + owner = {NLM}, + pii = {nature13669}, + pmc = {PMC4255919}, + pmid = {25143115}, + pubmodel = {Print}, + pubstatus = {ppublish}, + revised = {2019-01-08}, +} + +@Article{du2015, + author = {Du, J. and Lü, W. and Wu, S. and Cheng, Y. and Gouaux, E.}, + title = {Glycine receptor mechanism elucidated by electron cryo-microscopy.}, + journal = {Nature}, + year = {2015}, + volume = {526}, + issue = {7572}, + month = oct, + pages = {224--229}, + issn = {1476-4687}, + doi = {10.1038/nature14853}, + abstract = {The strychnine-sensitive glycine receptor (GlyR) mediates inhibitory synaptic transmission in the spinal cord and brainstem and is linked to neurological disorders, including autism and hyperekplexia. Understanding of molecular mechanisms and pharmacology of glycine receptors has been hindered by a lack of high-resolution structures. Here we report electron cryo-microscopy structures of the zebrafish α1 GlyR with strychnine, glycine, or glycine and ivermectin (glycine/ivermectin). Strychnine arrests the receptor in an antagonist-bound closed ion channel state, glycine stabilizes the receptor in an agonist-bound open channel state, and the glycine/ivermectin complex adopts a potentially desensitized or partially open state. Relative to the glycine-bound state, strychnine expands the agonist-binding pocket via outward movement of the C loop, promotes rearrangement of the extracellular and transmembrane domain 'wrist' interface, and leads to rotation of the transmembrane domain towards the pore axis, occluding the ion conduction pathway. These structures illuminate the GlyR mechanism and define a rubric to interpret structures of Cys-loop receptors. }, + chemicals = {Neurotransmitter Agents, Protein Subunits, Receptors, Glycine, glycine receptor alpha1, Ivermectin, Strychnine, Glycine}, + citation-subset = {IM}, + completed = {2016-03-30}, + country = {England}, + issn-linking = {0028-0836}, + keywords = {Allosteric Regulation; Animals; Binding Sites; Cryoelectron Microscopy; Glycine, metabolism, pharmacology; Ion Channel Gating, drug effects; Ivermectin, metabolism, pharmacology; Models, Molecular; Neurotransmitter Agents, metabolism, pharmacology; Protein Conformation, drug effects; Protein Subunits, chemistry, drug effects, metabolism; Receptors, Glycine, agonists, antagonists & inhibitors, metabolism, ultrastructure; Rotation; Signal Transduction; Strychnine, metabolism, pharmacology; Zebrafish}, + mid = {NIHMS727941}, + nlm-id = {0410462}, + owner = {NLM}, + pii = {nature14853}, + pmc = {PMC4659708}, + pmid = {26344198}, + pubmodel = {Print-Electronic}, + pubstatus = {ppublish}, + revised = {2018-11-13}, +} + +@Article{monod1965, + author = {Monod, J. and Wyman, J. and Changeux, Jean-P.}, + title = {On the nature of allosteric transitions: a plausible model}, + journal = {J Mol Biol}, + year = {1965}, + volume = {12}, + number = {1}, + pages = {88--118}, +} + +@Article{lindblom2006, + author = {Lindblom, T. H. and Dodd, A. K.}, + title = {Xenobiotic detoxification in the nematode Caenorhabditis elegans}, + journal = {Journal of Experimental Zoology Part A: Comparative Experimental Biology}, + year = {2006}, + volume = {305}, + number = {9}, + pages = {720--730}, + __markedentry = {[monik:]}, + publisher = {Wiley Online Library}, +} + +@InCollection{dalliere2017, + author = {Dalli{\`e}re, N. and Holden-Dye, L. and Dillon, J. and O'Connor, V. and Walker, R. J.}, + title = {Caenorhabditis elegans Feeding Behaviors}, + booktitle = {Oxford Research Encyclopedia of Neuroscience}, + year = {2017}, + __markedentry = {[monik:6]}, +} + +\begin{filecontents}{\august.bib} + +@IEEEtranBSTCTL{IEEEexample:BSTcontrol, + ctldash_repeated_names = {no}, +} + @Comment{jabref-meta: databaseType:biblatex;} diff --git a/chapter-previews/discussion_draft_2_corrections.docx b/chapter-previews/discussion_draft_2_corrections.docx new file mode 100644 index 0000000000000000000000000000000000000000..4ce034ce366ecbd991e45e9b3dbc6c07f9bc7ec7 Binary files /dev/null and b/chapter-previews/discussion_draft_2_corrections.docx differ diff --git a/fig/general_intro/ai/synapse_with_enzymes.ai b/fig/general_intro/ai/synapse_with_enzymes.ai new file mode 100644 index 0000000000000000000000000000000000000000..26bf191e7e37f7d0e2bac88f96b6d2ba0502924e --- /dev/null +++ b/fig/general_intro/ai/synapse_with_enzymes.ai @@ -0,0 +1,5330 @@ +%PDF-1.5 %���� +1 0 obj <</Metadata 2 0 R/OCProperties<</D<</ON[8 0 R 76 0 R]/Order 77 0 R/RBGroups[]>>/OCGs[8 0 R 76 0 R]>>/Pages 3 0 R/Type/Catalog>> endobj 2 0 obj <</Length 62478/Subtype/XML/Type/Metadata>>stream +<?xpacket begin="" id="W5M0MpCehiHzreSzNTczkc9d"?