Russell's viper venom metalloproteinase (RVV-MP)

Russell’s viper venom metalloproteinases (RVV-MPs) are a diverse group of zinc-dependent enzymes found in the venom of the Russell’s viper (Daboia russelii and Daboia siamensis). These enzymes are primary drivers of the systemic toxicity associated with envenomation, functioning as potent procoagulants and hemorrhagins. The most prominent member, Russell's viper venom factor X activator (RVV-X), specifically activates blood coagulation factor X, leading to rapid, uncontrolled thrombin generation and consumptive coagulopathy. Other RVV-MPs, such as daborhagin, target the vascular endothelium and basement membrane by degrading proteins like collagen, fibronectin, and laminin, which results in severe systemic hemorrhage and tissue necrosis. Due to their critical role in causing life-threatening conditions like acute renal failure and shock, RVV-MPs are major targets for therapeutic intervention. Current treatments rely on animal-derived antivenoms, but research is increasingly focused on small-molecule inhibitors like marimastat and batimastat to provide more accessible and rapid neutralization of these toxins.

Other names

Russell's viper venom factor X activatorRVV-XDaborhaginSnake venom metalloproteinaseSVMPRussell's viper venom procoagulant

Zinc-dependent hydrolysis of peptide bonds in coagulation factors (specifically Factor X and prothrombin) and extracellular matrix components (collagen, fibronectin, laminin).