HLA-B*3501-peptide interactions: role of anchor residues of peptides in their binding to HLA-B*3501 molecules.
Two HLA-B*3501 binding self-peptides, LPFDFTPGY (37F) and LPGPKFLQY (28H), were isolated from HLA-B*3501 molecules expressed by cultured human B lymphoid cells. Both sequences were consistent with previously reported motifs of HLA-B*3501 binding peptides which carry proline at position 2 and tyrosine at position 9 as anchor residues. Direct binding of these peptides to HLA-B*3501 molecules was quantitated by flow cytometry analysis of RMA-S cells. transfected with the HLA-B*3501 gene (RMA-S-B*3501). Both 37F and 28H peptides bound effectively to HLA-B*3501 molecules. Substitution of amino acids at position 2 and/or 9 of HLA-B*3501 binding peptides markedly reduced their binding to HLA-B*3501 molecules. These results indicate that two anchor residues, proline at position 2 and tyrosine at position 9 are critical in binding of peptides to HLA-B*3501 molecules. Insertion of up to four glycine residues at position 8 of the peptide 37F did not affect its binding affinity to HLA*3501 molecules. These results indicate that long peptides can effectively bind to HLA class I molecules provided that anchor residues are conserved.
Takamiya
Y
Y
Department of Tumor Biology, University of Tokyo, Japan.
Schönbach
C
C
Nokihara
K
K
Yamaguchi
M
M
Ferrone
S
S
Kano
K
K
Egawa
K
K
Takiguchi
M
M
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D005434:Flow Cytometry; D015797:HLA-B35 Antigen / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000276:immunology*; D011485:Protein Binding / Q000276:immunology; D011994:Recombinant Proteins / Q000276:immunology; D013329:Structure-Activity Relationship; D001613:beta 2-Microglobulin / Q000276:immunology
D015797:HLA-B35 Antigen; D010455:Peptides; D011994:Recombinant Proteins; D001613:beta 2-Microglobulin