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Susceptibility to spondyloarthropathies is strongly associated with the MHC class I molecule HLA-B27, and is hypothesized to result from the presentation of arthritogenic peptides. Subtypes of B27 that differ structurally but are disease-associated ought to be capable of presenting such peptides, while nondisease-associated subtypes would not. We demonstrate that B*2703, the predominant West African B27 subtype that may not predispose to disease, is not recognized by most B*2705-alloreactive CTL, and does not efficiently present a known B*2705-restricted influenza A nucleoprotein (NP) peptide. We show inefficient presentation is due to a reduced binding affinity of B*2703 for the NP peptide. Furthermore, substituting Arg for the naturally occurring Ser at P1 of the NP peptide, restores high affinity binding and efficient presentation by B*2703. Our results suggest that B*2703 will bind and present efficiently only a subset of the peptides that bind to B*2705, in particular those with Arg or Lys at P1. The apparent lack of disease in individuals with B*2703 may be due to an inability to bind and present putative arthritogenic peptides.


Journal article



Publication Date





121 - 130


Alleles, Amino Acid Sequence, Antigen Presentation, Arthritis, Base Sequence, Binding Sites, DNA, HLA-B27 Antigen, Humans, Influenza A virus, Molecular Sequence Data, Mutagenesis, Site-Directed, Nucleoproteins, Peptides, Protein Binding, RNA-Binding Proteins, Spinal Diseases, T-Lymphocytes, Cytotoxic, Viral Core Proteins