Monoclonal antibody neutralization escape mutants of respiratory syncytial virus with unique alterations in the attachment (G) protein

J Gen Virol. 1998 Mar;79 ( Pt 3):479-87. doi: 10.1099/0022-1317-79-3-479.


Five monoclonal antibody (MAb) neutralization escape mutants of respiratory syncytial virus (RSV) were produced by growing the Long strain RSV (group A virus) in the presence of a neutralizing, group cross-reactive MAb specific for the attachment protein (G). Four viruses (RSV-2, -6, -14 and -15) had amino acid replacements clustered within a highly conserved centrally located 13 amino acid region (position 164-176). Reactivity with group A-specific MAbs and with polyclonal anti-G serum was maintained and growth kinetics were unaffected. An additional virus (RSV-3) had four amino acid substitutions in the cytoplasmic tail and transmembrane region of G, and had restricted growth and formed small syncytia. Immunofluorescent and Western blot analysis indicated that G protein was not membrane associated and had reduced incorporation into the virion, thereby escaping neutralization by L9 and polyclonal anti-G serum. The predominant form of G produced by RSV-3 was found in infected cell supernatants, consistent with the size of secreted G.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal / metabolism
  • Attachment Sites, Microbiological
  • Base Sequence
  • Blotting, Western
  • Fluorescent Antibody Technique, Indirect
  • HN Protein*
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Respiratory Syncytial Viruses / genetics*
  • Respiratory Syncytial Viruses / growth & development
  • Respiratory Syncytial Viruses / immunology
  • Tumor Cells, Cultured
  • Viral Envelope Proteins
  • Viral Proteins / genetics*
  • Viral Proteins / immunology


  • Antibodies, Monoclonal
  • HN Protein
  • Viral Envelope Proteins
  • Viral Proteins
  • attachment protein G