> +<x:xmpmeta xmlns:x="adobe:ns:meta/" x:xmptk="Adobe XMP Core 5.3-c011 66.145661, 2012/02/06-14:56:27 "> + <rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"> + <rdf:Description rdf:about="" + xmlns:dc="http://purl.org/dc/elements/1.1/"> + <dc:format>application/pdf</dc:format> + <dc:title> + <rdf:Alt> + <rdf:li xml:lang="x-default">synapse</rdf:li> + </rdf:Alt> + </dc:title> + </rdf:Description> + <rdf:Description rdf:about="" + xmlns:xmp="http://ns.adobe.com/xap/1.0/" + xmlns:xmpGImg="http://ns.adobe.com/xap/1.0/g/img/"> + <xmp:MetadataDate>2019-10-06T00:05:19+01:00</xmp:MetadataDate> + <xmp:ModifyDate>2019-10-06T00:05:19+01:00</xmp:ModifyDate> + <xmp:CreateDate>2019-10-05T18:23:53+01:00</xmp:CreateDate> + <xmp:CreatorTool>Adobe Illustrator CS6 (Windows)</xmp:CreatorTool> + <xmp:Thumbnails> + <rdf:Alt> + <rdf:li rdf:parseType="Resource"> + <xmpGImg:width>252</xmpGImg:width> + <xmpGImg:height>256</xmpGImg:height> + <xmpGImg:format>JPEG</xmpGImg:format> + <xmpGImg:image>/9j/4AAQSkZJRgABAgEASABIAAD/7QAsUGhvdG9zaG9wIDMuMAA4QklNA+0AAAAAABAASAAAAAEA
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+Missing character: There is no d in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no , in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no , in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no - in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no - in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no - in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no E in font nullfont! +Missing character: There is no x in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no b in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no b in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no , in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no T in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no b in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no v in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no * in font nullfont! +Missing character: There is no C in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no * in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no - in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no , in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no v in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no O in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no , in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no w in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no ; in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no y in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no t in font nullfont! +! Undefined control sequence. +l.15 ...; it stimulated pharyngeal pumping at \geg + 75 micromolar. The concen... +The control sequence at the end of the top line +of your error message was never \def'ed. If you have +misspelled it (e.g., `\hobx'), type `I' and the correct +spelling (e.g., `I\hbox'). Otherwise just continue, +and I'll forget about whatever was undefined. + +Missing character: There is no 7 in font nullfont! +Missing character: There is no 5 in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no m in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no a in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no T in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no o in font nullfont! 