DEFINITION OF ESSENTIAL AMINO-ACID-RESIDUES IN THE RECOGNITION OF A PEPTIDE BY A MOUSE MONOCLONAL-ANTIBODY

A mouse monoclonal antibody reacting in ELISA with a synthetic peptide representing a linear amino acid stretch of the protein antigen was t ested on all overlapping 5-mer to 9-mer fragments of the peptide, as p repared by multi-pin synthesis. Analysis of the binding data suggests that several residues in the peptide might be relatively unrelevant fo r recognition, while few others seem to play a critical role as key re sidues. On the basis of such observations, we attempted to reconstruct an alternative essential epitope by introducing multiple amino acid s ubstitutions in the 9-mer peptide exhibiting the best binding activity , and then tested its ability to be recognized by the monoclonal antib ody.