Human collagen II peptide 256–271 preferentially binds to HLA-DR molecules associated with susceptibility to rheumatoid arthritis

Abstract

 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 β-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.