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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 A 2  (PLA 2 s), one of which is presumably an enzymatically active Asp49 and two are very likely enzymatically inactive Lys49 PLA 2  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 PLA 2 s from  Bothrops  species. The PLA 2 s isolated were named BmatTX-I (Lys49 PLA 2 -like), BmatTX-II (Lys49 PLA 2 -like), and BmatTX-III (Asp49 PLA 2 ). The PLA 2 s 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.

biomed research international

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

Purification and Biochemical Characterization of Three Myotoxins fromBothrops mattogrossensisSnake Venom with Toxicity againstLeishmaniaand Tumor Cells