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

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

Author Andrade-Silva, Debora Google Scholar
Zelanis, Andre Autor UNIFESP Google Scholar
Kitano, Eduardo S. Google Scholar
Junqueira-de-Azevedo, Inacio L. M. Google Scholar
Reis, Marcelo S. Google Scholar
Lopes, Aline S. Autor UNIFESP Google Scholar
Serrano, Solange M. T. Google Scholar
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.
Keywords glycoproteome
lectin-affinity chromatography
mass spectrometry
snake venom
xmlui.dri2xhtml.METS-1.0.item-coverage Washington
Language English
Sponsor Fundacao de Amparo a Pesquisa do Estado de Sao Paulo
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
Grant number FAPESP: 2013/07467-1
FAPESP: 2013/13548-4
Date 2016
Published in Journal Of Proteome Research. Washington, v. 15, n. 8, p. 2658-2675, 2016.
ISSN 1535-3893 (Sherpa/Romeo, impact factor)
Publisher Amer Chemical Soc
Extent 2658-2675
Access rights Closed access
Type Article
Web of Science ID WOS:000381235900028

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