, Volume 40, Issue 3, pp 192–198 | Cite as

The peptide binding specificity of HLA-B27 subtypes

  • Nobuyuki Tanigaki
  • Doriana Fruci
  • Eliana Vigneti
  • Giuseppe Starace
  • Paolo Rovero
  • Marco Londei
  • Richard H. Butler
  • Roberto Tosi
Original Paper


Five HLA-B27 subtypes, B*2701, B*2703, B*2704, B*2705, and B*2706, were tested for direct binding with twenty-six synthetic nonapeptides carrying the primary anchor residue motifs (combination of amino residues at positions 2 and 9) relevant to B*2705. The peptide sequences were derived from human HSP89α, P53 and MBP. The alpha chains were immunospecifically isolated from LH (B*2701), CH (B*2703), WE1 (B*2704), BTB (B*2705), and LIE (B*2706) cells and their peptide binding was measured by the HLA class I alpha chain refolding assay. The data obtained indicated that the B27 subtypes tested can bind a common set of peptides carrying several different anchor residue motifs. The motifs, R-K and R-R, reported for B*2705 and a new motif H-R were accepted by B*2703, B*2704, and B*2706, but not by B*2701. However, other motifs, including known B*2702 and/or B*2705 motifs, R-H, R-L, R-A, and R-F, and a new motif found here, R-G, were apparently accepted by all B27 subtypes tested. The observed cross-peptide binding in the B27 subgroup is compatible with the so-called arthritogenic peptide hypothesis in the pathogenesis of ankylosing spondylitis.


Peptide Spondylitis Peptide Binding Direct Binding Alpha Chain 
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Copyright information

© Springer-Verlag 1994

Authors and Affiliations

  • Nobuyuki Tanigaki
    • 4
  • Doriana Fruci
    • 1
  • Eliana Vigneti
    • 1
  • Giuseppe Starace
    • 5
  • Paolo Rovero
    • 2
  • Marco Londei
    • 3
  • Richard H. Butler
    • 1
  • Roberto Tosi
    • 1
  1. 1.Istituto di Biologia Cellulare, CNRRomaItaly
  2. 2.Istituto di Mutagenesi e Differenziamento, CNRPisaItaly
  3. 3.Kennedy Institute of RheumatologyLondonUK
  4. 4.Roswell Park Cancer InstituteNYBuffaloUSA
  5. 5.Istituto di Medicina Sperimentale, CNRRomaItaly

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