Different rhinovirus serotypes neutralized by antipeptide antibodies

Nature. 1987 Oct;329(6141):736-8. doi: 10.1038/329736a0.

Abstract

Recently, Rossman et al. have described the three-dimensional structure of a human rhinovirus. A possible host cell surface receptor binding site was identified with a cleft on each icosahedral face. Two highly conserved amino-acid sequences found in rhino-, polio-, and foot-and-mouth disease (FMD) viruses are located near the base of this site and could be important in maintaining its topology. We have prepared site-specific antibodies to two synthetic peptides which include these sequences. The antibodies bind to the predicted capsid proteins of rhinovirus and neutralize approximately 60% of 48 rhinovirus serotypes tested. These results could provide a route to a rhinovirus vaccine effective against most of the numerous serotypes of this virus.

MeSH terms

  • Antibodies, Viral / immunology*
  • Capsid / immunology
  • Epitopes
  • Immunosorbent Techniques
  • Molecular Weight
  • Neutralization Tests
  • Oligopeptides / immunology
  • Receptors, Virus / immunology
  • Rhinovirus / classification
  • Rhinovirus / immunology*
  • Species Specificity

Substances

  • Antibodies, Viral
  • Epitopes
  • Oligopeptides
  • Receptors, Virus