HLA-B*3501-peptide interactions: Role of anchor residues of peptides in their binding to HLA-B* 3501 molecules

Christian Schönbach, Kiyoshi Noklhara, Mlnoru Yamaguch, Soldano Ferrone, Kyoichi Kano, Kohji Egawa, Masafumi Takiguchi

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Two HLA-B*3501 binding self-peptldes, LPFDFTPQY (37F) and LPGPKFLQY (28H), were Isolated from HLA-B*3501 molecules expressed by cultured human B lymphold cells. Both sequences were consistent with previously reported motifs of HLA-B*3501 binding peptides which carry prollne at position 2 and tyroslne 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 amlno 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, prollne at position 2 and tyroslne 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-B*3501 molecules. These results indicate that long peptides can effectively bind to HLA class I molecules provided that anchor residues are conserved.

Original languageEnglish
Pages (from-to)255-261
Number of pages7
JournalInternational Immunology
Volume6
Issue number2
DOIs
Publication statusPublished - Feb 1 1994
Externally publishedYes

Keywords

  • HLA-B35 molecules
  • Peptide motifs
  • Self-peptide

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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