Russell's viper venom serine protease (RVV-SP)

Russell's viper venom serine proteases (SVSPs) are a group of enzymatic toxins found in the venom of the Russell's viper (Daboia russelii), a snake of significant medical importance in South and Southeast Asia [1.1.1, 1.3.2]. The most prominent member of this family is the Factor V activator (RVV-V), which specifically cleaves and activates host coagulation Factor V, leading to the assembly of the prothrombinase complex and the rapid generation of thrombin [1.3.3, 1.4.1]. This procoagulant activity results in venom-induced consumptive coagulopathy (VICC), characterized by the depletion of clotting factors and a high risk of life-threatening hemorrhage or thrombosis [1.1.3, 1.4.3]. SVSPs are the primary targets of therapeutic antivenoms and are being investigated as targets for small-molecule inhibitors like nafamostat to improve treatment accessibility [1.2.1, 1.2.2]. Beyond their role in envenomation, these proteases are also employed as diagnostic reagents in the dilute Russell's Viper Venom Time (dRVVT) test to detect lupus anticoagulants in patient plasma [1.4.2].

Other names

Factor V activatorRVV-VSnake venom serine proteaseSVSPDaboia russelii serine proteaseAlpha-fibrinogenaseBeta-fibrinogenase

Inhibition of the serine protease catalytic triad (His57, Asp102, Ser195) to prevent the proteolytic activation of Factor V and other coagulation factors, thereby inhibiting the formation of the prothrombinase complex and preventing venom-induced consumptive coagulopathy.