AFFINITY CAPILLARY ELECTROPHORESIS INVESTIGATION OF AN EPITOPE ON HUMAN-IMMUNODEFICIENCY-VIRUS RECOGNIZED BY A MONOCLONAL-ANTIBODY

Affinity capillary electrophoresis (ACE) has been used to investigate the epitope on the human immunodeficiency virus (HIV) core protein p24 recognized by the monoclonal antibody (mAb) 13-102-100. The affinity of a series of peptides with N- and C-terminal truncations of the epit ope sequence determined by mass spectrometry was studied. The peak are a change assay was used for the study of the interactions of the mAb w ith those peptides, exhibiting tight binding to the mAb, and the migra tion time shift assay was used to probe the relative affinities of pep tides showing weak binding to the mAb. The experimental results show t hat the monoclonal antibody 13-102-100 recognizes the peptide VHPVHAGP IAP with highest affinity. Smaller peptides incorporating only part of the epitope, however, are recognized to some extent in the ACE experi ments.