Snake venom toxins (Viperidae and Elapidae) (SVT)

Snake venom toxins from the Viperidae and Elapidae families are a heterogeneous group of proteins and peptides that cause the clinical manifestations of snakebite envenomation. Viperid venoms typically contain high levels of snake venom metalloproteinases (SVMPs), serine proteases (SVSPs), and phospholipase A2 (PLA2) enzymes, which lead to local tissue destruction, systemic hemorrhage, and consumptive coagulopathy (WHO, 2021; Casewell et al., 2020). Elapid venoms are characterized by potent neurotoxins, such as three-finger toxins (3FTx), which block nicotinic acetylcholine receptors at the neuromuscular junction, resulting in descending paralysis and potential respiratory failure (Tasoulis & Isbister, 2017). These toxins function by enzymatically degrading extracellular matrix components, interfering with the coagulation cascade, or disrupting ion channel and receptor signaling. The primary therapeutic approach is the administration of antivenom, which uses purified antibodies to neutralize venom components in the circulation (Casewell et al., 2020). Recent drug development efforts have focused on small molecule inhibitors like Varespladib (a PLA2 inhibitor) and Marimastat (an SVMP inhibitor) to provide rapid, field-deployable treatments that can bridge the gap to hospital-based antivenom therapy (Lewin et al., 2016; Albulescu et al., 2020).

Other names

Snake venom proteinsOphidian toxinsViperid toxinsElapid toxinsSnake venom enzymesSnake venom metalloproteinases (SVMP)Snake venom serine proteases (SVSP)Three-finger toxins (3FTx)Phospholipase A2 toxins (PLA2)

Neutralization of toxic activity through antibody-mediated sequestration (antivenoms) or direct enzymatic inhibition of specific toxin families, such as phospholipase A2 (by Varespladib) or metalloproteinases (by Marimastat).