Comparative Hemostatic Effects of Bothrops spp. and Daboia russelii Venoms

Venoms from Bothrops species and Daboia russelii are among the leading causes of venom-induced coagulopathy and snakebite-related deaths. In this study, we comparatively evaluated the biochemical composition and hemostatic effects of venoms from seven Bothrops species and D. russelii using protein profiling and functional coagulation assays. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed broadly similar molecular weight distributions between the two genera, consistent with the presence of snake venom metalloproteinases, serine proteases, and phospholipases A₂, but with notable interspecific variability among Bothrops venoms. Enzymatic assays demonstrated heterogeneous metalloproteinase, serine protease, and phospholipase A₂ activities across Bothrops species, whereas D. russelii venom showed strong phospholipase A₂ activity and limited fibrinogenolytic activity. Functional coagulation analyses revealed marked differences between the genera. Bothrops venoms induced rapid clot initiation, with alterations in clot formation observed in a species-dependent manner, accompanied by pronounced fibrinogen degradation, consistent with consumption coagulopathy driven by fibrinogenolysis and clot destabilization. In contrast, D. russelii venom exhibited a strong procoagulant profile, significantly reducing prothrombin time and activated partial thromboplastin time, with minimal direct fibrinogen degradation. Previous studies have shown that D. russelii venom also promotes rapid clot formation in rotational thromboelastometry assays. Together, these findings demonstrate that Bothrops spp. and D. russelii venoms converge functionally in disrupting hemostasis but do so through distinct biochemical strategies, providing experimental support for the divergent coagulation phenotypes observed clinically.