A MIMOTOPE FROM A SOLID-PHASE PEPTIDE LIBRARY INDUCES A MEASLES VIRUS-NEUTRALIZING AND PROTECTIVE ANTIBODY-RESPONSE

A solid-phase 8-mer random combinatorial peptide library was used to g enerate a panel of minotopes of an epitope recognized by a monoclonal antibody to the F protein of measles virus (MV). An inhibition immuno- assay was used to show that these peptides were bound by the monoclona l antibody with different affinities. BALB/c mice were coimmunized wit h the individual mimotopes and a T-helper epitope peptide (from MV fus ion protein), and the reactivity of the induced anti-mimotope antibodi es with the corresponding peptides and with MV was determined. The aff inities of the antibodies with the homologous peptides ranged from 8.9 X 10(5) to 4.4 X 10(7) liters/mol. However, only one of the anti-mimo tope antibodies cross-reacted with Rn in an enzyme-linked immunosorben t assay and inhibited MV plaque formation. Coimmunization of mice with this mimotope and the T-helper epitope peptide induced an antibody re sponse which conferred protection against fatal encephalitis induced f ollowing challenge with MV and with the structurally related canine di stemper virus. These results indicate that peptide libraries can be us ed to identify mimotopes of conformational epitopes and that appropria te immunization with these mimotopes can induce protective antibody re sponses.