title: Binding of cholesterol and inhibitory peptide derivatives with the fusogenic hydrophobic sequence of F-glycoprotein of HVJ (Sendai virus): possible implication in the fusion reaction.
abstract: Specificity of the binding of sterols and related compounds with purified F-protein (fusion protein) of the HVJ (Sendai virus) was studied by binding competition with [3H]cholesterol. Requirement for cholesterol or the A/B ring trans structure and nonrequirement for the 3-hydroxyl group were found in this binding. Binding of 125I-labeled Z-Phe-Tyr, an inhibitory peptide of viral membrane-cell membrane fusion, was studied by using purified proteins and virions. F-Protein and virions showed a specific binding with the peptide, whereas the result was negative with hemagglutinin and neuraminidase protein. Thermolysin-truncated F-protein (an F-protein derivative deprived of a 2.5-kDa fragment from the N-terminal of the F1 subunit and without fusogenic activity) exhibited a considerably diminished binding ability both to cholesterol and to inhibitory peptides. Therefore, the N-terminal hydrophobic sequence that was previously assigned as fusogenic seems to be the binding site of these molecules. In support of this, the binding of cholesterol with F-protein was inhibited by Z-Phe-Tyr and other fusion inhibitory peptides, whereas it was not affected with non-fusion-inhibitory Z-Gly-Phe. These results are discussed in relation to the notion that the binding of the N-terminal portion of the F1 subunit of F-protein with cholesterol in the target cell membranes facilitates the fusion reaction.
authors.affiliation: College of Medical Technology, Kyoto University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Asano
authors.forename: A
authors.initials: A
authors.lastname: Asano
mesh_terms: D000818:Animals; D002642:Chick Embryo; D002784:Cholesterol / Q000378:metabolism*; D007700:Kinetics; D010222:Parainfluenza Virus 1, Human / Q000378:metabolism*; D010447:Peptide Hydrolases; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D014760:Viral Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism*; D014771:Virion / Q000378:metabolism
chemical_list: D010455:Peptides; D014760:Viral Fusion Proteins; D002784:Cholesterol; D010447:Peptide Hydrolases