Daboia siamensis coagulation factor V activator (RVV-V)

Daboia siamensis coagulation factor V activator, commonly referred to as RVV-V, is a specialized serine protease found in the venom of the Eastern Russell's Viper (Daboia siamensis) (UniProt: P00771). This enzyme plays a critical role in the pathophysiology of envenomation by specifically cleaving and activating human coagulation factor V at the Arg1545-Ser1546 peptide bond (PubMed: 11461395). Unlike thrombin, RVV-V does not act on fibrinogen, but its activation of factor V leads to the rapid assembly of the prothrombinase complex, resulting in massive thrombin generation and subsequent venom-induced consumption coagulopathy (VICC) (PubMed: 25448271). In clinical medicine, RVV-V is a primary target for neutralization by monovalent and polyvalent antivenoms to prevent fatal hemorrhaging in snakebite victims (WHO Guidelines). Furthermore, it serves as an essential diagnostic tool in hematology laboratories for measuring factor V activity and identifying the Factor V Leiden mutation (StatPearls). The high specificity of this toxin makes it a subject of interest for understanding protease-substrate interactions in the blood coagulation cascade.

Other names

Russell's viper venom factor V activatorRVV-VFactor V-activating enzymeDS-VDaboia siamensis factor V activator

The toxin acts as a highly specific serine protease that catalyzes the proteolytic activation of coagulation factor V by cleaving the Arg1545-Ser1546 peptide bond, converting the procofactor into its active form (Va) and promoting the formation of the prothrombinase complex (PubMed: 11461395).