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Crotalus durissus venom toxins comprise a complex array of proteins and peptides secreted by the South American rattlesnake, primarily responsible for severe systemic envenomation. The most significant component is crotoxin, a potent neurotoxic complex consisting of a basic phospholipase A2 (CB) and an acidic non-enzymatic subunit (crotapotin or CA) that acts by blocking acetylcholine release at the presynaptic neuromuscular junction (PMID: 17174462). Other critical toxins include crotamine, a small basic polypeptide that targets voltage-gated sodium channels to induce muscle contraction, and convulxin, a C-type lectin-like protein that potently activates platelets via the glycoprotein VI receptor (PMID: 11368296). Clinically, these toxins lead to a syndrome characterized by progressive muscular paralysis, systemic rhabdomyolysis, and coagulopathy, which can result in fatal respiratory failure or acute renal injury (PMID: 15182911). Therapeutic management relies on the administration of polyvalent or monovalent antivenoms, which contain purified antibodies that bind and neutralize these toxins in the circulation (PMID: 25443539). Additionally, novel small-molecule inhibitors like varespladib are being investigated for their ability to specifically inhibit the phospholipase A2 activity inherent in these venom complexes (PMID: 27383169).
Antibody-mediated neutralization of venom proteins to prevent binding to physiological targets and competitive inhibition of enzymatic subunits such as phospholipase A2 (PMID: 25443539, PMID: 27383169).
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