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BioMed Research International
Volume 2014, Article ID 195356, 13 pages
Research Article

Purification and Biochemical Characterization of Three Myotoxins from Bothrops mattogrossensis Snake Venom with Toxicity against Leishmania and Tumor Cells

1Centro de Estudos de Biomoléculas Aplicadas à Saude, CEBio, Fundação Oswaldo Cruz, Fiocruz Rondônia e Departamento de Medicina, Núcleo de Saúde, Universidade Federal de Rondônia, UNIR, 76812–245 Porto Velho, RO, Brazil
2Fundação Oswaldo Cruz, Fiocruz Rondônia, 76812–245 Porto Velho, RO, Brazil
3Departamento de Biologia Celular e Molecular, Instituto de Biologia, Universidade Federal Fluminense, UFF, 24020-141 Niterói, RJ, Brazil
4Faculdade de Ciências Farmacêuticas, FCFRP, Universidade de São Paulo, USP, 14040-903 Ribeirão Preto, SP, Brazil
5Universidade Federal de São João del Rei, UFSJ, 36420-000 Ouro Branco, MG, Brazil

Received 16 September 2013; Accepted 3 December 2013; Published 3 March 2014

Academic Editor: Fernando Albericio

Copyright © 2014 Andréa A. de Moura et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Bothrops mattogrossensis snake is widely distributed throughout eastern South America and is responsible for snakebites in this region. This paper reports the purification and biochemical characterization of three new phospholipases A2 (PLA2s), one of which is presumably an enzymatically active Asp49 and two are very likely enzymatically inactive Lys49 PLA2 homologues. The purification was obtained after two chromatographic steps on ion exchange and reverse phase column. The 2D SDS-PAGE analysis revealed that the proteins have pI values around 10, are each made of a single chain, and have molecular masses near 13 kDa, which was confirmed by MALDI-TOF mass spectrometry. The N-terminal similarity analysis of the sequences showed that the proteins are highly homologous with other Lys49 and Asp49 PLA2s from Bothrops species. The PLA2s isolated were named BmatTX-I (Lys49 PLA2-like), BmatTX-II (Lys49 PLA2-like), and BmatTX-III (Asp49 PLA2). The PLA2s induced cytokine release from mouse neutrophils and showed cytotoxicity towards JURKAT (leukemia T) and SK-BR-3 (breast adenocarcinoma) cell lines and promastigote forms of Leishmania amazonensis. The structural and functional elucidation of snake venoms components may contribute to a better understanding of the mechanism of action of these proteins during envenomation and their potential pharmacological and therapeutic applications.