Replacement and parallel simplification of non-homologous proteinases maintain venom phenotypes in rear-fanged snakes

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dc.contributorLETA - Laboratório de Toxinologia Aplicadapt_BR
dc.contributorCentro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributorLab. Imunopatologiapt_BR
dc.contributorLECZ - Laboratório de Coleções Zoológicaspt_BR
dc.contributor.authorBayona-Serrano, Juan Davidpt_BR
dc.contributor.authorViala, Vincent Louispt_BR
dc.contributor.authorRautsaw, Rhett Mpt_BR
dc.contributor.authorSchramer, Tristan Dpt_BR
dc.contributor.authorCarvalho, Gesiele Almeida Barros dept_BR
dc.contributor.authorNishiyama Junior, Milton Yutakapt_BR
dc.contributor.authorFreitas-de-Sousa, Luciana Aparecidapt_BR
dc.contributor.authorMoura-da-Silva, Ana Mariapt_BR
dc.contributor.authorParkinson, Christopher Lpt_BR
dc.contributor.authorGrazziotin, Felipe Gobbipt_BR
dc.contributor.authorJunqueira-de-Azevedo, Inácio de Loiola Meirellespt_BR
dc.date.accessioned2020-08-06T18:44:27Z-
dc.date.available2020-08-06T18:44:27Z-
dc.date.issued2020pt_BR
dc.identifier.citationBayona-Serrano JD, Viala VL, Rautsaw RM, Schramer TD, Carvalho GAB, Nishiyama Junior MY, et al. Replacement and parallel simplification of non-homologous proteinases maintain venom phenotypes in rear-fanged snakes. Mol. Biol. Evol.. 2020 Jul;37(12):3563-3575. doi:10.1093/molbev/msaa192.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3117-
dc.description.abstractNovel phenotypes are commonly associated with gene duplications and neofunctionalization, less documented are the cases of phenotypic maintenance through the recruitment of novel genes. Proteolysis is the primary toxic character of many snake venoms, and ADAM metalloproteinases, named Snake Venom Metalloproteinases (SVMPs), are largely recognized as the major effectors of this phenotype. However, by investigating original transcriptomes from 58 species of advanced snakes (Caenophidia) across their phylogeny, we discovered that a different enzyme, matrix metalloproteinase (MMP), is actually the dominant venom component in three tribes (Tachymenini, Xenodontini, and Conophiini) of rear-fanged snakes (Dipsadidae). Proteomic and functional analyses of these venoms further indicate that MMPs are likely playing an ‘SVMP-like’ function in the proteolytic phenotype. A detailed look into the venom-specific sequences revealed a new highly expressed MMP subtype, named snake venom MMP (svMMP), which originated independently on at least three occasions from an endogenous MMP-9. We further show that by losing ancillary non-catalytic domains present in its ancestors, svMMPs followed an evolutionary path toward a simplified structure during their expansion in the genomes, thus paralleling what has been proposed for the evolution of their Viperidae counterparts, the SVMPs. Moreover, we inferred an inverse relationship between the expression of svMMPs and SVMPs along the evolutionary history of Xenodontinae, pointing out that one type of enzyme may be substituting for the other, while the general (metallo)proteolytic phenotype is maintained. These results provide rare evidence on how relevant phenotypic traits can be optimized via natural selection on non-homologous genes, yielding alternate biochemical components.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipNational Science Foundation (NSF)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado do Amazonas (FAPEAM)pt_BR
dc.format.extent3563–3575pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofMolecular Biology and Evolutionpt_BR
dc.rightsOpen Accesspt_BR
dc.titleReplacement and parallel simplification of non-homologous proteinases maintain venom phenotypes in rear-fanged snakespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1093/molbev/msaa192pt_BR
dc.identifier.urlhttps://doi.org/10.1093/molbev/msaa192pt_BR
dc.contributor.externalClemson Universitypt_BR
dc.identifier.citationvolume37pt_BR
dc.identifier.citationissue12pt_BR
dc.subject.keywordmatrix metalloproteinasept_BR
dc.subject.keywordprotein family evolutionpt_BR
dc.subject.keywordgenotype-phenotype linkpt_BR
dc.subject.keywordgene co-optionpt_BR
dc.subject.keywordvenompt_BR
dc.subject.keywordsnakept_BR
dc.relation.ispartofabbreviatedMol. Biol. Evol.pt_BR
dc.identifier.citationabntv. 12, n. 12, p. 3563-3575, jul. 2020pt_BR
dc.identifier.citationvancouver2020 Jul;37(12):3563-3575pt_BR
dc.contributor.butantanBayona-Serrano, Juan David|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA)|:PrimeiroAutorpt_BR
dc.contributor.butantanViala, Vincent Louis|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA):Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.butantanCarvalho, Gesiele Almeida Barros de|:|:Laboratório Especial de Toxinologia Aplicada (LETA)pt_BR
dc.contributor.butantanNishiyama Junior, Milton Yutaka|:Pesquisador|:Laboratório Especial de Toxinologia Aplicada (LETA):Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.butantanFreitas-de-Sousa, Luciana Aparecida|:Aluno|:Lab. Imunopatologiapt_BR
dc.contributor.butantanMoura-da-Silva, Ana Maria|:Pesquisador|:Lab. Imunopatologiapt_BR
dc.contributor.butantanGrazziotin, Felipe Gobbi|:Pesquisador:Docente colaborador PPGTOX|:LECZ - Laboratório de Coleções Zoológicaspt_BR
dc.contributor.butantanJunqueira-de-Azevedo, Inácio de Loiola Meirelles|:Pesquisador|:Laboratório Especial de Toxinologia Aplicada (LETA):Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)|:Autor de correspondênciapt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2016/50127- 5pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/07467-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/24498-9pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/24546-3pt_BR
dc.sponsorship.butantanNational Science Foundation (NSF)¦¦1638879pt_BR
dc.sponsorship.butantanNational Science Foundation (NSF)¦¦1822417pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦309791/2017-0pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦ 303958/2018-9pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado do Amazonas (FAPEAM)¦¦pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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