Detection of amino acid motifs on the agretopes of antigens highly bound to MHC molecules

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After constitution of tri-molecular complexes among TCR, MHC molecules,and peptide fragments of antigens, T cells are activated. In this event, binding between antigen peptides and MHC molecules is critical for constitution of the tri-molecular complex. we have reported pigeon cytochrome c related peptides substituted at agretopes (sites bound to MHC molecules) bound to murine MHC class II molecules in an allele specific manner. In order to detect peptides bound to human class II molecules we tried to establish DR transgenic mice. Since we detected the injected DNAs in some mice by PCR technique, we are testing expression of the DR molecules in various tissues of the mice.In another work we found that pigeon cytochrome c related peptides bound to DQw6 molecules and activated T cells in the DQw6 transgenic mice kindly provided by Dr. Sasazuki. Peptides carrying arginine at position 46 and alanine at position 54 which had been determined as agretopes bound to DQw6 molecules (AEGRSYTVANKAKGIT). Further, we found a peptide consisted of influenza virus haemagglutinin 123-138 (EGFTWTGVTQNGGSNA) bound to DQw6 molecules.We have also reported that pigeon cytochrome c related peptides carrying the murine MHC binding motif with substituted epitopic residues (sites bound to TCR) to haemagglutinin of influenza virus can stimulate immune responses to influenza virus in mice (cassette theory). Since the motif bound to human MHC molecules has been appeared, peptide vaccines prepared by the cassette theory to influenza virus will be effective in human.