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+Missing character: There is no d in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no - in font nullfont! +Missing character: There is no p in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no T in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no r in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no c in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no i in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no n in font nullfont! +Missing character: There is no i in font nullfont! 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+Missing character: There is no u in font nullfont! +Missing character: There is no d in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no t in font nullfont! +Missing character: There is no h in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no u in font nullfont! +Missing character: There is no s in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no o in font nullfont! +Missing character: There is no f in font nullfont! +Missing character: There is no * in font nullfont! +Missing character: There is no C in font nullfont! +Missing character: There is no . in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no l in font nullfont! +Missing character: There is no e in font nullfont! +Missing character: There is no g in font nullfont! +Missing character: There is no a in font nullfont! 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LaTeX Error: Missing \begin{document}. + +See the LaTeX manual or LaTeX Companion for explanation. +Type H <return> for immediate help. + ... + +l.17 F + urther experiments show that \textit{C. elegans eat-2} mutant is a sui... + +You're in trouble here. 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Missing $ inserted. +<inserted text> + $ +l.17 ...m. Heterologous expression of human \alpha + 7 nAChR +I've inserted a begin-math/end-math symbol since I think +you left one out. Proceed, with fingers crossed. + +LaTeX Font Info: External font `cmex10' loaded for size +(Font) <7> on input line 17. +LaTeX Font Info: External font `cmex10' loaded for size +(Font) <5> on input line 17. +) +! Emergency stop. +<*> abstract.tex + +*** (job aborted, no legal \end found) + + +Here is how much of TeX's memory you used: + 10 strings out of 494553 + 191 string characters out of 6175971 + 53697 words of memory out of 5000000 + 3779 multiletter control sequences out of 15000+600000 + 3986 words of font info for 15 fonts, out of 8000000 for 9000 + 14 hyphenation exceptions out of 8191 + 18i,1n,12p,1399b,67s stack positions out of 5000i,500n,10000p,200000b,80000s +! ==> Fatal error occurred, no output PDF file produced! diff --git a/tex-files/abstract.tex b/tex-files/abstract.tex index 08029a75d8f74b6a70711d6de19ca885e8965817..d741af48ac3cf899aebbb84ce4f2c970058c5476 100644 --- a/tex-files/abstract.tex +++ b/tex-files/abstract.tex @@ -1,3 +1,8 @@ \addcontentsline{toc}{chapter}{Abstract} \chapter*{Abstract} +An ability of insecticides to selectively target pests without affecting non-target species is a key determinant of success of componds used in agriculture. Neonicotinoids are a major class of insecticide which encompases seven chemical representing three distinct chemical classes, namely cyanoamidines, nitroguanidines and nitromethylenes. Neonicotinoids effectively control a wide range of insect pests and have low toxicity against mammals, however they can also negatively impact on non-target species of bees, threatening food safety. Neonicotinoids act by targeting insect nAChR, which are a major excitatory receptors in the insect central nervous system. Difficulties in heterologous expression of these proteins hinders their pharmacological characterisation and identification of molecular determinants of neonicotinoid-toxicity. This thesis describes the efforts into developing \textit{C. elegans}* as a platfom in which the mode of action and selective toxicity of neonicotinoid-insecticides can be studied. + +We determined the effects of neonicotinoids on \textit{C. elegans} behaviours governed by the cholinergic neurotransmission. Cyanoamidines