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Daboia siamensis venom Kunitz-type protease inhibitor toxins are a group of small, disulfide-rich proteins found in the venom of the Eastern Russell's viper (UniProt Consortium, 2024). These toxins belong to the Kunitz/Bovine pancreatic trypsin inhibitor (BPTI) family and typically function as potent inhibitors of serine proteases such as trypsin, plasmin, and kallikrein (Tan et al., 2015). By interfering with these enzymes, they play a significant role in the complex coagulopathy and hemorrhagic symptoms observed during envenomation. While some Kunitz-type toxins in other snake species act as neurotoxins by blocking potassium channels, the variants in Daboia siamensis are primarily recognized for their protease-inhibiting activity (WHO, 2016). In clinical practice, these toxins are the primary targets for neutralization by specific monovalent or polyvalent antivenoms. Understanding their structure and function is crucial for improving antivenom efficacy and for the potential development of therapeutic agents targeting fibrinolysis or inflammation. Their presence in the venom contributes to the overall lethality and systemic complications associated with Russell's viper bites.
Neutralization of toxin activity via antibody-mediated binding, preventing the toxin from inhibiting endogenous serine proteases.
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