Proteomic and Glycoproteomic Profilings Reveal That Post- translational Modifications of Toxins Contribute to Venom Phenotype in Snakes

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dc.contributor.author Andrade-Silva, Debora
dc.contributor.author Zelanis, Andre [UNIFESP]
dc.contributor.author Kitano, Eduardo S.
dc.contributor.author Junqueira-de-Azevedo, Inacio L. M.
dc.contributor.author Reis, Marcelo S.
dc.contributor.author Lopes, Aline S. [UNIFESP]
dc.contributor.author Serrano, Solange M. T.
dc.date.accessioned 2020-08-14T13:43:59Z
dc.date.available 2020-08-14T13:43:59Z
dc.date.issued 2016
dc.identifier http://dx.doi.org/10.1021/acs.jproteome.6b00217
dc.identifier.citation Journal Of Proteome Research. Washington, v. 15, n. 8, p. 2658-2675, 2016.
dc.identifier.issn 1535-3893
dc.identifier.uri https://repositorio.unifesp.br/handle/11600/57477
dc.description.abstract Snake venoms are biological weapon systems composed of secreted proteins and peptides that are used for immobilizing or killing prey. Although post-translational modifications are widely investigated because of their importance in many biological phenomena, we currently still have little understanding of how protein glycosylation impacts the variation and stability of venom proteomes. To address these issues, here we characterized the venom proteomes of seven Bothrops snakes using a shotgun proteomics strategy. Moreover, we compared the electrophoretic profiles of native and deglycosylated venoms and, in order to assess their subproteomes of glycoproteins, we identified the proteins with affinity for three lectins with different saccharide specificities and their putative glycosylation sites. As proteinases are abundant glycosylated toxins, we examined the effect of N-deglycosylation on their catalytic activities and show that the proteinases of the seven venoms were similarly affected by removal of N-glycans. Moreover, we prospected putative glycosylation sites of transcripts of a B. jararaca venom gland data set and detected toxin family related patterns of glycosylation. Based on our global analysis, we report that Bothrops venom proteomes and glycoproteomes contain a core of components that markedly define their composition, which is conserved upon evolution in parallel to other molecular markers that determine their phylogenetic classification. en
dc.description.sponsorship Fundacao de Amparo a Pesquisa do Estado de Sao Paulo
dc.description.sponsorship Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
dc.format.extent 2658-2675
dc.language.iso eng
dc.publisher Amer Chemical Soc
dc.relation.ispartof Journal Of Proteome Research
dc.rights Acesso restrito
dc.subject glycoproteome en
dc.subject lectin-affinity chromatography en
dc.subject mass spectrometry en
dc.subject peptidome en
dc.subject proteome en
dc.subject snake venom en
dc.subject transcriptome en
dc.title Proteomic and Glycoproteomic Profilings Reveal That Post- translational Modifications of Toxins Contribute to Venom Phenotype in Snakes en
dc.type Artigo
dc.description.affiliation Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Especial Toxinol Aplicada, BR-05503000 Sao Paulo, Brazil
dc.description.affiliation Univ Fed Sao Paulo ICT UNIFESP, Inst Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, Brazil
dc.description.affiliation Univ Fed Sao Paulo, Dept Ciencias Exatas & Terra, BR-04021001 Diadema, Brazil
dc.description.affiliationUnifesp Univ Fed Sao Paulo ICT UNIFESP, Inst Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, Brazil
dc.description.affiliationUnifesp Univ Fed Sao Paulo, Dept Ciencias Exatas & Terra, BR-04021001 Diadema, Brazil
dc.description.sponsorshipID FAPESP: 2013/07467-1
dc.description.sponsorshipID FAPESP: 2013/13548-4
dc.identifier.doi 10.1021/acs.jproteome.6b00217
dc.description.source Web of Science
dc.identifier.wos WOS:000381235900028
dc.coverage Washington
dc.citation.volume 15
dc.citation.issue 8



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