BoaγPLI from Boa constrictor blood is a broad-spectrum inhibitor of venom PLA2 pathophysiological actions

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dc.contributorLab. Herpetologiapt_BR
dc.contributor.authorFabri, Carolinept_BR
dc.contributor.authorZdenek, Christina N.pt_BR
dc.contributor.authorSilva, Caroline Serinopt_BR
dc.contributor.authorMorais-Zani, Karen dept_BR
dc.contributor.authorGrego, Kathleen Fernandespt_BR
dc.contributor.authorBénard-Valle, Melisapt_BR
dc.contributor.authorNeri-Castro, Edgarpt_BR
dc.contributor.authorAlagón, Alejandropt_BR
dc.contributor.authorTanaka-Azevedo, Anita Miticopt_BR
dc.contributor.authorFry, Bryan Griegpt_BR
dc.date.accessioned2021-07-02T16:22:30Z-
dc.date.available2021-07-02T16:22:30Z-
dc.date.issued2021pt_BR
dc.identifier.citationFabri C, Zdenek CN., Silva CS, Morais-Zani K, Grego KF, Bénard-Valle M, et al. BoaγPLI from boa constrictor blood is a broad-spectrum inhibitor of venom PLA2 pathophysiological actions. J. Chem. Ecol.. 2021 June;in press. doi:10.1007/s10886-021-01289-4.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3873-
dc.description.abstractThe use of venom in predation exerts a corresponding selection pressure for the evolution of venom resistance. One of the mechanisms related to venom resistance in animals (predators or prey of snakes) is the presence of molecules in the blood that can bind venom toxins, and inhibit their pharmacological effects. One such toxin type are venom phospholipase A2s (PLA2s), which have diverse effects including anticoagulant, myotoxic, and neurotoxic activities. BoaγPLI isolated from the blood of Boa constrictor has been previously shown to inhibit venom PLA2s that induced myotoxic and edematogenic activities. Recently, in addition to its previously described and very potent neurotoxic effect, the venoms of American coral snakes (Micrurus species) have been shown to have anticoagulant activity via PLA2 toxins. As coral snakes eat other snakes as a major part of their diet, neonate Boas could be susceptible to predation by this sympatric species. Thus, this work aimed to ascertain if BoaγPLI provided a protective effect against the anticoagulant toxicity of venom from the model species Micrurus laticollaris in addition to its ability shown previously against other toxin types. Using a STA R Max coagulation analyser robot to measure the effect upon clotting time, and TEG5000 thromboelastographers to measure the effect upon clot strength, we evaluated the ability of BoaγPLI to inhibit M. laticollaris venom. Our results indicate that BoaγPLI is efficient at inhibiting the M. laticollaris anticoagulant effect, reducing the time of coagulation (restoring them closer to non-venom control values) and increasing the clot strength (restoring them closer to non-venom control values). These findings demonstrate that endogenous PLA2 inhibitors in the blood of non-venomous snakes are multi-functional and provide broad resistance against a myriad of venom PLA2-driven toxic effects including coagulotoxicity, myotoxicity, and neurotoxicity. This novel form of resistance could be evidence of selective pressures caused by predation from venomous snakes and stresses the need for field-based research aimed to expand our understanding of the evolutionary dynamics of such chemical arms race.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.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofJournal of Chemical Ecologypt_BR
dc.rightsRestricted accesspt_BR
dc.titleBoaγPLI from Boa constrictor blood is a broad-spectrum inhibitor of venom PLA2 pathophysiological actionspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1007/s10886-021-01289-4pt_BR
dc.identifier.urlhttps://doi.org/10.1007/s10886-021-01289-4pt_BR
dc.contributor.externalUniversity of Queensland (UQ)pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)pt_BR
dc.contributor.externalUniversidad Nacional Autónoma de México (UNAM)pt_BR
dc.subject.keywordPLA2 inhibitorpt_BR
dc.subject.keywordAnticoagulationpt_BR
dc.subject.keywordVenom resistancept_BR
dc.subject.keywordEndogenous inhibitorspt_BR
dc.relation.ispartofabbreviatedJ. Chem. Ecol.pt_BR
dc.identifier.citationabntin press, jun. 2021pt_BR
dc.identifier.citationvancouver2021 June;in presspt_BR
dc.contributor.butantanFabri, Caroline|:Aluno|:Lab. Herpetologia|:PrimeiroAutorpt_BR
dc.contributor.butantanSilva, Caroline Serino|:Aluno|:Lab. Herpetologiapt_BR
dc.contributor.butantanMorais-Zani, Karen de|:Pesquisador|:Lab. Herpetologiapt_BR
dc.contributor.butantanGrego, Kathleen Fernandes|:Pesquisador|:Lab. Herpetologiapt_BR
dc.contributor.butantanTanaka-Azevedo, Anita Mitico|:Pesquisador|:Lab. Herpetologiapt_BR
dc.sponsorship.butantanAustralian Research Council (ARC)¦¦DP190100304pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2018/25786–0pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦001pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.languageiso639-1English-
item.fulltextCom Texto completo-
item.openairetypeArticle-
item.grantfulltextembargo_29990101-
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