Tanigaki N, Fruci D, Vigneti E, Starace G, Rovero P, Londei M, Butler R H, Tosi R
Istituto di Biologia Cellulare, CNR, Roma, Italy.
Immunogenetics. 1994;40(3):192-8. doi: 10.1007/BF00167079.
Five HLA-B27 subtypes, B2701, B2703, B2704, B2705, and B2706, 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 B2705. The peptide sequences were derived from human HSP89 alpha, P53 and MBP. The alpha chains were immunospecifically isolated from LH (B2701), CH (B2703), WE1 (B2704), BTB (B2705), and LIE (B2706) 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 B2705 and a new motif H-R were accepted by B2703, B2704, and B2706, but not by B2701. However, other motifs, including known B2702 and/or B2705 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.
对五种HLA - B27亚型，即B2701、B2703、B2704、B2705和B2706，进行了与26种携带与B2705相关的主要锚定残基基序（第2和9位氨基酸残基的组合）的合成九肽直接结合的测试。这些肽序列源自人HSP89α、P53和MBP。从LH（B2701）、CH（B2703）、WE1（B2704）、BTB（B2705）和LIE（B2706）细胞中免疫特异性分离出α链，并通过HLA I类α链重折叠试验测量其肽结合情况。获得的数据表明，所测试的B27亚型能够结合一组携带几种不同锚定残基基序的共同肽段。报告的B2705的基序R - K和R - R以及新基序H - R被B2703、B2704和B2706接受，但不被B2701接受。然而，其他基序，包括已知的B2702和/或B2705基序R - H、R - L、R - A和R - F，以及在此发现的新基序R - G，显然被所有测试的B27亚型接受。在B27亚组中观察到的交叉肽结合与强直性脊柱炎发病机制中所谓的致关节炎肽假说相符。