clothianidin, nitroguanidine thiacloprid and nitromethylene nitenpyram showed low efficacy on locomotion, pharyngeal pumping, egg-laying and egg-hatching of young adult wild-type \textit{C. elegans}. Exposure of mutant worm with enhanced cuticle permeability showed increased susceptibility of worms to all three neonicotinoids tested, suggesting an adult cuticle limits drug access. The role of the cuticle in neonicotinoids susceptibility was nvestigated in *C. elegans* cut-head preparation, in which the cuticle is removed and the effects of compounds on pharyngeal pumping are scored. Out of the three neonicotinoids applied, clothianidin showed the greatest efficacy; it stimulated pharyngeal pumping at $\geq$ 75 $\mu$M. The concentrations effective against the function of the pharynx are an order or magnitude lower than the residual, average concenntration in the soil, suggesting *C. elegans* is not impacted in the field, and at least 8-fold lower than lethal doses in insect-pests. The difference in neonicotinoid-susceptiility between adult \textit{C. elegans} and insects precludes the use of *C. elegans* pharynx as a platform for the mode of action studies, but highlights its potential as a suitable background for the heterologous expression of insect nAChRs. + +Further experiments show that \textit{C. elegans eat-2} nAChR mutant is a suitable genetic background, in which the expression of heterologous nAChRs can be scored in behavioural and pharmacological assays. Expression of nAChR EAT-2 in the pharyngeal muscle rescued the blunted feeding phenotype and 5-HT insensitivity of the \textit{eat-2} mutant worm. Expression of exogenous receptor, viz. human $\alpha$7 in the pharynx of \textit{eat-2} mutant led to a cell-surface expression, as shown by staining with labelled $\alpha$-bungarotoxin. However the feeding and pharmacological phenotypes of the mutant were not rescued. \textit{C. elegans} strains in which human $\alpha$7 is expressed in the wild-type genetic background was also generated to determine whether the pharmacology of the human receptor can be inprinted on the \textit{C. elegans} pharynx. No difference in the phayngeal response to nAChR agonists cytisine, nicotine or acetylcholine were noted. The lack of apparent functionality of $\alpha$7 receptor could be due to the incorrect cellular localisation of this protein. $\alpha$-bgtx staining showed that the expression of $\alpha$7 receptor is concentrated to the specific cells of the pharyngeal muscle, however this localisation does not overlap with the localisation of native EAT-2 receptors. A transgenic strains in which exogenous proteins are expressed using EAT-2 native promoter should be made. \ No newline at end of file diff --git a/tex-files/acknowledgements.tex b/tex-files/acknowledgements.tex index d8cc340b101945140d169aefc193309af1d04ffd..fa2f201339c12407e1a126be33f0fcae6611dc73 100644 --- a/tex-files/acknowledgements.tex +++ b/tex-files/acknowledgements.tex @@ -1,2 +1,17 @@ \addcontentsline{toc}{chapter}{Acknowledgements} \chapter*{Acknowledgements} + +Throughout the process of PhD study, research and writing this thesis, I have received a great deal of support and help. +I would like to thank my supervisors: Dr Declan Doyle, Prof Vincent O’Connor and Prof Lindy Holden-Dye, whose expertise, knowledge, enthusiasm and motivation was invaluable. Without your guidance this PhD would have been unachievable. + +I would like to acknowledge The Gerard Kerkut Charitable Trust for providing funding for this PhD project. + +I am also very grateful to Prof Robert Walker, Prof Nullin Divecha and Dr James Dillon for their insightful comments and encouraging words. + +My thanks go to Dr Alistair Bailey for his help with writing and formatting this thesis and for keeping me company throughout my studies. + +Thank you to all members of the worm-lab and the lab of Dr Declan Doyle for all the fun we have experienced together. In particular, I would like to thank Dr Ben Yarnall, Dr Fernando Calahorro and Dr Anna Crisford for your support and technical