Biochemical characterization of the venom of the Bolivian endemic pit viper .

Ophidic accidents are an important public health problem in South America, specifically those related to the genus, due to their high incidence, complexity and severity of envenomation symptoms. The species , the only one from this genus endemic to Bolivia, is the most frequently found and involved in snakebites in the Chapare region of Cochabamba; however, its toxicological implications on human health are poorly known. Herein we conducted the first biochemical characterization of its venom. Its electrophoretic profile showed components mainly ranging from ∼10 to 37 kDa, resembling other venoms. The venom exhibited high activity on azocasein (47.65 U/mg) and the thrombin-specific substrate S-2238 (625.55 μmol/min/mg), and noticeably hydrolyzed gelatin and human fibrin(ogen). The venom also degraded lecithin and hyaluronic acid, but both at low levels. These results point out a toxic mechanism of action fundamentally at a local level, with tissue damage likely caused (although not exclusively) by SVMPs. Immunochemical reactivity was evaluated against antivenoms produced in Argentina, which not only exhibited cross-reaction by Western Blotting but also neutralized the procoagulant activity of the venom. This study offers first insights into the venom components of , and provides preliminary and important information about the pathophysiological mechanisms involved in the envenomation by this species, paving the way for treatment strategies in such accidents.