Phospholipase A2 from coral snake venom (PLA2)

Phospholipase A2 from coral snake venom is a small, secretory enzyme belonging to the sPLA2 family, typically 13–15 kDa in mass, that hydrolyzes the sn-2 ester bond of phospholipids, resulting in membrane disruption and potent cytotoxicity[1][2][3]. These enzymes are endowed with unique pharmacological activities, including presynaptic neurotoxicity (blocking acetylcholine release), myotoxicity, and inflammation, and often act by targeting specific proteins or receptors in tissues via dedicated pharmacological sites distinct from their catalytic sites[1][6]. In coral snakes (genus Micrurus), PLA2 enzymes display substantial sequence diversity and contribute to the pathophysiology of envenomation, including muscle paralysis, necrosis, and systemic toxicities[3][4][6]. Their extreme toxicity makes them a chief target in the development of antivenoms, while their mechanism of membrane targeting and disruption is also being studied for the design of new therapeutics and molecular probes.

Other names

Coral snake phospholipase A2Snake venom PLA2Micrurus phospholipase A2Myotoxin

Enzymatic hydrolysis of membrane phospholipids (leads to lysis/disruption of cell membranes) Blockade of acetylcholine release at synapses (presynaptic neurotoxicity) Induction of oxidative stress (production of lysophospholipids and free fatty acids, ROS generation) Direct binding to target proteins/receptors (site-specific pharmacological effects, often independent of catalytic site)