Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
Andrade-Silva, Debora ; Zelanis, Andre ; Kitano, Eduardo S. ; Junqueira-de-Azevedo, Inacio L. M. ; Reis, Marcelo S. ; Lopes, Aline S. ; Serrano, Solange M. T.
Total Authors: 7
Document type: Journal article
Source: JOURNAL OF PROTEOME RESEARCH; v. 15, n. 8, p. 2658-2675, AUG 2016.
Web of Science Citations: 9
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. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 13/13548-4 - Proteomic/Glycoproteomic characterization of the venoms of the Bothrops jararaca complex with emphasis on the N-terminome and N-glycome of toxins
Grantee:Solange Maria de Toledo Serrano
Support type: Regular Research Grants