Proteomic and glycoproteomic profilings reveal that posttranslational modifications of toxins contribute to venom phenotype in snakes

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dc.citation.issue8
dc.citation.volume15
dc.contributor.authorAndrade-Silva, Debora
dc.contributor.authorZelanis, Andre [UNIFESP]
dc.contributor.authorKitano, Eduardo Shigueo
dc.contributor.authorJunqueira-de-Azevedo, Inácio de Loiola Meirelles
dc.contributor.authorReis, Marcelo da Silva
dc.contributor.authorLopes, Aline Soriano [UNIFESP]
dc.contributor.authorSerrano, Solange Maria de Toledo
dc.coverageWashington
dc.date.accessioned2020-08-14T13:43:59Z
dc.date.available2020-08-14T13:43:59Z
dc.date.issued2016
dc.description.abstractSnake 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.affiliationInst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Especial Toxinol Aplicada, BR-05503000 Sao Paulo, Brazil
dc.description.affiliationUniv Fed Sao Paulo ICT UNIFESP, Inst Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Ciencias Exatas & Terra, BR-04021001 Diadema, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo ICT UNIFESP, Inst Ciencia & Tecnol, BR-12231280 Sao Jose Dos Campos, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Ciencias Exatas & Terra, BR-04021001 Diadema, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
dc.description.sponsorshipIDFAPESP: 2013/07467-1
dc.description.sponsorshipIDFAPESP: 2013/13548-4
dc.format.extent2658-2675
dc.identifierhttps://dx.doi.org/10.1021/acs.jproteome.6b00217
dc.identifier.citationJournal Of Proteome Research. Washington, v. 15, n. 8, p. 2658-2675, 2016.
dc.identifier.doi10.1021/acs.jproteome.6b00217
dc.identifier.issn1535-3893
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/57477
dc.identifier.wosWOS:000381235900028
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal Of Proteome Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectGlycoproteomeen
dc.subjectLectin-affinity chromatographyen
dc.subjectMass spectrometryen
dc.subjectPeptidomeen
dc.subjectProteomeen
dc.subjectSnake venomen
dc.subjectTranscriptomeen
dc.titleProteomic and glycoproteomic profilings reveal that posttranslational modifications of toxins contribute to venom phenotype in snakesen
dc.typeinfo:eu-repo/semantics/article
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