Daboia russelii siamensis venom protein

Daboia russelii siamensis venom proteins comprise a complex mixture of enzymatic and non-enzymatic proteins produced in the venom glands of the eastern Russell’s viper. Major protein families include serine proteinases (such as factor X activator, RVV-X), phospholipase A2, Kunitz-type protease inhibitors, C-type lectin-like proteins, L-amino acid oxidase, snake venom vascular endothelial growth factor, nerve growth factor, and others[1][2][3][5]. These proteins collectively act to immobilize and pre-digest prey through drastic disruption of coagulation, induction of hypotension, tissue damage, and paralysis. Individual proteins can have specific molecular targets, such as RVV-X activating human coagulation factor X, or phospholipase A2 catalyzing phospholipid hydrolysis and promoting inflammation and cell lysis. The composition and abundance of these protein families vary according to geographic population, age, and other factors[1][2][5]. The venom’s biological effects in humans include profound coagulopathy, bleeding, nephrotoxicity, and shock, and its components are targets for antivenom development and biomedical research.

Other names

Eastern Russell’s viper venom proteinsDaboia siamensis venom proteinsRussell’s viper siamensis toxinsD. russelii siamensis venom components

For antivenoms: antibody neutralization via binding to epitopes on venom proteins For direct inhibitors (e.g., metalloproteinase inhibitors): block enzymatic active site or critical cofactors required for catalytic activity