INTERACTIONS OF THE HUMAN CLASS-II MAJOR HISTOCOMPATIBILITY COMPLEX PROTEIN HLA-DR4 WITH A PEPTIDE LIGAND DEMONSTRATED BY AFFINITY CAPILLARY ELECTROPHORESIS

The interactions of empty recombinant major histocompatibility complex (MHC) class II molecules (DRA10101/DRB1*0401) with a known peptide l igand [the HA(307-319) fragment of influenza virus hemagglutinin] were studied by capillary electrophoresis. Using an alkaline buffer system with the addition of non-ionic or zwitterionic detergent and high sen sitivity laser-induced fluorescence detection, both slowly and rapidly equilibrating binding could be demonstrated. This was accomplished us ing a pre-equilibration approach as well as migration shift experiment s where receptor molecules were added to the electrophoresis buffer. T his system may be useful for the study of both peptide binding to MHC molecules and screening for inhibition or amplification of binding by other ligands as well as for the study of the interactions of T-cell r eceptors with MHC-peptide complexes. (C) 1997 Elsevier Science B.V.