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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.)

Analysis of the Ontogenetic Variation in the Venom Proteome/Peptidome of Bothrops jararaca Reveals Different Strategies to Deal with Prey

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Author(s):
Zelanis, Andre [1, 2] ; Tashima, Alexandre K. [3, 2] ; Rocha, Marisa M. T. [4] ; Furtado, Maria F. [4] ; Camargo, Antonio C. M. [2] ; Ho, Paulo L. [1, 5] ; Serrano, Solange M. T. [2]
Total Authors: 7
Affiliation:
[1] Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-05508 Sao Paulo - Brazil
[2] Inst Butantan, Lab Especial Toxinol Aplicada CAT CEPID, BR-05503900 Sao Paulo - Brazil
[3] Univ Fed Sao Paulo, Dept Ciencias Exatas & Terra, Sao Paulo - Brazil
[4] Inst Butantan, Lab Herpetol, BR-05503900 Sao Paulo - Brazil
[5] Inst Butantan, Ctr Biotecnnol, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 5
Document type: Journal article
Source: JOURNAL OF PROTEOME RESEARCH; v. 9, n. 5, p. 2278-2291, MAY 2010.
Web of Science Citations: 73
Abstract

Previous studies have demonstrated that the pharmacological activities displayed by Bothrops jararaca venom undergo a significant ontogenetic shift. Variation in the venom proteome is a well-documented phenomenon; however, variation in the venom peptidome is poorly understood. We report a comparative proteomic and peptidomic analysis of venoms from newborn and adult specimens of B. jararaca and correlate it with the evaluation of important venom features. We demonstrate that newborn and adult venoms have similar hemorrhagic activities, while the adult venom has a slightly higher lethal activity in mice; however, the newborn venom is extremely more potent to kill chicks. The coagulant activity of newborn venom upon human plasma is 10 times higher than that of adult venom. These differences were clearly reflected in their different profiles of SDS-PAGE, gelatin zimography, immunostaining using specific antibodies, glycosylation pattern, and concanavalin A-binding proteins. Furthermore, we report for the first time the analysis of the peptide fraction of newborn and adult venoms by MALDI-TOF mass spectrometry and LC-MS/MS, which revealed different contents of peptides, while the bradykinin potentiating peptides (BPPs) showed rather similar profiles and were detected in the venoms showing their canonical sequences and also novel sequences corresponding to BPPs processed from their precursor protein at sites so far not described. As a result of these studies, we demonstrated that the ontogenetic shift in diet, from ectothermic prey in early life to endothermic prey in adulthood, and in animal size are associated with changes in the venom proteome in B. jararaca species. (AU)

FAPESP's process: 98/14307-9 - Center for Applied Toxinology
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC