A FIV EPITOPE DEFINED BY A PHAGE PEPTIDE LIBRARY SCREENED WITH A MONOCLONAL ANTI-FIV ANTIBODY

Phage peptide libraries constitute powerful tools for the mapping of e pitopes recognized by monoclonal antibodies, We report here the charac terization of an antibody directed against a 20-residue peptide derive d from the surface glycoprotein of the feline immunodeficiency virus. The isolation of the WRPDF consensus sequence from a phage display lib rary defined the exact epitope recognized by the mAb. Compared with kn own immunogenic peptides of the FIV envelope, it corresponds to the mo st immunodominant peptide found in the whole molecule. Kinetic data de scribing the antibody-peptide interactions were obtained by surface pl asmon resonance. The antibody binds the peptide with a K-D in the nano molar range. (C) 1997 Published by Elsevier Science B.V.