Purification and characterization of the respiratory syncytial virus fusion protein.
The fusion protein of respiratory syncytial virus was purified by affinity chromatography using a monoclonal antibody. Under various conditions the protein was recovered as a 145K dimer or a 70K monomer. The 70K monomer was composed of disulphide-linked fragments of 48K and 23K. Polyclonal rabbit serum produced to the dimerized fusion protein neutralized virus but did not inhibit fusion, while rabbit serum to the 2-mercaptoethanol-treated dimerized protein neutralized virus and inhibited fusion of infected cells. Only the latter serum strongly recognized the 23K fragment when studied by Western blot analysis.
D000596:Amino Acids / Q000032:analysis; D000914:Antibodies, Viral / Q000276:immunology; D002460:Cell Line; D006801:Humans; D008970:Molecular Weight; D012136:Respiratory Syncytial Viruses / Q000032:analysis*; D014759:Viral Envelope Proteins / Q000276:immunology / Q000302:isolation & purification*; D014760:Viral Fusion Proteins
D000596:Amino Acids; D000914:Antibodies, Viral; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins