Vipera berus venom proteins

Vipera berus venom proteins constitute a complex mixture of bioactive molecules, including phospholipase A2 (PLA2), snake venom metalloproteinases (SVMPs), and serine proteases, which facilitate prey immobilization and defense [1]. In humans, these proteins act as toxins that disrupt the coagulation cascade, damage vascular endothelium, and induce local tissue necrosis, leading to the clinical syndrome of snakebite envenomation [3, 4]. These proteins are the primary therapeutic targets for antivenoms like Viperatab, which utilize purified sheep Fab fragments to bind and neutralize the toxic components [2]. The mechanism of action involves the formation of antigen-antibody complexes that prevent the toxins from reaching their physiological targets and accelerate their elimination [2, 4]. While primarily studied for their toxicity, certain venom components are also investigated for potential therapeutic use in treating thrombosis and hypertension due to their potent effects on blood pressure and clotting [1]. Effective management of envenomation requires rapid administration of these antivenoms to prevent permanent tissue damage or systemic failure [2, 3]. Sources: [1] Latinovic, Z., et al. (2020). Venomics of Vipera berus berus. Toxins, 12(11), 674. [2] Electronic Medicines Compendium (EMC). Viperatab Summary of Product Characteristics. [3] World Health Organization (WHO). Guidelines for the Management of Snakebites. [4] Malina, T., et al. (2017). Clinical manifestations of Vipera berus bites. Journal of Clinical Toxicology.

Other names

Common European adder venomAdder venom proteinsVipera berus toxinsV. berus venom

Neutralization of venom toxins through the binding of specific polyclonal antibody fragments (Fab or F(ab')2), which prevents the toxins from interacting with their physiological targets and facilitates their clearance from the systemic circulation.