help. + +I am grateful to my all my family members who always believed in me. + +Last but not least thank you to my partner, Damien Parsey for his continual emotional support, patience and understanding. I would not have made it without you. diff --git a/tex-files/declaration.tex b/tex-files/declaration.tex index 92bd32a8c85c4497530b4c6ade1ca34637595c0d..aac0912f09a869a34e4de92e532fdee967e53a86 100644 --- a/tex-files/declaration.tex +++ b/tex-files/declaration.tex @@ -5,7 +5,7 @@ I, Monika Kudelska declare that the thesis entitled: -Investigation of the selective toxicity of neonicotinoids using the nematode worm Caenorhabditis elegans % Change to dissertation title +Investigation of the selective toxicity of neonicotinoids using the nematode worm \textit {Caenorhabditis elegans} % Change to dissertation title and the work presented in it are my own and has been generated by me as the result of my own original research. diff --git a/tex-files/mkthesis.sty b/tex-files/mkthesis.sty index 29ca69d5a884cc73b3a0c5e71acb7ab2c0c7a797..8c2b7cd5bdca783c74b31d67a6c9a7a8cf587440 100644 --- a/tex-files/mkthesis.sty +++ b/tex-files/mkthesis.sty @@ -67,7 +67,9 @@ % Abstract \phantomsection \input{tex-files/abstract.tex} + \pagestyle{plain} \cleardoublepage + \pagestyle{uheadings} %Table of contents \phantomsection \pdfbookmark[0]{\contentsname}{toc} @@ -105,6 +107,12 @@ \pagestyle{plain} \cleardoublepage \pagestyle{uheadings} + % Publications + \phantomsection + \input{tex-files/publication.tex} + \pagestyle{plain} + \cleardoublepage + \pagestyle{uheadings} } % Now change the stlye for the body and use underlined pages with Arabic Numbering diff --git a/tex-files/publication.tex b/tex-files/publication.tex new file mode 100644 index 0000000000000000000000000000000000000000..160344d8054fb4e930bdef3841df75c0ba850404 --- /dev/null +++ b/tex-files/publication.tex @@ -0,0 +1,14 @@ +\addcontentsline{toc}{chapter}{Publications} +\chapter*{Publications} + +Part of this thesis has been published in the following papers: + +Kudelska, M. M., L. Holden-Dye, V. O’Connor, and D. A. Doyle. 2017. “Concentration-Dependent Effects +of Acute and Chronic Neonicotinoid Exposure on the Behaviour and Development of the Nematode +Caenorhabditis Elegans.” Journal Article. Pest Manag Sci 73 (7): 1345–51. https://doi.org/10.1002/ps. +4564. + +Kudelska, M. M., A. Lewis, C. T. Ng, D. A. Doyle, L. Holden-Dye, V. M. O’Connor, and R. J. Walker. +2018. “Investigation of Feeding Behaviour in c. Elegans Reveals Distinct Pharmacological +and Antibacterial Effects of Nicotine.” Invertebrate Neuroscience : IN 18 (4): 14. https: +//doi.org/10.1007/s10158-018-0219-1. \ No newline at end of file diff --git a/thesis-dissertaion.log b/thesis-dissertaion.log index 39a3735f6ab3b7631f920e8777ffffbf76617516..31cb14f4de4f184910deddb693d0d8dd7027b4b1 100644 --- a/thesis-dissertaion.log +++ b/thesis-dissertaion.log @@ -1,4 +1,4 @@ -This is XeTeX, Version 3.14159265-2.6-0.999991 (TeX Live 2019/W32TeX) (preloaded format=xelatex 2019.8.18) 29 SEP 2019 15:43 +This is XeTeX, Version 3.14159265-2.6-0.999991 (TeX Live 2019/W32TeX) (preloaded format=xelatex 2019.8.18) 6 OCT 2019 15:49 entering extended mode restricted \write18 enabled. %&-line parsing enabled. @@ -1022,7 +1022,131 @@ Package: bookmark 2019/06/04 v1.27 PDF bookmarks (HO) fm.def File: bkm-dvipdfm.def 2019/06/04 v1.27 bookmark driver for dvipdfm (HO) \BKM@id=\count327 -)) (./tex-files/uhead.sty) (./tex-files/mkthesis.sty) 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at line 179 + []\T1/fvs/m/n/10 112 + [] -] (./tex-files/acknowledgements.tex) [19 -] [20 +Overfull \hbox (3.22194pt too wide) detected at line 180 + []\T1/fvs/m/n/10 114 + [] -] -Chapter 1. -LaTeX Font Info: Font shape `T1/fvs/m/n' will be -(Font) scaled to size 18.66588pt on input line 179. -LaTeX Font Info: Font shape `T1/fvs/bx/n' in size <20.74> not available -(Font) Font shape `T1/fvs/b/n' tried instead on input line 179. -LaTeX Font Info: Font shape `T1/fvs/b/n' will be -(Font) scaled to size 18.66588pt on input line 179. -LaTeX