Assessing the binding of venoms from aquatic elapids to the nicotinic acetylcholine receptor orthosteric site of different prey models

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dc.contributorLaboratório de Coleções Zoológicaspt_BR
dc.contributor.authorHarris, Richard J.pt_BR
dc.contributor.authorYoungman, Nicholas J.pt_BR
dc.contributor.authorZdenek, Christina N.pt_BR
dc.contributor.authorHuynh, Tam M.pt_BR
dc.contributor.authorNouwens, Amandapt_BR
dc.contributor.authorHodgson, Wayne C.pt_BR
dc.contributor.authorHarrich, Davidpt_BR
dc.contributor.authorDunstan, Nathanpt_BR
dc.contributor.authorPortes Junior, José Antoniopt_BR
dc.contributor.authorFry, Bryan G.pt_BR
dc.identifier.citationHarris RJ., Youngman NJ., Zdenek CN., Huynh TM., Nouwens A, Hodgson WC., et al. Assessing the binding of venoms from aquatic elapids to the nicotinic acetylcholine receptor orthosteric site of different prey models. Int. J. Mol. Sci.. 2020 Oct;21(19):7377. doi:10.3390/ijms21197377.pt_BR
dc.description.abstractThe evolution of an aquatic lifestyle from land dwelling venomous elapids is a radical ecological modification, bringing about many evolutionary changes from morphology to diet. Diet is an important ecological facet which can play a key role in regulating functional traits such as venom composition and prey-specific targeting of venom. In addition to predating upon novel prey (e.g., fish, fish eggs and invertebrates), the venoms of aquatic elapids also face the challenge of increased prey-escape potential in the aquatic environment. Thus, despite the independent radiation into an aquatic niche on four separate occasions, the venoms of aquatic elapids are evolving under convergent selection pressures. Utilising a biolayer interferometry binding assay, this study set out to elucidate whether crude venoms from representative aquatic elapids were target-specific to the orthosteric site of postsynaptic nicotinic acetylcholine receptor mimotopes of fish compared to other terrestrial prey types. Representatives of the four aquatic lineages were: aquatic coral snakes representative was Micrurus surinamensis;, sea kraits representative was Laticauda colubrina; sea snakes representatives were two Aipysurus spp. and eight Hydrophis spp; and water cobras representative was Naja annulata. No prey-specific differences in crude venom binding were observed from any species tested, except for Aipysurus laevis, which showed slight evidence of prey-potency differences. For Hydrophis caerulescens, H. peronii, H. schistosus and M. surinamensis, there was a lack of binding to the orthosteric site of any target lineage. Subsequent testing on the in vitro chick-biventer cervicis muscle preparation suggested that, while the venoms of these species bound postsynaptically, they bound to allosteric sites rather than orthosteric. Allosteric binding is potentially a weaker but faster-acting form of neurotoxicity and we hypothesise that the switch to allosteric binding is likely due to selection pressures related to prey-escape potential. This research has potentially opened up the possibility of a new functional class of toxins which have never been assessed previously while shedding light on the selection pressures shaping venom evolution.pt_BR
dc.description.sponsorshipUniversity of Queensland internationalpt_BR
dc.description.sponsorshipNational Health and Medical Research Council (NHMRC)pt_BR
dc.description.sponsorshipAustralian Research Council (ARC)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.relation.ispartofInternational Journal of Molecular Sciencespt_BR
dc.rightsOpen accesspt_BR
dc.titleAssessing the binding of venoms from aquatic elapids to the nicotinic acetylcholine receptor orthosteric site of different prey modelspt_BR
dc.rights.licenseCC BYpt_BR
dc.contributor.externalUniversity of Queensland (UQ)pt_BR
dc.contributor.externalMonash Universitypt_BR
dc.contributor.externalRoyal Brisbane and Women's Hospital (RBWH)pt_BR
dc.contributor.externalVenom Suppliespt_BR
dc.subject.keywordnicotinic acetylcholine receptorspt_BR
dc.relation.ispartofabbreviatedInt J Mol Scipt_BR
dc.identifier.citationabntv. 21, n. 19, 7377, out. 2020pt_BR
dc.identifier.citationvancouver2020 Oct;21(19):7377pt_BR
dc.contributor.butantanPortes Júnior, José Antonio|:Aluno|:Laboratório de Coleções Zoológicaspt_BR
dc.sponsorship.butantanUniversity of Queensland international¦¦pt_BR
dc.sponsorship.butantanNational Health and Medical Research Council (NHMRC)¦¦1110343pt_BR
dc.sponsorship.butantanAustralian Research Council (ARC)¦¦DP190100304pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2018/25749-8pt_BR
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