Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3736
Title: Antipeptide monoclonal antibodies inhibit the binding of rabiesvirus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor
Authors: Bracci, Luisa
Antoni, G.
Cusi, MARIA GRAZIA
Lozzi, Luisa
Niccolai, Neri 
Petreni, S.
Rustici, M.
Santucci, Annalisa 
Soldani, Patrizia 
Valensin, PIER EGISTO
Neri, Paolo
Issue Date: 1988
Project: None 
Journal: MOLECULAR IMMUNOLOGY
Abstract: 
It has been reported that binding to muscle nicotinic acetylcholine receptor at the post-synaptic membrane is an important event of the rabies virus neurotropism. The binding site can be located within the 190-203 region of the virus glycoprotein sharing a high degree of homology with the "toxic loop" of the curare-mimetic snake neurotoxins. We have synthesized a tetradecapeptide corresponding to this glycoprotein region and used it, following conjugation with an immunogenic carrier to raise MAbs. We found that some MAbs raised against the peptide were able to recognize both the virus glycoprotein and the snake neurotoxin alpha-bungarotoxin; moreover, they can inhibit the binding of rabies virus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor extracted from the electric organs of Torpedo marmorata. On the basis of this cross-reactivity, we suggest that rabies virus glycoprotein and curare-mimetic snake neurotoxins share three-dimensionally similar structures in order to bind to the nicotinic cholinergic receptor. The potential use of the immunogenic properties of the peptide for the rational design of a synthetic vaccine against rabies is proposed.
Description: 
36895
URI: http://hdl.handle.net/20.500.12779/3736
ISSN: 0161-5890
DOI: 10.1016/0161-5890(88)90125-3
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