Snake venom toxins from Indian species (SVTs)

Snake venom toxins from Indian species represent a complex and heterogeneous mixture of bioactive proteins and peptides primarily derived from the Big Four venomous snakes: the Spectacled Cobra (Naja naja), Common Krait (Bungarus caeruleus), Russell's Viper (Daboia russelii), and Saw-scaled Viper (Echis carinatus) (WHO, 2021). These venoms contain diverse toxin families, including phospholipase A2 (PLA2), three-finger toxins (3FTx), snake venom metalloproteinases (SVMP), and snake venom serine proteases (SVSP), which act synergistically to induce life-threatening neurotoxicity, systemic hemorrhage, and local tissue destruction (Casewell et al., 2020). Clinically, these toxins are the primary targets for polyvalent antivenom, the standard treatment in India, which utilizes antibodies to neutralize venom components (National Health Portal India, 2016). Emerging pharmacological research is exploring the use of small molecule inhibitors, such as varespladib for PLA2 and marimastat for SVMPs, as potential adjuncts to traditional antivenom therapy to improve efficacy and reduce adverse reactions associated with animal-derived products (Lewin et al., 2016; Albulescu et al., 2020). Understanding the specific venomics of these species is critical for developing more targeted and effective treatments for snakebite envenomation, which remains a major public health challenge in the Indian subcontinent (Senji Laxme et al., 2019).

Other names

Indian snake venomBig Four venom toxinsOphitoxinsSnake venom proteinsIndian cobra and viper toxins

The primary therapeutic mechanism involves the administration of polyvalent antivenom, which contains equine-derived antibodies that bind to and neutralize the various toxic components of the venom through steric hindrance and immune clearance (Warrell, 2010). Small molecule inhibitors like varespladib act by competitively inhibiting the active site of phospholipase A2 (PLA2) enzymes, while metalloproteinase inhibitors like marimastat chelate the zinc ion required for the catalytic activity of snake venom metalloproteinases (SVMPs), thereby preventing basement membrane degradation and hemorrhage (Lewin et al., 2016; Albulescu et al., 2020).