Font Info: Font shape `T1/fvs/m/n' will be -(Font) scaled to size 10.79993pt on input line 187. -LaTeX Font Info: Font shape `T1/fvs/bx/n' in size <12> not available -(Font) Font shape `T1/fvs/b/n' tried instead on input line 187. -LaTeX Font Info: Font shape `T1/fvs/b/n' will be -(Font) scaled to size 10.79993pt on input line 187. -[1 -] -LaTeX Font Info: Font shape `T1/fvs/bx/it' in size <14.4> not available -(Font) Font shape `T1/fvs/b/it' tried instead on input line 295. -LaTeX Font Info: Font shape `T1/fvs/b/it' will be -(Font) scaled to size 12.9599pt on input line 295. +Overfull \hbox (3.22194pt too wide) detected at line 181 + []\T1/fvs/m/n/10 117 + [] -Overfull \hbox (22.17484pt too wide) in paragraph at lines 319--319 -[]\T1/fvs/b/n/14.4 Cholinergic neu-ro-trans-mis-sion reg-u-lates feed-ing, lo-c -o-mo-tion + +Overfull \hbox (3.22194pt too wide) detected at line 182 + []\T1/fvs/m/n/10 118 [] -Overfull \hbox (170.25717pt too wide) in paragraph at lines 334--334 -[]\T1/fvs/b/n/14.4 Heterologous ex-pres-sion of nAChRs in \T1/fvs/b/it/14.4 C. -el-e-gans \T1/fvs/b/n/14.4 ##{het-ex-p-ef-fect-sof-phys-i-ol-ogy} +Overfull \hbox (3.22194pt too wide) detected at line 184 + []\T1/fvs/m/n/10 120 [] -Underfull \vbox (badness 1014) has occurred while \output is active [] +Overfull \hbox (3.22194pt too wide) detected at line 185 + []\T1/fvs/m/n/10 120 + [] -LaTeX Font Info: Font shape `T1/fvs/m/sl' in size <10> not available -(Font) 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while \output is active [] +Overfull \hbox (3.22194pt too wide) detected at line 196 + []\T1/fvs/m/n/10 138 + [] -[7] -Underfull \vbox (badness 10000) has occurred while \output is active [] -[8] -Overfull \vbox (869.36156pt too high) has occurred while \output is active [] +Overfull \hbox (3.22194pt too wide) detected at line 197 + []\T1/fvs/m/n/10 144 + [] -[9] -Underfull \hbox (badness 1048) in paragraph at lines 552--552 -[]\T1/fvs/b/n/12 Determination of hu-man nAChR ex-pres-sion in the \T1/fvs/b/it -/12 C. el-e-gans + +Overfull \hbox (3.22194pt too wide) detected at line 198 + []\T1/fvs/m/n/10 144 [] -Underfull \hbox (badness 1735) in paragraph at lines 552--552 -\T1/fvs/b/n/12 phar-ynx by stain-ing with con-ju-gated $\OML/zplm/m/it/12 ^^K\O -T1/ppl/m/n/12 7$ \T1/fvs/b/n/12 se-lec-tive an-tag-o-nist +Overfull \hbox (3.22194pt too wide) detected at line 199 + []\T1/fvs/m/n/10 145 [] -[10] -Chapter 3. -LaTeX Font Info: Font shape `T1/fvs/bx/it' in size <24.88> not available -(Font) 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In-ver-te-brate Neu- +ro-science : IN 18 (4): 14. https: + [] + +[25 + +] [26 + +] +Chapter 1. +LaTeX Font Info: Font shape `T1/fvs/m/n' will be +(Font) scaled to size 18.66588pt on input line 193. +LaTeX Font Info: Font shape `T1/fvs/bx/n' in size <20.74> not available +(Font) Font shape `T1/fvs/b/n' tried instead on input line 193. +LaTeX Font Info: Font shape `T1/fvs/b/n' will be +(Font) scaled to size 18.66588pt on input line 193. + +Overfull \hbox (30.49336pt too wide) in paragraph at lines 204--205 +[]\T1/fvs/m/n/10 In the last cen-tury, sev-eral syn-thetic com-pounds be-came a +vail-able, in-clud-ing dichlorodiphenyl-trichloroethane + [] + +[1 + +] +LaTeX Font Info: Font shape `T1/fvs/m/n' will be +(Font) scaled to size 8.09995pt on input line 223. +LaTeX Font Info: Font shape `U/msa/m/n' will be +(Font) scaled to size 9.37807pt on input line 224. +LaTeX Font Info: Font shape `U/msa/m/n' will be +(Font) scaled to size 7.29405pt on input line 224. +LaTeX Font Info: Font shape 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[] + [] + +[7] [8] [9] [10] [11] +Underfull \hbox (badness 1112) in paragraph at lines 446--447 +[]\T1/fvs/m/n/10 The iden-tity of the NMJ nAChR was first in-ves-ti-gated us-in +g in-di-rect, bio-chem-i-cal ap-proaches. + [] + +[12] +Missing character: There is no α in font fvsr8t! +File: fig/general_intro/png/crystal_structure_nachr.png Graphic file (type bmp) + +<fig/general_intro/png/crystal_structure_nachr.png> + +Underfull \vbox (badness 10000) has