Peptide binding to empty HLA-B27 molecules of viable human cells

Nature. 1991 May 2;351(6321):74-7. doi: 10.1038/351074a0.


Intracellular binding of antigenic peptides by polymorphic class I major histocompatibility complex molecules creates the ligands recognized by receptors of CD8+ T cells. Previously described in vitro assays of peptide binding to class I molecules have been limited by either the low proportion of accessible binding sites or the lack of allelic specificity. Here we describe a system in which the human class I molecule HLA-B27 binds considerable amounts of an influenza peptide with precise allelic discrimination. Binding requires viable cells, is stimulated by gamma-interferon and is inhibited by brefeldin A. Our results are consistent with the presence of fairly stable 'empty' HLA-B27 molecules at the cell surface. By contrast, analysis of the binding of a second influenza peptide indicates that empty HLA-Aw68 molecules are relatively short-lived. We speculate that HLA-B27 might bind extracellular peptides in vivo and that this property could underlie its association with autoimmune disease.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alleles
  • Amino Acid Sequence
  • Antibodies, Monoclonal
  • B-Lymphocytes
  • Binding, Competitive
  • Cell Line
  • HLA-B27 Antigen / genetics
  • HLA-B27 Antigen / immunology*
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Peptides / chemical synthesis
  • Protein Binding
  • T-Lymphocytes / immunology*
  • Transfection


  • Antibodies, Monoclonal
  • HLA-B27 Antigen
  • Peptides