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

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)192-198
Number of pages7
JournalImmunogenetics
Volume40
Issue number3
DOIs
Publication statusPublished - Jul 1994

ASJC Scopus subject areas

  • Immunology
  • Genetics

Fingerprint Dive into the research topics of 'The peptide binding specificity of HLA-B27 subtypes'. Together they form a unique fingerprint.

  • Cite this

    Tanigaki, N., Fruci, D., Vigneti, E., Starace, G., Rovero, P., Londei, M., Butler, R. H., & Tosi, R. (1994). The peptide binding specificity of HLA-B27 subtypes. Immunogenetics, 40(3), 192-198. https://doi.org/10.1007/BF00167079