Profilings of subproteomes of lectin-binding proteins of nine Bothrops venoms reveal variability driven by different glycan types

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dc.contributorLab. de Toxinologia Aplicadapt_BR
dc.contributor(LCC) Laboratório de Ciclo Celularpt_BR
dc.contributor.authorBrás-Costa, Carolinapt_BR
dc.contributor.authorChaves, Alison Felipe Alencarpt_BR
dc.contributor.authorCajado-Carvalho, Danielapt_BR
dc.contributor.authorPires, David da Silvapt_BR
dc.contributor.authorAndrade-Silva, Déborapt_BR
dc.contributor.authorSerrano, Solange Maria de Toledopt_BR
dc.date.accessioned2022-06-10T15:23:05Z-
dc.date.available2022-06-10T15:23:05Z-
dc.date.issued2022pt_BR
dc.identifier.citationBrás-Costa C, Chaves AFA, Cajado-Carvalho D, Pires DS, Andrade-Silva D, Serrano SMT. Profilings of subproteomes of lectin-binding proteins of nine Bothrops venoms reveal variability driven by different glycan types. Biochim. Biophys. Acta Proteins Proteom.. 2022 July;1870(7):140795. doi:10.1016/j.bbapap.2022.140795.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/4387-
dc.description.abstractSnake venom proteomes have long been investigated to explore a multitude of biologically active components that are used for prey capture and defense, and are involved in the pathological effects observed upon mammalian envenomation. Glycosylation is a major protein post-translational modification in venoms and contributes to the diversification of proteomes. We have shown that Bothrops venoms are markedly defined by their content of glycoproteins, and that most N-glycan structures of eight Bothrops venoms contain sialic acid, while bisected N-acetylglucosamine was identified in Bothrops cotiara venom. To further investigate the mechanisms involved in the generation of different venoms by related snakes, here the glycoproteomes of nine Bothrops venoms (Bothrops atrox, B. cotiara, Bothrops erythromelas, Bothrops fonsecai, B. insularis, Bothrops jararaca, Bothrops jararacussu, Bothrops moojeni and Bothrops neuwiedi) were comparatively analyzed by enrichment with three lectins of different specificities, recognizing bisecting N-acetylglucosamine- and sialic acid-containing glycoproteins, and mass spectrometry. The lectin capture strategy generated venom fractions enriched with several glycoproteins, including metalloprotease, serine protease, and L- amino acid oxidase, in addition to various types of low abundant enzymes. The different contents of lectin-enriched proteins underscore novel aspects of the variability of the glycoprotein subproteomes of Bothrops venoms and point to the role of distinct types of glycan chains in generating different venoms by closely related snake species.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.description.sponsorship(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.format.extent140795pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofBiochimica et biophysica Acta. Proteins and Proteomics.pt_BR
dc.rightsRestricted accesspt_BR
dc.titleProfilings of subproteomes of lectin-binding proteins of nine Bothrops venoms reveal variability driven by different glycan typespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.bbapap.2022.140795pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.bbapap.2022.140795pt_BR
dc.identifier.citationvolume1870pt_BR
dc.identifier.citationissue7pt_BR
dc.subject.keywordBothropspt_BR
dc.subject.keywordglycoproteomicspt_BR
dc.subject.keywordmass spectrometrypt_BR
dc.subject.keywordBisecting N-acetylglucosaminept_BR
dc.subject.keywordsialic acidpt_BR
dc.subject.keywordsnake venompt_BR
dc.relation.ispartofabbreviatedBiochim. Biophys. Acta Proteins Proteom.pt_BR
dc.identifier.citationabntv. 1870, n. 7, 140795, jul. 2022pt_BR
dc.identifier.citationvancouver2022 July;1870(7):140795pt_BR
dc.contributor.butantanBrás-Costa, Carolina|:Aluno|:Lab. de Toxinologia Aplicada|:PrimeiroAutorpt_BR
dc.contributor.butantanChaves, Alison Felipe Alencar|:Aluno|:Lab. de Toxinologia Aplicadapt_BR
dc.contributor.butantanCajado-Carvalho, Daniela|:Técnico|:Lab. de Toxinologia Aplicadapt_BR
dc.contributor.butantanPires, David da Silva|:Técnico|:(LCC) Laboratório de Ciclo Celularpt_BR
dc.contributor.butantanAndrade-Silva, Débora|:Lab. de Toxinologia Aplicadapt_BR
dc.contributor.butantanSerrano, Solange Maria de Toledo|:Pesquisador|:Lab. de Toxinologia Aplicadapt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2013/13548-4pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2013/07467-1pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2017/09929-3pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2015/23017-1pt_BR
dc.sponsorship.butantan(CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico¦¦308133/2015-3pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.fulltextCom Texto completo-
item.languageiso639-1English-
item.grantfulltextembargo_20990101-
item.openairetypeArticle-
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