We report the comparative proteomic characterization of the venoms of Bothrops atrox, B. barnetti and B. pictus. The venoms were subjected to RP-HPLC and the resulting fractions analyzed by SDS-PAGE. The proteins were cut from the gels, digested with trypsin and identified via peptide mass fingerprint and manual sequencing of selected peptides by MALDI-TOF/TOF mass spectrometry. Around 20-25 proteins were identified belonging to only 6-7 protein families. Metalloproteinases of the classes P-I and P-III were the most abundant proteins in all venoms (58-74% based on peak area A214 nm), followed by phospholipases-A 2 (6.4-14%), disintegrins (3.2-9%) and serine proteinases (7-11%), and some of these proteins occurred in several isoforms. In contrast cysteine-rich secretory proteins and L-amino acid oxidases appeared only as single isoforms and were found only in B. atrox and B. barnetti. C-type lectins were also detected in all venoms but at low levels (~ 5%). Furthermore, the venoms contain variable numbers of peptides (<3kDa) and non-protein compounds which were not considered in this work. The protein composition of the investigated Bothrops species is in agreement with their pharmacological and pathological effects.
Bibliographical noteFunding Information:
We thank Prof. F.S. Markland (University of Southern California) for critical comments. This work was supported by the Brazilian Agencies Fundação de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG, Grants: CBB 359/06 and CBB-APQ-01791-10 to EFS) and Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) .
Copyright 2012 Elsevier B.V., All rights reserved.
- Bothrops atrox
- Bothrops barnetti
- Bothrops pictus
- Snake venomics