Isolation and characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake)

Neuropharmacology. 2007 Mar;52(4):1065-70. doi: 10.1016/j.neuropharm.2006.11.002. Epub 2006 Dec 27.

Abstract

Colubrid snake venoms potentially represent a vast source of novel biological actives and structural motifs owing to their diverse phylogeny. The present study describes the identification of rufoxin, a neurotoxin from the venom of Rhamphiophis oxyrhynchus (Rufous beaked snake) which is a member of the African colubrid lineage, the psammophiines. Rufoxin (1 microM) displayed reversible post-synaptic neurotoxic activity as evidenced by significant inhibition of indirect twitches and responses to exogenous nicotinic agonists in the chick biventer cervicis nerve-muscle preparation. Rufoxin (0.1-1.0 microM) also caused a rightward parallel shift of cumulative concentration-response curves to carbachol (CCh; 0.6-80 microM) without a significant depression of the maximum response, suggestive of classical competitive antagonism at the skeletal muscle nicotinic receptor. Rufoxin lacks NH(2)-terminal sequence homology to previously identified snake venom toxins. This work indicates a wider distribution of neurotoxins across the advanced snake superfamily than previously described.

MeSH terms

  • Analysis of Variance
  • Animals
  • Chickens
  • Cholinesterase Inhibitors / pharmacology
  • Chromatography, High Pressure Liquid / methods
  • Colubridae
  • Dose-Response Relationship, Drug
  • In Vitro Techniques
  • Muscle Contraction / drug effects
  • Neostigmine / pharmacology
  • Neuromuscular Junction / drug effects*
  • Neurotoxins / isolation & purification*
  • Neurotoxins / pharmacology*
  • Snake Venoms / chemistry*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
  • Time Factors

Substances

  • Cholinesterase Inhibitors
  • Neurotoxins
  • Snake Venoms
  • Neostigmine