Diab B Y, Lambert N C, L'Faqihi F E, Loubet-Lescoulié P, de Préval C, Coppin H
U. 395 INSERM, IFR 30 "INSERM-UPS-CNRS-CHU", CHU Purpan, F-31300 Toulouse, France.
Immunogenetics. 1999 Jan;49(1):36-44. doi: 10.1007/s002510050461.
The binding ability of 23 overlapping peptides, all derived from the CB11 fragment of CII, was tested on several HLA-DR molecules associated or not with disease susceptibility. These experiments were performed on a variety of cells expressing different HLA-DR molecules, using both indirect and direct binding assays. The CII (256-271) fragment was shown to bind to a restricted population among which the HLA-DR molecules associated with susceptibility to rheumatoid arthritis. The results also clearly indicate that the binding specificity of CII (256-271), among the DR4 molecules, is controlled by the nature of the HLA-DR molecule beta-chain residues 71 and 74, residues previously shown by X-ray crystallography to be involved in the HLA-DR/peptide interaction. The human CII (256-271) peptide is thus likely to play a role in the disease process.
对源自CII的CB11片段的23种重叠肽与几种与疾病易感性相关或无关的HLA - DR分子的结合能力进行了测试。这些实验在表达不同HLA - DR分子的多种细胞上进行，采用间接和直接结合试验。结果表明，CII（256 - 271）片段可与一部分受限群体结合，其中包括与类风湿性关节炎易感性相关的HLA - DR分子。结果还清楚地表明，在DR4分子中，CII（256 - 271）的结合特异性受HLA - DR分子β链第71和74位残基性质的控制，X射线晶体学先前已表明这些残基参与HLA - DR/肽相互作用。因此，人CII（256 - 271）肽可能在疾病进程中发挥作用。
