Combined snake venomics and venom gland transcriptomic analysis of Bothropoides pauloensis

J Proteomics. 2012 May 17;75(9):2707-20. doi: 10.1016/j.jprot.2012.03.028. Epub 2012 Mar 27.

Abstract

Unraveling the repertoire of venom toxins of Bothropoides pauloensis was assessed by snake venomics and venom gland transcriptomic surveys. Both approaches yielded converging overall figures, pointing to metalloproteinases (~37%), PLA(2)s (26-32%), and vasoactive (bradykinin-potentiating) peptides (12-17%) as the major toxin classes. The high occurrence of SVMPs, PLA(2) molecules, vasoactive peptides, along with serine proteinases, explains the local and systemic effects observed in envenomations by B. pauloensis. Minor (<3%) C-type lectin, serine proteinase, L-amino acid oxidase, nerve growth factor, and CRISP molecules were also identified in the transcriptome and the proteome. Low abundance (0.3%) EST singletons coding for vascular endothelial growth factor (svVEGF), ohanin, hyaluronidase, and 5' nucleotidase were found only in the venom gland cDNA library. At the molecular level, the transcriptomic and proteomic datasets display low compositional concordance. In particular, although there is good agreement between transcriptome and proteome in the identity of BPPs, PLA(2) molecules and L-amino acid oxidase, both datasets strongly depart in their C-type lectin and SVMP complements. These data support the view that venom composition is influenced by transcriptional and translational mechanisms and emphasize the value of combining proteomic and transcriptomic approaches to acquire a more complete understanding of the toxinological profile and natural history of the snake venom.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / toxicity
  • Exocrine Glands / chemistry*
  • Expressed Sequence Tags
  • Gene Library
  • Humans
  • Metalloproteases / analysis
  • Metalloproteases / toxicity
  • Phospholipases A2 / analysis
  • Phospholipases A2 / toxicity
  • Proteome / analysis
  • Snake Bites / pathology
  • Snake Bites / physiopathology
  • Transcriptome
  • Viperidae

Substances

  • Crotalid Venoms
  • Proteome
  • Phospholipases A2
  • Metalloproteases