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A monoclonal antibody to a synthetic fragment of rabies virus glycoprotein binds ligands of the nicotinic cholinergic receptor
Author(s) -
Rustici Mauro,
Santucci Annalisa,
Lozzi Luisa,
Petreni Simonetta,
Spreafico Adriano,
Neri Paolo,
Bracci Luisa,
Soldani Patrizia
Publication year - 1989
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300020202
Subject(s) - affinity chromatography , acetylcholine receptor , monoclonal antibody , nicotinic acetylcholine receptor , rabies virus , glycoprotein , chemistry , biochemistry , cholinergic , nicotinic agonist , microbiology and biotechnology , receptor , antibody , rabies , biology , virology , immunology , neuroscience , enzyme
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.