Home

Isolation and characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake).
by Natalie G Lumsden, Yajnavalka Banerjee, R Manjunatha Kini, Sanjaya Kuruppu, Wayne C Hodgson
Neuropharmacology 52, 1065-1070 (2007).

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.

Source:
http://www.mendeley.com/research/isolation-characterization-rufoxin-novel-protein-exhibiting-neurotoxicity-venom-psammophiine-rhamphiophis-oxyrhynchus-rufous-beaked-snake/

 

 
Lumsden, N.G., Banerjee, Y., Kini, R.M., Kuruppu, S. & Hodgson, W.C. Isolation and characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake).