Bothrops moojeni myotoxin-II, an example of function versatility of snake venom proteins / MIOTOXINA-II DE Bothrops moojeni, UM EXEMPLO DE VERSATILIDADE FUNCIONAL DE UMA PROTEÍNA DO VENENO DE SERPENTES.

AUTOR(ES)
DATA DE PUBLICAÇÃO

2005

RESUMO

MjTX-II, a myotoxic phospholipase A2 (PLA2) homologue from Bothrops moojeni venom, was purified using a single-step CM-Sepharose-FF 9 x 190 mm chromatography procedure, liofilized, functionally and structurally characterized. The MjTX-II characterization included: (i) functional characterization (antitumoral, antimicrobial and antiparasitic effects); (ii) effects of structural modifications by 4-bromophenacyl bromide (BPB), cyanogen bromide (CNBr), acetic anhydride and 2-nitrobenzenesulphonyl fluoride (NBSF); (iii) enzymatic characterization: inhibition by low molecular weight heparin and EDTA; and (iv) molecular characterization: cDNA sequence and molecular structure prediction. The results demonstrated that MjTX-II displayed antimicrobial activity by growth inhibition against Escherichia coli and Candida albicans, antitumoral activity against Erlich ascitic tumor (EAT), human breast adenocarcinoma (SK-BR-3) and human T leukemia cells (JURKAT) and antiparasitic effects against Schistosoma mansoni and Leishmania spp., which makes MjTX-II a promising molecular model for future therapeutic applications, as well as other multifunctional homologous Lys49-PLA2s or even derived peptides. This work provides useful insights into the structural determinants of the action of Lys49-PLA2 homologues and, together with additional strategies, supports the concept of the presence of others bioactive sites distinct from the catalytic site in snake venom myotoxic PLA2s.

ASSUNTO(S)

serpentes myotoxin snake biologia geral veneno miotoxina venom

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