Promiscuous T-cell recognition of a rubella capsid protein epitope restricted by DRB1*0403 and DRB1*0901 molecules sharing an HLA DR supertype

Hum Immunol. 1998 Mar;59(3):149-57. doi: 10.1016/s0198-8859(98)00006-8.

Abstract

Two T cell clones derived from different donors with HLA-DRB1*0403 or DRB1*0901 phenotype recognize a rubella capsid peptide, C(265-273) in the context of several different HLA-DR molecules in addition to DRB1*0403 and DRB1*0901. All DR molecules restricting the T-cell clones have in common residues, R or Q at position beta 70, R at position beta 71, and E at position beta 74 in pocket '4' of the DR peptide binding groove, suggesting that a DR subregion structure or supertype, "Q/RRE" underlies the promiscuous T-cell recognition of this peptide. Single amino acid substituted analogs of peptide C(263-275) at anchor position 4 for natural residue R were tested for their ability to induce clonal T-cell cytotoxic responses. The results indicated that a positively charged residue, R or K, was required for T-cell recognition, suggesting a possible mechanism of electrostatic interactions between the negatively charged residue E at position beta 74 of these DR molecules and the positively charged residue at anchor position 4 of the peptide in T-cell recognition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids
  • Capsid / chemical synthesis
  • Capsid / genetics
  • Capsid / immunology*
  • Cell Line, Transformed
  • Epitopes, T-Lymphocyte / genetics
  • Epitopes, T-Lymphocyte / immunology*
  • HLA-DR Antigens / immunology*
  • HLA-DRB1 Chains
  • Humans
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptides / chemical synthesis
  • Peptides / immunology*
  • Rubella virus / immunology*
  • T-Lymphocytes, Cytotoxic / immunology*

Substances

  • Amino Acids
  • Epitopes, T-Lymphocyte
  • HLA-DR Antigens
  • HLA-DRB1 Chains
  • Peptides