Phospholipases A2: unveiling the secrets of a functionally versatile group of snake venom toxins

Toxicon. 2013 Feb:62:27-39. doi: 10.1016/j.toxicon.2012.09.006. Epub 2012 Sep 28.

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.

Publication types

  • Review

MeSH terms

  • Evolution, Molecular
  • Models, Molecular
  • Neurotoxins / chemistry
  • Neurotoxins / pharmacology
  • Neurotoxins / toxicity
  • Phospholipases A2 / chemistry*
  • Phospholipases A2 / isolation & purification
  • Phospholipases A2 / pharmacology
  • Phospholipases A2 / toxicity
  • Protein Structure, Tertiary
  • Reptilian Proteins / chemistry*
  • Reptilian Proteins / pharmacology
  • Reptilian Proteins / toxicity
  • Sequence Analysis, Protein
  • Snake Venoms / chemistry
  • Snake Venoms / enzymology*
  • Structure-Activity Relationship

Substances

  • Neurotoxins
  • Reptilian Proteins
  • Snake Venoms
  • Phospholipases A2