Bothrops asper venom toxins (BaV) (BaV)

Bothrops asper venom toxins represent a complex cocktail of bioactive proteins and peptides responsible for the severe clinical manifestations of envenomation by the terciopelo snake. The venom is primarily composed of snake venom metalloproteinases (SVMPs), phospholipases A2 (PLA2s), and serine proteinases, which collectively disrupt the vascular endothelium, degrade extracellular matrix components, and interfere with the coagulation cascade (Gutiérrez et al., 2009, Toxicon). SVMPs are the major drivers of local and systemic hemorrhage, while PLA2s contribute significantly to myonecrosis and inflammatory responses (UniProt, 2024). Clinically, these toxins lead to tissue loss, permanent disability, or death if not neutralized promptly. Therapeutic management relies on polyvalent antivenoms that utilize equine or ovine antibodies to bind and clear the toxins from the circulation (WHO, 2021). Recent pharmacological research has identified small-molecule inhibitors like varespladib (a PLA2 inhibitor) and various metalloproteinase inhibitors as potential adjuncts to traditional antivenom therapy (Lewin et al., 2016, J Med Toxicol).

Other names

Terciopelo venomFer-de-lance venomBothrops asper snake venom

Neutralization of toxic components via antibody binding or competitive inhibition of enzymatic active sites.