Neutralizing antibodies to human rhinovirus produced in laboratory animals and humans that recognize a linear sequence from VP2.

Synthetic peptides representing amino acids 156 to 170 of virus capsid protein VP2 from human rhinovirus (HRV) type 2 have previously been used to elicit a neutralizing antibody response; polyclonal antisera against this peptide have been compared with a virus-neutralizing monoclonal antibody (8F5) which recognizes the same linear sequence. The neutralizing activity of both antibodies against virus is abolished by an amino acid substitution in VP2 at position 163 but only the peptide antiserum neutralizing activity is affected by a change in VP2 at position 158. The minimal binding site of 8F5 has been mapped, using overlapping peptides, to a sequence TRLNPD covering VP2 residues 160 to 165. Using affinity purification it has been shown that 8 to 10% of total neutralizing activity of polyclonal rabbit or guinea-pig antivirus antiserum is due to recognition of this linear VP2 156 to 170 determinant. Furthermore, a similar population of neutralizing antibodies appears to be associated with an immune response to recent HRV infection in humans. These results confirm the existence of linear determinants on the surface of HRV which may be mimicked by suitable synthetic peptides.