Manipulation of antipeptide immune response by varying the coupling of the peptide with the carrier protein

Antibodies were raised against synthetic peptides of two regions of the surface protein VP1 of foot-and-mouth disease virus. The peptides were conjugated with keyhole limpet hemocyanin via C- or N-terminal amino acid residues by use of different coupling agents. The fine specificity of the resulting antibodies was determined by PEPSCAN methods. In general, amino acid residues specific for antibody recognition tended to be located opposite to those used for coupling with the carrier protein. Depending on the method of conjugation, the orientation of the peptide at the carrier protein changes and directs the immune response. Thus, the method of conjugation can be used to manipulate the immune response and to improve the antiviral activity of antipeptide antibodies. The PEPSCAN method is an effective monitor in this process.