Location of a highly conserved neutralizing epitope in the F glycoprotein of human respiratory syncytial virus

J Virol. 1990 Feb;64(2):927-30. doi: 10.1128/JVI.64.2.927-930.1990.

Abstract

Trypsin digestion of the purified F protein from human respiratory syncytial virus (Long strain) generated a set of fragments in the amino-terminal third of the F1 subunit which contained the epitope 47F involved in neutralization. Sequencing of five escape mutant viruses selected with monoclonal antibody 47F allowed us to map precisely two amino acid residues (262 and 268) of the F1 subunit which are essential for the integrity of this important epitope. The results are discussed in terms of the mechanisms involved in virus neutralization and the design of potential synthetic vaccines.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / genetics*
  • Antigens, Viral / immunology
  • Base Sequence
  • Epitopes / genetics*
  • Genes, Viral
  • HN Protein*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Neutralization Tests
  • Peptide Fragments / isolation & purification
  • RNA, Messenger / genetics
  • Respiratory Syncytial Viruses / genetics*
  • Respiratory Syncytial Viruses / immunology
  • Trypsin
  • Viral Envelope Proteins
  • Viral Proteins*
  • Viral Structural Proteins / genetics

Substances

  • Antigens, Viral
  • Epitopes
  • HN Protein
  • Macromolecular Substances
  • Peptide Fragments
  • RNA, Messenger
  • Viral Envelope Proteins
  • Viral Proteins
  • Viral Structural Proteins
  • attachment protein G
  • Trypsin