Hemotoxic snake venom toxin

Hemotoxic snake venom toxins are a heterogeneous group of proteins and peptides found in the venoms of many viperid, some elapid, and colubrid snakes[1][2][3]. The main families include snake venom metalloproteinases (SVMPs) and serine proteases (SVSPs), but also disintegrins, C-type lectin-like proteins, and others. These toxins act principally by disrupting hemostasis: they can break down blood vessel structural proteins, impair blood clotting (either causing excessive clotting followed by consumption of clotting factors, or direct bleeding and coagulopathy), promote tissue damage, inhibit platelet function, and cause vascular leakage, leading to hemorrhage, hypovolemia, organ infarction, and shock[1][3][2]. While some components are structurally and mechanistically related (such as SVMPs being part of a conserved metalloproteinase family), "hemotoxic snake venom toxins" is not a single molecular entity or even a single family, but rather a descriptive group for the pathophysiological effects they induce. These effects are the main cause of morbidity and mortality after bites by viperid snakes and some others. Medical interventions are based on polyclonal antivenoms, which neutralize the toxins by antibody binding, but specific molecular inhibitors are still mostly experimental[1][3].

Other names

HemotoxinHaemotoxinSnake venom hemotoxinHemorrhaginSnake venom metalloproteinases (SVMPs)Snake venom serine proteases (SVSPs)DisintegrinsC-type lectin-like proteins

Antivenoms bind and neutralize toxins, promoting clearance and preventing interaction with blood proteins, endothelium, or other molecular targets. Protease inhibitors inhibit SVMP or SVSP catalytic activity. Chelators bind essential zinc (SVMP) or calcium, blocking enzymatic function.