Please use this identifier to cite or link to this item:
|Title:||Antipeptide monoclonal antibodies inhibit the binding of rabiesvirus glycoprotein and alpha-bungarotoxin to the nicotinic acetylcholine receptor||Authors:||Bracci, Luisa
Cusi, MARIA GRAZIA
Valensin, PIER EGISTO
|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.
|Appears in Collections:||Publications|
Show full item record
checked on May 5, 2021
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.