Structures of N-glycans of Bothrops venoms revealed as molecular signatures that contribute to venom phenotype in viperid snakes

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dc.contributor(LETA) Lab. Toxinologia Aplicadapt_BR
dc.contributorCentro de Desenvolvimento Culturalpt_BR
dc.contributor(LCC) Lab. Ciclo Celularpt_BR
dc.contributor(CeTICS) Centro de Toxinas, Resposta-imune e Sinalização Celularpt_BR
dc.contributor.authorAndrade-Silva, Déborapt_BR
dc.contributor.authorAshline, Davidpt_BR
dc.contributor.authorTran, Thuypt_BR
dc.contributor.authorLopes, Aline Sorianopt_BR
dc.contributor.authorTravaglia-Cardoso, Silvia Reginapt_BR
dc.contributor.authorReis, Marcelo da Silvapt_BR
dc.contributor.authorZelanis, Andrépt_BR
dc.contributor.authorSerrano, Solange Maria de Toledopt_BR
dc.contributor.authorReinhold, Vernonpt_BR
dc.date.accessioned2020-07-09T21:20:35Z-
dc.date.available2020-07-09T21:20:35Z-
dc.date.issued2018pt_BR
dc.identifier.citationAndrade-Silva D, Ashline D, Tran T, Lopes AS, Travaglia-Cardoso SR, Reis MS, et al. Structures of N-glycans of Bothrops venoms revealed as molecular signatures that contribute to venom phenotype in viperid snakes. Mol. Cell. Proteomics. 2018 Jul;17(7):1261-84. doi:10.1074/mcp.RA118.000748.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2504-
dc.description.abstractThe complexity of snake venoms has long been investigated to explore a myriad of biologically active proteins and peptides that are used for immobilizing or killing prey, and are responsible for the pathological effects observed on envenomation. Glycosylation is the main post-translational modification (PTM) of viperid venoms but currently there is little understanding of how protein glycosylation impacts the variation of venom proteomes. We have previously reported that Bothrops venom glycoproteomes contain a core of components that markedly define their composition and parallel their phylogenetic classification. Here we extend those observations to eight Bothrops species evaluating the N-glycomes by LC-MS as assigned cartoon structures and detailing those structures separately as methylated analogs using ion-trap mass spectrometry (MSn). Following ion disassembly through multiple steps provided sequence and linkage isomeric details that characterized 52 unique compositions in Bothrops venoms. These occurred as 60 structures, of which 26 were identified in the venoms of the Jararaca Complex (B. alcatraz, B. insularis, and B. jararaca), 20 in B. erythromelas, B. jararacussu, B. moojeni and B. neuwiedi venoms, and 22 in B. cotiara venom. Further, quantitative analysis of these N-glycans showed variable relative abundances in the venoms. For the first time a comprehensive set of N-glycan structures present in snake venoms are defined. Despite the fact that glycosylation is not template-defined, the N-glycomes of these venoms mirror the phylogeny cladograms of South American bothropoid snakes reported in studies on morphological, molecular data and feeding habits, exhibiting distinct molecular signatures for each venom. Considering the complexity of N-glycan moieties generally found in glycoproteins, characterized by different degrees of branching, isomer structures, and variable abundances, our findings point to these factors as another level of complexity in Bothrops venoms, features that could dramatically contribute to their distinct biological activities.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.extentp. 1261-1284pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofMolecular & Cellular Proteomicspt_BR
dc.rightsOpen accesspt_BR
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/pt_BR
dc.titleStructures of N-glycans of Bothrops venoms revealed as molecular signatures that contribute to venom phenotype in viperid snakespt_BR
dc.typeArticlept_BR
dc.rights.licenseCC BYpt_BR
dc.identifier.doi10.1074/mcp.RA118.000748pt_BR
dc.identifier.urlhttp://dx.doi.org/10.1074/mcp.RA118.000748pt_BR
dc.contributor.externalUniversity of New Hampshire¦¦Estados Unidospt_BR
dc.contributor.external(UNIFESP) Universidade Federal de São Paulopt_BR
dc.identifier.citationvolume17pt_BR
dc.identifier.citationissue7pt_BR
dc.subject.keywordvenomspt_BR
dc.subject.keywordN-Glycosylationpt_BR
dc.subject.keywordmass spectrometrypt_BR
dc.subject.keywordGlycomicspt_BR
dc.subject.keywordGlycoproteomicspt_BR
dc.subject.keywordBothropspt_BR
dc.subject.keywordSnake venom variabilitypt_BR
dc.relation.ispartofabbreviatedMol Cell Proteomicspt_BR
dc.identifier.citationabntv. 17, n. 7, p. 1261-1284, jul. 2018pt_BR
dc.identifier.citationvancouver2018 Jul;17(7):1261-84pt_BR
dc.contributor.butantanTravaglia-Cardoso, Silvia Regina|:Pesquisador|:Museu Biológico|:pt_BR
dc.contributor.butantanAndrade-Silva, Débora|:Aluno|:(LETA) Lab. Toxinologia Aplicada|:PrimeiroAutorpt_BR
dc.contributor.butantanReis, Marcelo da Silva|:Pesquisador|:LCC - Laboratório de Ciclo Celular:Centro de Toxinas, Resposta-imune e Sinalização Celular (CeTICS)|:pt_BR
dc.contributor.butantanSerrano, Solange Maria de Toledo|:Pesquisador:Docente Permanente PPGTOX|:(LETA) Lab. Toxinologia Aplicada|:Autor de correspondênciapt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦308133/2015-3pt_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)¦¦2014/12245-0pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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