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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Individual Variability in the Venom Proteome of Juvenile Bothrops jararaca Specimens

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Author(s):
Dias, Gabriela S. [1] ; Kitano, Eduardo S. [1, 2] ; Pagotto, Ana H. [1] ; Sant'anna, Savio S. [3] ; Rocha, Marisa M. T. [3] ; Zelanis, Andre [1] ; Serrano, Solange M. T. [1]
Total Authors: 7
Affiliation:
[1] Inst Butantan, CeTICS, Lab Especial Toxinol Aplicada, BR-05503900 Sao Paulo - Brazil
[2] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05508070 Sao Paulo - Brazil
[3] Inst Butantan, Lab Herpetol, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: JOURNAL OF PROTEOME RESEARCH; v. 12, n. 10, p. 4585-4598, OCT 2013.
Web of Science Citations: 27
Abstract

Snake venom proteomes/peptidomes are highly complex and subject to ontogenetic changes. Individual variation in the venom proteome of juvenile snakes is poorly known. We report the proteomic analysis of venoms from 21 juvenile specimens of Bothrops jararaca of different geographical origins and correlate it with the evaluation of important venom features. Individual venoms showed similar caseinolytic activities; however, their amidolytic activities were significantly different. Rather intriguingly, plasma coagulant activity showed remarkable variability among the venoms but not the prothrombin-activating activity. LC-MS analysis showed significant differences between venoms; however, an interesting finding was the ubiquitous presence of the tripeptide ZKW, an endogenous inhibitor of metalloproteinases. Electrophoretic profiles of proteins submitted to reduction showed significant variability in total proteins, glycoproteins, and in the subproteomes of proteinases. Moreover, identification of differential bands revealed variation in most B. jararaca toxin classes. Profiles of venoms analyzed under non reducing conditions showed less individual variability and identification of proteins in presence of metalloproteinases and L-amino acid oxidase as common components of these venoms. Taken together, our findings suggest that individual venom proteome variability in B. jararaca exists from a very early animal age and is not a result of ontogenetic and diet changes. (AU)

FAPESP's process: 11/11308-0 - Proteomic analysis of leaves of sugarcane cultivars and genotypes
Grantee:Eduardo Shigueo Kitano
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 98/14307-9 - Center for Applied Toxinology
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC