Different rhinovirus serotypes neutralized by antipeptide antibodies.
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.
D000914:Antibodies, Viral / Q000276:immunology*; D002213:Capsid / Q000276:immunology; D000939:Epitopes; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D009500:Neutralization Tests; D009842:Oligopeptides / Q000276:immunology; D011991:Receptors, Virus / Q000276:immunology; D012229:Rhinovirus / Q000145:classification / Q000276:immunology*; D013045:Species Specificity
D000914:Antibodies, Viral; D000939:Epitopes; D009842:Oligopeptides; D011991:Receptors, Virus