Snake venomics of Bothriechis nigroviridis reveals extreme variability among palm pitviper venoms: different evolutionary solutions for the same trophic purpose

J Proteome Res. 2010 Aug 6;9(8):4234-41. doi: 10.1021/pr100545d.

Abstract

We report the proteomic characterization and biological activities of the venom of the black-speckled palm pitviper, Bothriechis nigroviridis, a neotropical arboreal pitviper from Costa Rica. In marked contrast to other Bothriechis species investigated, the venom of B. nigroviridis does not possess detectable Zn(2+)-dependent metalloproteinases, and is uniquely characterized by a high content of crotoxin-like PLA(2) and vasoactive peptides. These data suggest that different evolutionary solutions have evolved within the arboreal genus Bothriechis for the same trophic purpose. The venom from B. nigroviridis is devoid of hemorrhagic activity, has low edematogenic and coagulant effects, presents modest myotoxic and phospholipase A(2) activities, but has higher lethality than the venoms of other Bothriechis species. Neutralization of its lethal activity by an anti-Crotalus durissus terrificus antivenom confirmed the major role of crotoxin-like PLA(2) in B. nigroviridis venom-induced lethality.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Evolution*
  • Costa Rica
  • Creatine Kinase / blood
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / toxicity
  • Hemorrhage / chemically induced
  • Lethal Dose 50
  • Mass Spectrometry
  • Metalloproteases / metabolism
  • Mice
  • Neutralization Tests
  • Phospholipases A2 / metabolism
  • Phylogeny
  • Proteomics / methods*
  • Species Specificity
  • Viperidae / genetics
  • Viperidae / metabolism*

Substances

  • Crotalid Venoms
  • Creatine Kinase
  • Phospholipases A2
  • Metalloproteases