Purification and characterization of the respiratory syncytial virus fusion protein

J Gen Virol. 1985 Mar;66 ( Pt 3):409-15. doi: 10.1099/0022-1317-66-3-409.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Antibodies, Viral / immunology
  • Cell Line
  • Humans
  • Molecular Weight
  • Respiratory Syncytial Viruses / analysis*
  • Viral Envelope Proteins / immunology
  • Viral Envelope Proteins / isolation & purification*
  • Viral Fusion Proteins

Substances

  • Amino Acids
  • Antibodies, Viral
  • Viral Envelope Proteins
  • Viral Fusion Proteins