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Russell's Viper venom toxins are a complex mixture of bioactive proteins and enzymes produced by snakes of the Daboia genus, which are responsible for a significant portion of snakebite morbidity and mortality in South and Southeast Asia (StatPearls, 2024). The venom's primary pathophysiology involves severe coagulopathy, driven by specific activators of Factor X (RVV-X) and Factor V (RVV-V) that induce a prothrombotic state followed by consumption of clotting factors (UniProt, 2023). Additionally, the venom contains high levels of Phospholipase A2 (PLA2) and metalloproteinases that cause systemic hemorrhage, acute kidney injury, and local tissue destruction (PubMed, 2022). Therapeutic intervention primarily relies on the administration of polyvalent or monovalent antivenoms, which contain antibodies that neutralize these toxic components. Recent pharmacological research has also explored the use of small-molecule inhibitors, such as Varespladib for PLA2 and Marimastat for metalloproteinases, as adjunct or field-stable treatments (Nature Communications, 2020). Beyond its role in envenomation, the venom is a critical component of the dilute Russell's Viper venom time (dRVVT) test, a standard diagnostic tool for detecting lupus anticoagulants in clinical hematology (Journal of Thrombosis and Haemostasis, 2021).
Antibody-mediated neutralization of venom components; competitive inhibition of Phospholipase A2; chelation of zinc ions in metalloproteinases.
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