Venom profiling of the insular species Bothrops alcatraz: characterization of proteome, Glycoproteome, and N-Terminome using terminal amine isotopic labeling of substrates

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dc.contributorLaboratório de Toxinologia Aplicadapt_BR
dc.contributorCentro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributorMuseu Biológicopt_BR
dc.contributor.authorAndrade-Silva, Déborapt_BR
dc.contributor.authorZelanis, Andrépt_BR
dc.contributor.authorTravaglia-Cardoso, Silvia Reginapt_BR
dc.contributor.authorNishiyama Junior, Milton Yutakapt_BR
dc.contributor.authorSerrano, Solange Maria de Toledopt_BR
dc.date.accessioned2021-01-12T20:16:22Z-
dc.date.available2021-01-12T20:16:22Z-
dc.date.issued2021pt_BR
dc.identifier.citationAndrade-Silva D, Zelanis A, Travaglia-Cardoso SR, Nishiyama Junior MY, Serrano SMT. Venom profiling of the insular species Bothrops alcatraz: characterization of proteome, Glycoproteome, and N-Terminome using terminal amine isotopic labeling of substrates. J. Proteome Res.. 2021 Jan;20(2):1341-1358. doi:10.1021/acs.jproteome.0c00737.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3438-
dc.description.abstractBothrops alcatraz, a species endemic to Alcatrazes Islands, is regarded as critically endangered due to its small area of occurrence and the declining quality of its habitat. We recently reported the identification of N-glycans attached to toxins of Bothrops species, showing similar compositions in venoms of the B. jararaca complex (B. jararaca, B. insularis, and B. alcatraz). Here, we characterized B. alcatraz venom using electrophoretic, proteomic, and glycoproteomic approaches. Electrophoresis showed that B. alcatraz venom differs from B. jararaca and B. insularis; however, N-glycan removal revealed similarities between them, indicating that the occupation of N-glycosylation sites contributes to interspecies variability in the B. jararaca complex. Metalloproteinase was the major toxin class identified in the B. alcatraz venom proteome followed by serine proteinase and C-type lectin, and overall, the adult B. alcatraz venom resembles that of B. jararaca juvenile specimens. The comparative glycoproteomic analysis of B. alcatraz venom with B. jararaca and B. insularis indicated that there may be differences in the utilization of N-glycosylation motifs among their different toxin classes. Furthermore, we prospected for the first time the N-terminome of a snake venom using the terminal amine isotopic labeling of substrates (TAILS) approach and report the presence of ∼30% of N-termini corresponding to truncated toxin forms and ∼37% N-terminal sequences blocked by pyroglutamic acid in B. alcatraz venom. These findings underscore a low correlation between venom gland transcriptomes and proteomes and support the view that post-translational processes play a major role in shaping venom phenotypes.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.format.extent1341-1358pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofJournal of Proteome Researchpt_BR
dc.rightsOpen accesspt_BR
dc.titleVenom profiling of the insular species Bothrops alcatraz: characterization of proteome, Glycoproteome, and N-Terminome using terminal amine isotopic labeling of substratespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1021/acs.jproteome.0c00737pt_BR
dc.identifier.urlhttps://doi.org/10.1021/acs.jproteome.0c00737pt_BR
dc.identifier.citationvolume20pt_BR
dc.identifier.citationissue2pt_BR
dc.subject.keywordBothrops alcatrazpt_BR
dc.subject.keywordsnake venompt_BR
dc.subject.keywordproteomept_BR
dc.subject.keywordglycoproteomept_BR
dc.subject.keywordN-terminomept_BR
dc.subject.keywordproteolytic processingpt_BR
dc.relation.ispartofabbreviatedJ. Proteome Res.pt_BR
dc.identifier.citationabntv. 20, n. 2, p. 1341-1358, jan. 2021pt_BR
dc.identifier.citationvancouver2021 Jan;20(2):1341-1358pt_BR
dc.contributor.butantanAndrade-Silva, Débora|:Aluno|:Laboratório de Toxinologia Aplicada:Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)|:PrimeiroAutorpt_BR
dc.contributor.butantanTravaglia-Cardoso, Silvia Regina|:Pesquisador|:Museu Biológicopt_BR
dc.contributor.butantanNishiyama Junior, Milton Yutaka|:Pesquisador|:Laboratório de Toxinologia Aplicada|:Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)pt_BR
dc.contributor.butantanSerrano, Solange Maria de Toledo|:Pesquisador:Docente permanente PPGTOX|:Laboratório de Toxinologia Aplicada|: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)¦¦2013/07467-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/13548-4pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/14651-3pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2016/16935-7pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦308133/2015-3pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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