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Rabies virus binding to an acetylcholine receptor α‐subunit peptide
Author(s) -
Lentz Thomas L.
Publication year - 1990
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.300030205
Subject(s) - acetylcholine receptor , nicotinic acetylcholine receptor , peptide , rabies virus , receptor , rhabdoviridae , protein subunit , biology , biochemistry , binding site , lyssavirus , virus , muscarinic acetylcholine receptor m5 , microbiology and biotechnology , chemistry , virology , muscarinic acetylcholine receptor m3 , gene
The binding of 125 I‐labeled rabies virus to a synthetic peptide comprising residues 173–204 of the α1‐subunit of the nicotinic acetylcholine receptor was investigated. Binding of rabies virus to the receptor peptide was dependent on pH, could be competed with by unlabeled homologous virus particles, and was saturable. Synthetic peptides of snake venom, curaremimetic neurotoxins and of the structurally similar segment of the rabies virus glycoprotein, were effective in competing with labeled virus binding to the receptor peptide at micromolar concentrations. Similarly, synthetic peptides of the binding domain on the acetylcholine receptor competed for binding. These findings suggest that both rabies virus and neurotoxins bind to residues 173–204 of the α1‐subunit of the acetylcholine receptor. Competition studies with shorter α‐subunit peptides within this region indicate that the highest affinity virus binding determinants are located within residues 179–192. A rat nerve α3‐subunit peptide, that does not bind α‐bungarotoxin, inhibited binding of virus to the α1 peptide, suggesting that rabies binds to neuronal nicotinic acetylcholine receptors. These studies indicate that synthetic peptides of the glycoprotein binding domain and of the receptor binding domain may represent useful antiviral agents by targeting the recognition event between the viral attachment protein and the host cell receptor, and inhibiting attachment of virus to the receptor.