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

Lumsden, Natalie G., Banerjee, Yajnavalka, Kini, R. Manjunatha, Kuruppu, Sanjaya and Hodgson, Wayne C. (2007) Isolation and characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake). Neuropharmacology, 52 4: 1065-1070. doi:10.1016/j.neuropharm.2006.11.002


Author Lumsden, Natalie G.
Banerjee, Yajnavalka
Kini, R. Manjunatha
Kuruppu, Sanjaya
Hodgson, Wayne C.
Title Isolation and characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake)
Formatted title
Isolation and characterization of rufoxin, a novel protein exhibiting neurotoxicity from venom of the psammophiine, Rhamphiophis oxyrhynchus (Rufous beaked snake)
Journal name Neuropharmacology   Check publisher's open access policy
ISSN 0028-3908
Publication date 2007-03
Sub-type Article (original research)
DOI 10.1016/j.neuropharm.2006.11.002
Volume 52
Issue 4
Start page 1065
End page 1070
Total pages 6
Place of publication Oxford
Publisher Pergamon-elsevier Science Ltd
Language eng
Subject 1115 Pharmacology and Pharmaceutical Sciences
1109 Neurosciences
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 mu M) 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 mu M) also caused a rightward parallel shift of cumulative concentration-response curves to carbachol (CCh; 0.6-80 mu M) without a significant depression of the maximum response, suggestive of classical competitive antagonism at the skeletal muscle nicotinic receptor. Rufoxin lacks NH2-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. (c) 2006 Elsevier Ltd. All rights reserved.
Keyword Neurosciences
Pharmacology & Pharmacy
colubrid venom
neurotoxin
skeletal muscle nicotinic receptor
Nicotinic Acetylcholine-receptors
Dendrophila Mangrove Catsnake
Vitro Neuromuscular Activity
Boiga-dendrophila
Naja-kaouthia
Antagonist
Muscle
Toxin
Components
Alpha-7
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Mon, 18 Feb 2008, 16:47:09 EST