Snake venom metalloproteinase (SVMP)

Snake venom metalloproteinase (SVMP) is a zinc-dependent proteolytic enzyme abundantly present in viper and some elapid snake venoms[1][2]. SVMPs are responsible for the prominent hemorrhagic, necrotic, and inflammatory effects seen in snakebite victims, through enzymatic degradation of extracellular matrix proteins, disruption of endothelial cell adhesion, activation or inhibition of blood coagulation pathways, and platelet dysfunction[1][2]. SVMPs have multidomain structures and are classified as P-I (catalytic domain only), P-II (catalytic + disintegrin domain), or P-III (catalytic + disintegrin-like + cysteine-rich domains), with some P-III variants also including a lectin domain[1][2]. These enzymes are the primary drivers of local tissue destruction, inflammation, and hemorrhage following envenomation, and their pathological actions are difficult to neutralize with conventional antivenoms[1][3]. Due to their functional homology to mammalian matrix metalloproteinases and ADAM proteins, SVMPs are also studied as models for human inflammatory and neoplastic processes[1]. Inhibitors targeting the zinc-binding motif of SVMPs are under investigation as possible adjunctive therapies for snakebite envenomation[3].

Other names

SVMPSnake venom metalloproteaseVenom metalloproteinaseReprolysin (M12B) family enzyme

Chelation of active site zinc, inhibiting proteolytic activity; Inhibition of enzyme-substrate binding; Blocking cleavage of extracellular matrix and blood coagulation proteins