Evidence for Snake Venom Plasticity in a Long-Term Study with Individual Captive Bothrops atrox

Toxins (Basel). 2019 May 24;11(5):294. doi: 10.3390/toxins11050294.

Abstract

Variability in snake venom composition has been frequently reported and correlated to the adaptability of snakes to environmental conditions. Previous studies report plasticity for the venom phenotype. However, these observations are not conclusive, as the results were based on pooled venoms, which present high individual variability. Here we tested the hypothesis of plasticity by influence of confinement and single diet type in the venom composition of 13 adult specimens of Bothrops atrox snakes, maintained under captivity for more than three years. Individual variability in venom composition was observed in samples extracted just after the capture of the snakes. However, composition was conserved in venoms periodically extracted from nine specimens, which presented low variability restricted to the less abundant components. In a second group, composed of four snakes, drastic changes were observed in the venom samples extracted at different periods, mostly related to snake venom metalloproteinases (SVMPs), the core function toxins of B. atrox venom, which occurred approximately between 400 and 500 days in captivity. These data show plasticity in the venom phenotype during the lifetime of adult snakes maintained under captive conditions. Causes or functional consequences involved in the phenotype modification require further investigations.

Keywords: enzyme toxins; metalloproteinases; venom variability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Variation, Individual
  • Bothrops*
  • Crotalid Venoms / analysis*
  • Crotalid Venoms / enzymology
  • Female
  • Metalloproteases / chemistry
  • Phenotype
  • Phospholipases A2 / chemistry
  • Reptilian Proteins / chemistry
  • Serine Proteases / chemistry

Substances

  • Crotalid Venoms
  • Reptilian Proteins
  • Phospholipases A2
  • Metalloproteases
  • Serine Proteases