Phage peptide libraries constitute powerful tools for the mapping of epitopes recognized by monoclonal antibodies. We report here the characterization of an antibody directed against a 20-residue peptide derived from the surface glycoprotein of the feline immunodeficiency virus. The isolation of the WRPDF consensus sequence from a phage display library defined the exact epitope recognized by the mAb. Compared with known immunogenic peptides of the FIV envelope, it corresponds to the most immunodominant peptide found in the whole molecule. Kinetic data describing the antibody-peptide interactions were obtained by surface plasmon resonance. The antibody binds the peptide with a KD in the nanomolar range.