Effect of polymorphism of the HLA-DPA1 chain on presentation of antigenic peptides

J S Gaston, J C Goodall, J L Young, S P Young

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Human T-cell clones that recognize a peptide from mycobacterial heat shock protein 60 in the context of HLA-DP were found to be sensitive to changes in the DPA1 chain of the restricting element, optimal responses being seen with the combination HLA-DPA1*0201 and HLA-DPB*0301. HLA-DP dimers containing HLA-DPA1*01 were only able to present antigenic peptides to T-cell clones when peptides were present throughout the period of coculture of T cells with antigen presenting cells. In contrast the optimal HLA-DP dimer could also stimulate T-cell clones maximally when incubated with peptides for 1 h and then thoroughly washed. This suggests that the DPA1 polymorphism influenced the strength of binding of antigenic peptides to the HLA-DP dimer. Modeling studies identified amino acid 31 of DPA1 as the polymorphic residue most likely to account for this effect. This is the first demonstration that the relatively limited polymorphism displayed by DPA1 has functional consequences.
Original languageEnglish
Pages (from-to)40-7
Number of pages8
JournalHuman Immunology
Issue number1
Publication statusPublished - 15 Apr 1997


  • Clone Cells
  • Antigen Presentation
  • Models, Molecular
  • Polymorphism, Genetic
  • Humans
  • Amino Acid Sequence
  • Lymphocyte Activation
  • HLA-DP alpha-Chains
  • HLA-DP Antigens
  • Chaperonin 60
  • Molecular Sequence Data
  • Peptides
  • T-Lymphocytes


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