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.
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Tanigaki, N., Fruci, D., Vigneti, E. et al. The peptide binding specificity of HLA-B27 subtypes. Immunogenetics 40, 192–198 (1994). https://doi.org/10.1007/BF00167079
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DOI: https://doi.org/10.1007/BF00167079