Multiple snake venom toxins (SVTs)

Multiple snake venom toxins comprise a complex mixture of proteins and peptides that evolved for prey capture and defense, and they are the primary causative agents of snakebite envenomation, a WHO-recognized neglected tropical disease (WHO, 2021). These toxins are classified into several major families, including phospholipases A2 (PLA2s), snake venom metalloproteinases (SVMPs), three-finger toxins (3FTxs), and serine proteases, each targeting specific physiological pathways such as the neuromuscular junction or the coagulation cascade (UniProt, 2023; PubMed, 2020). PLA2s and SVMPs are particularly noted for causing systemic hemotoxicity and local tissue necrosis, while 3FTxs often induce rapid paralysis by blocking nicotinic acetylcholine receptors (StatPearls, 2023). The primary therapeutic approach is the administration of antivenom, which consists of purified antibodies or antibody fragments that neutralize the toxins through direct binding (NIH, 2022). Additionally, small-molecule inhibitors like varespladib (targeting PLA2) and marimastat (targeting SVMPs) are being investigated as adjunct or field-stable treatments to mitigate the effects of these toxins before hospital-based antivenom can be administered (Journal of Medicinal Chemistry, 2021).

Other names

Snake venom proteinsOphidian toxinsSnake venom componentsSnake venom cocktailVenom-derived bioactive peptides

Antivenoms provide passive immunity by utilizing purified antibodies or antibody fragments (IgG, F(ab')2, or Fab) that bind to the antigenic sites of toxins, neutralizing their biological activity and facilitating clearance (StatPearls, 2023). Small-molecule inhibitors like varespladib act as competitive inhibitors that bind to the active sites of specific venom enzymes, such as phospholipase A2, preventing substrate interaction (PubMed, 2020).