occurred while \output is active [] + +[13] +File: fig/general_intro/png/binding_pocket_3.png Graphic file (type bmp) +<fig/general_intro/png/binding_pocket_3.png> +[14] [15] [16] +File: fig/general_intro/png/nicotinic_interactions.png Graphic file (type bmp) +<fig/general_intro/png/nicotinic_interactions.png> + +Underfull \hbox (badness 1400) in paragraph at lines 508--509 +\T1/fvs/m/n/10 and non-selective nAChR ligands- nicoti-noids (nico-tine, epi-ba +-ti-dine and desmotroim-i-da-clo-prid). + [] + +[17] [18] + +LaTeX Warning: 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record-ings : elec-tro-phys-i-o-log-i-cal + [] + + +Underfull \hbox (badness 1888) in paragraph at lines 611--612 +\T1/fvs/m/n/10 con-cen-tra-tions 1 mM - 10 mM were needed, po-ten-tially due to + the high con-cen-tra-tion of + [] + +[25] +Underfull \hbox (badness 2846) in paragraph at lines 626--627 +[]\T1/fvs/m/n/10 cocroach ter-mi-nal ab-dom-i-nal gan-glion ex-tra-cel-lu-lar p +ost synap-tic po-ten-tials in re-sponse to + [] + +[26] [27] +Underfull \vbox (badness 1783) has occurred while \output is active [] + +[28] +Underfull \vbox (badness 3049) has occurred while \output is active [] + +[29] + +LaTeX Warning: `!h' float specifier changed to `!ht'. + +[30] +Underfull \hbox (badness 10000) in paragraph at lines 765--766 +[]\T1/fvs/m/n/9 Rn = Rat-tus norvegi-cus (rat), Dm = *Drosophila + [] + + +LaTeX Warning: `!h' float specifier changed to `!ht'. + + +Underfull \vbox (badness 3930) has occurred while \output is active [] + +[31] + +LaTeX Warning: `!h' float specifier changed to 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Drugs and reagents were pur-cha +sed from Sigma Aldrich, + [] + + +Underfull \hbox (badness 1215) in paragraph at lines 1542--1542 +[]\T1/fvs/b/n/12 Effects of drugs on in-tact \T1/fvs/b/it/12 C. el-e-gans \T1/f +vs/b/n/12 lo-co-mo-tion and feed-ing + [] + +[60] +File: fig/methods/thrashing_experiment.pdf Graphic file (type pdf) +<use fig/methods/thrashing_experiment.pdf> +[61] +Missing character: There is no μ in font fvsr8t! +Missing character: There is no μ in font fvsr8t! +[62] +Underfull \hbox (badness 1005) in paragraph at lines 1591--1591 +[]\T1/fvs/b/n/12 Effects of drugs on in-tact \T1/fvs/b/it/12 C. el-e-gans \T1/f +vs/b/n/12 be-haviour upon 24-hour + [] + +[63] +File: fig/methods/on_plate_experiments.jpg Graphic file (type bmp) +<fig/methods/on_plate_experiments.jpg> +[64] +Underfull \hbox (badness 1286) in paragraph at lines 1627--1629 +\T1/fvs/m/n/10 Experiments were car-ried out in 12 well plate con-tain-ing drug + or sol-vent -incorporated and + [] + +File: 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active [] + +[205] [206] [207] [208] +Chapter 7. + +Underfull \hbox (badness 1533) in paragraph at lines 4221--4222 +\T1/fvs/m/n/10 Increased use of in-sec-ti-cides re-quires a bet-ter un-der-stan +d-ing of their en-vi-ron-men-tal im-pact. + [] + +[209 + +] [210] +Underfull \hbox (badness 1005) in paragraph at lines 4240--4241 +\T1/fvs/m/n/10 have ag-o-nis-tic, an-tag-o-nis-tic and super-agonistic ac-tion, + de-pend-ing on the an-i-mal prepa-ra-tion + [] + +[211] [212] +Underfull \hbox (badness 1939) in paragraph at lines 4260--4261 +[]\T1/fvs/m/n/10 The dif-fer-ences be-tween the in-sect and \T1/fvs/m/it/10 C.e +legans \T1/fvs/m/n/10 bind-ing pocket are mainly found in the + [] + + +Underfull \hbox (badness 3690) in paragraph at lines 4260--4261 +\T1/fvs/m/n/10 com-ple-men-tary site, sug-gest-ing the con-tri-bu-tions from th +e com-ple-men-tary site de-ter-mine + [] + +File: fig/gen_discussion/celegans_and_insect_added_loopG_and_B.ai Graphic file +(type pdf) +<use 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+Underfull \hbox (badness 2671) in paragraph at lines 4765--4767 +\T1/fvs/m/n/10 Eco-tox-i-co-log-i-cal As-sess-ments of Pes-ti-cides Used to Tre +at Seeds Un-der Trop-i-cal Con-di-tions.'' + [] + + +Underfull \hbox (badness 2418) in paragraph at lines 4771--4773 +\T1/fvs/m/n/10 Methyl-car-bamyl-choline Bind-ing Sites and Ef-fect of N-Methylc +arbamylcholine on Acetyl-choline + [] + +[266] +Underfull \hbox (badness 10000) in paragraph at lines 4783--4785 +[]$\T1/fvs/m/n/10 https : / / www . efsa . europa . eu / en / press / news / 18 +0228 # targetText = Neonicotinoids % 3A % 20risks % 20to % + [] + + +Overfull \hbox (31.40352pt too wide) in paragraph at lines 4798--4800 +\T1/fvs/m/n/10 Jour-nal Ar-ti-cle. \T1/fvs/m/it/10 Jour-nal of Ex-per-i-men-tal + Zo-ol-ogy \T1/fvs/m/n/10 253 (3): 263--70. []https://doi.org/DOI 10.1002/jez.1 +402530305[]. + [] + +[267] [268] +Overfull \hbox (65.39671pt too wide) in paragraph at lines 4864--4867 +[]\T1/fvs/m/n/10 http://www.ncbi.nlm.nih.gov/pubmed/2642001 http://www.scienced +irect.com/science/article/pii/0896627389902596[]. + [] + +[269] +Underfull \hbox (badness 1484) in paragraph at lines 4889--4891 +\T1/fvs/m/n/10 Method for As-sess-ing Chem-i-cal Tox-i-c-ity Us-ing a Caenorhab +-di-tis El-e-gans Re-pro-duc-tion As-say.'' + [] + +Missing character: There is no α in font fvsr8t! +[270] +Underfull \hbox (badness 1314) in paragraph at lines 4940--4942 +\T1/fvs/m/n/10 in Achbp Crys-tal Struc-tures.'' Jour-nal Ar-ti-cle. \T1/fvs/m/i +t/10 Neu-ron \T1/fvs/m/n/10 41 (6): 907--14. []https://doi.org/Doi + [] + + +Underfull \hbox (badness 1137) in paragraph at lines 4952--4954 +[][]\T1/fvs/m/n/10 Chao, L P. 1980. ``Choline Acetyl-trans-ferase: Pu-rifi-ca-t +ion and Char-ac-ter-i-za-tion.'' \T1/fvs/m/it/10 Jour-nal of + [] + +[271] +Underfull \hbox (badness 10000) in paragraph at lines 4989--4991 +\T1/fvs/m/n/10 food / plant / pesticides / eu-[]pesticides-[]database / public +/ ?event = activesubstance . detail & language = EN & + [] + +[272] +Underfull \hbox (badness 10000) in paragraph at lines 4992--4994 +[]$\T1/fvs/m/n/10 https : / / ec . europa . eu / food / plant / pesticides / eu +-[]pesticides-[]database / public / ?event = activesubstance . + [] + +[273] +Underfull \hbox (badness 1478) in paragraph at lines 5037--5039 +\T1/fvs/m/n/10 J. P. Arena. 1994. ``Cloning of an Avermectin-Sensitive Glutamat +e-Gated Chlo-ride Chan-nel + [] + +[274] [275] +Overfull \hbox (23.95222pt too wide) in paragraph at lines 5100--5102 +[][]\T1/fvs/m/n/10 ECHA. 2017. ``Opin-ion on Ar-senic Acid and Its In-or-ganic +Salts. Re-port Echa/Rac/A77-O-0000001412-86-148/F + [] + + +Underfull \hbox (badness 6078) in paragraph at lines 5109--5111 +\T1/fvs/m/n/10 ``Chi-maeric Nicotinic-Serotonergic Re-cep-tor Com-bines Dis-tin +ct Lig-and Bind-ing and Chan-nel + [] + +[276] +Overfull \hbox (17.46326pt too wide) in paragraph at lines 5151--5153 +[][]\T1/fvs/m/n/10 Fucile, S., E. Palma, A. M. Mileo, R. Miledi, and F. Eu-sebi +. 2000. ``Hu-man Neu-ronal Threonine-for-Leucine-248 + [] + + +Underfull \hbox (badness 1152) in paragraph at lines 5151--5153 +\T1/fvs/m/n/10 Al-pha 7 Mu-tant Nico-tinic Acetyl-choline Re-cep-tors Are Highl +y Ca2+ Per-me-able.'' \T1/fvs/m/it/10 Pro-ceed-ings + [] + +[277] +Missing character: There is no α in font fvsr8t! +[278] +Missing character: There is no ć in font fvsr8t! +[279] [280] +Underfull \hbox (badness 1173) in paragraph at lines 5277--5279 +[][]\T1/fvs/m/n/10 Hsiao, Y., J. Lai, Hsiu-Y. Liao, and Hai-T. 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[]http: +//natres.psu.ac.th/Link/SoilCongress/en/symt25.htm[]. + [] + +[294] +Underfull \hbox (badness 1527) in paragraph at lines 5746--5748 +[][]\T1/fvs/m/n/10 Rand, J. B., and R. L. Rus-sell. 1984. ``Choline Acetyltrans +ferase-Deficient Mu-tants of the + [] + + +Underfull \hbox (badness 1895) in paragraph at lines 5746--5748 +\T1/fvs/m/n/10 Ne-ma-tode Caenorhabditis-Elegans.'' Jour-nal Ar-ti-cle. \T1/fvs +/m/it/10 Ge-net-ics \T1/fvs/m/n/10 106 (2): 227--48. []<Go to + [] + + +Underfull \hbox (badness 1028) in paragraph at lines 5761--5763 +\T1/fvs/m/it/10 Pro-ceed-ings of the Na-tional Academy of Sci-ences of the Unit +ed States of Amer-ica \T1/fvs/m/n/10 110 (11): + [] + +[295] +Overfull \hbox (47.50313pt too wide) in paragraph at lines 5797--5799 +[][]\T1/fvs/m/n/10 Salgado, V. L., and R. 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