Snake venom metalloproteinase (Vipera ammodytes and Vipera berus) (SVMP)

Snake venom metalloproteinases (SVMPs) from Vipera ammodytes (nose-horned viper) and Vipera berus (common adder) are primary toxic enzymes responsible for the local and systemic pathologies associated with European viper envenomation (Slagboom et al., 2017). These zinc-dependent enzymes belong to the M12B reprolysin family and are classified into P-I, P-II, and P-III groups based on their domain structure, which often includes disintegrin-like and cysteine-rich domains (Leonardi et al., 2019). Their biological function involves the rapid degradation of basement membrane components, such as type IV collagen, fibronectin, and laminin, leading to capillary rupture and profuse hemorrhage (Latinovic et al., 2016). Furthermore, they contribute to coagulopathy by activating prothrombin or degrading fibrinogen, which complicates the clinical presentation of snakebite (WHO, 2021). Therapeutic intervention primarily relies on the administration of polyvalent antivenoms, such as ViperaTab or European Viper Antivenom, which contain antibodies that neutralize the enzymatic activity of these proteins. Recent research also explores the use of small-molecule inhibitors like batimastat and marimastat, which act by chelating the essential zinc ion in the catalytic site to prevent tissue necrosis (Ainsworth et al., 2020).

Other names

Hemorrhagic toxinVipera metalloproteinaseAmmodytaseBeruslysinZinc-metalloproteinaseSnake venom reprolysin

Antibody-mediated neutralization of enzymatic activity; Zinc-dependent catalytic site inhibition via chelation or competitive binding.