CHARACTERIZATION OF MONOCLONAL-ANTIBODIES RAISED AGAINST A SYNTHETIC PEPTIDE CAPABLE OF INDUCING A NEUTRALIZING RESPONSE TO HUMAN RHINOVIRUS TYPE-2

Synthetic peptides incorporating the derived amino acid sequence of VP 2 residues 156 to 170 of human rhinovirus type 2 (HRV2) have previousl y been shown to elicit antibodies that neutralize virus infectivity. T he proportion of virus-reactive antibodies present in polyclonal antis era to these peptides is, however, very low. Moreover, neutralization titrations of such antisera correlate poorly with other assays of eith er anti-virus or anti-peptide activity, suggesting the presence of ant ibodies with different specificities. To investigate these findings fu rther, we produced a panel of monoclonal antibodies (MAbs) to VP2 pept ides of residues 156 to 170 and characterized their reactions with a r ange of antigens in ELISA, precipitation and neutralization titrations . All the MAbs obtained recognized the homologous peptide, but could b e divided into four main reaction groups according to their specificit y for viral antigens. Antibodies in the first group recognized and neu tralized native virus, apparently by preventing attachment to cells. A second group of MAbs bound to intact particles with similar affinitie s to the first group. but failed to neutralize infectivity. Antibodies in the third group recognized virus only after capsid distortions inc urred by heating or by previous reaction with polyclonal antibodies. T he fourth group comprised MAbs that were mainly peptide-specific. Some possible applications of anti-peptide MAbs to improving the design of peptide immunogens are considered.