Snake venom phospholipase A2 (svPLA2) (svPLA2)

Snake venom phospholipase A2 (svPLA2) enzymes are a major family of toxic proteins found in the venoms of vipers, cobras, and other venomous snakes. These enzymes catalyze the hydrolysis of the sn-2 ester bond in phospholipids, releasing arachidonic acid and lysophospholipids, which leads to membrane damage and inflammatory signaling [1]. The toxic effects of svPLA2s are diverse, encompassing systemic myotoxicity, presynaptic neurotoxicity, and interference with blood coagulation [2]. While traditional treatment relies on animal-derived antivenoms, svPLA2s have become a primary target for small-molecule inhibitors like varespladib, which aim to provide broad-spectrum neutralization [3]. These inhibitors work by binding to the enzyme's active site, thereby preventing the catalytic activity that drives much of the venom's pathology [4]. Understanding the structure and function of svPLA2 is essential for developing more effective, shelf-stable treatments for snakebite envenomation globally [5].

Other names

Phosphatidylcholine 2-acylhydrolaseSecretory phospholipase A2 (Group I and II)svPLA2Snake venom PLA2Snake venom phospholipase A2 toxins

Competitive inhibition of the enzyme's catalytic active site (specifically residues His48 and Asp49), preventing the hydrolysis of the sn-2 ester bond of glycerophospholipids and the subsequent release of pro-inflammatory and toxic mediators [3, 4].