The 208–222 Region of the Peplomer Glycoprotein as a Putative Binding Site of Rabies Virus with the Nicotinic Acetylcholine Receptor
There is increasing evidence that viruses utilize recep tors for physiological ligands in order to infect their host cells. For instance, it has been shown that vaccinia virus binds to the receptors of epidermal growth factor (1), Eppstein-Barr virus to the receptor for the complement on B-lymphocytes (2), and those of HTLV-III and rabies to the T4 antigen of T lymphocytes (3) and acetylcholine receptor (4), respectively. Since the acetyl choline receptor is the target organ of many other non-physiological ligands as, for instance, the neurotoxins of snake venoms, the structure of which is well-known, we decided to compare the amino acid sequence of the glycoprotein peplomers of rabies virus (RGV) with that of snake neurotoxins (NTX) in order to detect homologies, which in turn can lead to the identification of the binding site of the viral protein with the receptor.
KeywordsCircular Dichro Spectrum Nicotinic Acetylcholine Receptor Rabies Virus Peptide Binding Site Cationic Moiety
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