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Crotalinae venom toxins represent a diverse array of bioactive proteins and peptides secreted by pit vipers, such as rattlesnakes, copperheads, and cottonmouths [1]. The primary toxic constituents include snake venom metalloproteinases (SVMPs), which degrade extracellular matrix components leading to hemorrhage; phospholipases A2 (PLA2s), which cause cell membrane damage and inflammation; and serine proteases that interfere with the coagulation cascade [1][4]. Envenomation by these species typically results in local tissue damage, systemic coagulopathy, and occasionally neurotoxicity or myotoxicity [4][5]. Therapeutic management relies on antivenoms, which are composed of purified antibodies or antibody fragments (Fab or F(ab')2) derived from immunized animals [2][3]. These antivenoms function by binding to and neutralizing the circulating toxins, thereby halting the progression of systemic and local symptoms [2][3].
The mechanism of action involves passive immunization where the antivenom's Fab or F(ab')2 fragments bind to the venom's antigenic sites, neutralizing the toxins' enzymatic and toxicological activities and facilitating their redistribution and elimination from the body [2][3][5].
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