title: Phospholipases A2: unveiling the secrets of a functionally versatile group of snake venom toxins.
abstract: Phospholipases A(2) (PLA(2)s) are abundant components of snake venoms, where they play toxic and digestive roles. Despite having a similar three-dimensional structure, venom PLA(2)s exert an amazing variety of toxic and pharmacological effects, which include neurotoxic, myotoxic, hemolytic, edematogenic, hyperalgesic, pro-inflammatory, hypotensive, platelet-aggregation inhibitory, anticoagulant, cytotoxic, and bactericidal activities. Toxinologists have made significant contributions to deciphering the structure, molecular evolution, mechanisms of action, receptors, role of enzymatic activity for toxicity, structural determinants of toxicity and selectivity, and the impact of these enzymes in the overall pathophysiology of snakebite envenoming. The present work highlights some of the most relevant contributions in the study of venom PLA(2)s, including the personal accounts of the authors of these studies.
authors.affiliation: Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica. jose.gutierrez@ucr.ac.cr
authors.forename: José María
authors.initials: JM
authors.lastname: Gutiérrez
authors.forename: Bruno
authors.initials: B
authors.lastname: Lomonte
mesh_terms: D019143:Evolution, Molecular; D008958:Models, Molecular; D009498:Neurotoxins / Q000737:chemistry / Q000494:pharmacology / Q000633:toxicity; D054467:Phospholipases A2 / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology / Q000633:toxicity; D017434:Protein Structure, Tertiary; D030162:Reptilian Proteins / Q000737:chemistry* / Q000494:pharmacology / Q000633:toxicity; D020539:Sequence Analysis, Protein; D012910:Snake Venoms / Q000737:chemistry / Q000201:enzymology*; D013329:Structure-Activity Relationship
chemical_list: D009498:Neurotoxins; D030162:Reptilian Proteins; D012910:Snake Venoms; D054467:Phospholipases A2