HLA-B27: a registry of constitutive peptide ligands

Tissue Antigens. 2004 May;63(5):424-45. doi: 10.1111/j.0001-2815.2004.00220.x.


The very strong association of human leukocyte antigen (HLA)-B27 with spondyloarthritis might be related to its peptide-presenting properties. The natural polymorphism of this molecule influences both peptide specificity and disease susceptibility. In this study, we present a comprehensive compilation of known natural ligands of HLA-B27 arising from endogenous proteins of human cells, together with a statistical assessment of residue usage among constitutive peptide repertoires of multiple HLA-B27 subtypes. This analysis provides evidence that every peptide position, including "non-anchor" ones, may be subjected to selection on the basis of its contribution to HLA-B27 binding and also allows a quantization of residue preferences at known anchor positions. The present registry is intended as a basis on which to build up reliable criteria to assess the effect of HLA-B27 polymorphism on peptide presentation, for T-cell epitope predictions, and for molecular mimicry studies.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Antigen Presentation
  • Cell Line
  • Cell Transformation, Viral
  • Data Interpretation, Statistical
  • Databases, Factual
  • HLA-B27 Antigen / genetics*
  • HLA-B27 Antigen / immunology
  • Herpesvirus 4, Human
  • Humans
  • Ligands
  • Molecular Sequence Data
  • Peptides / genetics*
  • Peptides / immunology
  • Polymorphism, Genetic
  • Protein Binding
  • Spondylarthritis / immunology


  • HLA-B27 Antigen
  • Ligands
  • Peptides