Hemotoxic and coagulotoxic snake venom toxins (Viperidae) (SVTs)

Hemotoxic and coagulotoxic snake venom toxins from the Viperidae family are a diverse group of proteins that disrupt the circulatory system and tissue integrity of the victim. These toxins primarily include snake venom metalloproteinases (SVMPs), snake venom serine proteases (SVSPs), phospholipases A2 (PLA2s), and disintegrins (Slagboom et al., 2017, Toxins). SVMPs are responsible for degrading the vascular basement membrane, leading to systemic hemorrhage, while SVSPs often act as thrombin-like enzymes that deplete fibrinogen, causing consumptive coagulopathy (Gutiérrez et al., 2016, Nature Reviews Disease Primers). PLA2s contribute to local tissue necrosis and inflammation by hydrolyzing phospholipids and releasing arachidonic acid. These toxins are the therapeutic targets for antivenoms, such as CroFab and Anavip, which use purified antibodies to bind and neutralize the venom components (FDA, 2018). Emerging small-molecule therapies like Varespladib target the enzymatic activity of PLA2s, and metalloproteinase inhibitors like Marimastat are being investigated to prevent the devastating tissue damage associated with viper bites (Lewin et al., 2016, J Med Toxicol). The complexity of these venom mixtures necessitates broad-spectrum or polyvalent therapeutic approaches to ensure clinical efficacy across different species.

Other names

Viperid venom toxinsHemotoxinsCoagulotoxinsSnake venom metalloproteinasesSnake venom serine proteasesSnake venom phospholipase A2SVMPsSVSPsPLA2s

Neutralization of toxin activity through antibody binding (antivenom), competitive inhibition of enzymatic sites (e.g., PLA2 inhibition by Varespladib), or chelation of essential metal cofactors (e.g., zinc chelation in SVMPs).