Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3776
Title: A monoclonal antibody to a synthetic fragment of rabies virus glycoprotein binds ligands of the nicotinic cholinergic receptor.
Authors: Rustici, M
Santucci, Annalisa 
Lozzi, Luisa
Petreni, S
Spreafico, Adriano
Neri, Paolo
Bracci, Luisa
Soldani, Patrizia 
Issue Date: 1989
Project: None 
Journal: JOURNAL OF MOLECULAR RECOGNITION
Abstract: 
Rabies virus glycoprotein and snake venom curaremimetic neurotoxins share a region of high homology (30–45 for neurotoxins and 190–203 for the glycoprotein) in the regions that are believed to be responsible for binding the nicotinic acetylcholine receptor. Monoclonal antibodies raised to the 190–203 synthetic fragment of rabies virus glycoprotein were immobilized on a high performance affinity chromatography column and were able to bind neurotoxins. Toxins were displaced from the affinity column by elution at acidic pH and by affinity competition with acetylcholine at neutral pH. Furthermore, the affinity column proved to be useful for the purification of cholinergic ligands. Overall, these results indicate that the paratope of our monoclonal antibodies could behave as an ‘internal image’ of the nicotinic cholinergic receptor acetylcholine binding site.
Description: 
37544
URI: http://hdl.handle.net/20.500.12779/3776
ISSN: 0952-3499
DOI: 10.1002/jmr.300020202
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