Contribution of baltergin to the bactericidal activity exhibited by Bothrops alternatus venom.

RODRIGUEZ J.; BUSTILLO S.; GAY C.; LEIVA L.; ACOSTA O.

Tandil, Buenos Aires

Congreso; XL Reunión Anual de la Asociación Argentina de Farmacología Experimental; 2008

Asociación Argentina de Farmacología Experimental

We have previously demonstrated the bactericidal activity of B. alternatus venom against Gram (-) and Gram (+) strains. Baltergin is a metalloproteinase enzyme isolated from B. alternatus venom, with an extensive biological toxicity. In this work, we examined the microbicidal role of baltergin and its contribution to the antimicrobial activity exhibited by the whole venom against Staphilococus aureus (ATCC 25923). A turbidimetric method was employed to measure the bactericidal activity of the enzyme. Inhibitory concentration 50 (IC50) was defined as the concentration of toxin needed to reduce the 50% of bacterial growth. To evaluate the contribution of this toxin, antibodies against baltergin were produced in rabbits and neutralization was developed using inhibitory halos test. The enzyme showed a high bactericidal activity (IC50 70 mg/ml) and the neutralization assay demonstrated that this hemorrhagin contributed to 45% of the total activity exhibited by the venom. These results show that baltergin, would be a microbicidal protein emerging as a promising therapeutic alternative to cope with the increasing rates of antibiotic resistance encountered worldwide.