T-cell studies in the spondyloarthropathies

Author:

Märker-Hermann Elisabeth,Schwab Pascale

Publisher

Springer Science and Business Media LLC

Subject

Rheumatology

Reference61 articles.

1. Gao X-M, Wordsworth P, McMichael AJ, et al.: Homocysteine modicifcation of HLA antigens and its immunological consequences. Eur J Immunol 1996, 26:1443–1450.

2. Allen RL, O’Callaghan CA, McMichael AJ, Bowness P: Cutting edge: HLA-B27 can form a novel beta 2-microglobulin-free heavy chain homodimer structure. J Immunol 1999, 162:5045–5048. It is shown that free HLA-B27 heavy chains can form a disulfidebonded homodimer, dependent on residue Cys67 in their extracellular alpha 1 domain. Despite the absence of b 2-microglobulin, HLA-B27 heavy chain homodimers were stabilized by a known peptide epitope. Heavy chain-B27 homodimer formation might explain the ability of HLA-B27 to induce spondyloarthropathy in β 2-microglobulin-deficient mice.

3. Benjamin R, Parham P: Guilt by association: HLA-B27 and ankylosing spondylitis. Immunol Today 1990, 11:137–142.

4. Krebs S, Rognan D, López de Castro JA: Long-range effects in protein-ligand interactions mediate peptide specificity in the human histocompatibility antigen HLA-B27 (B*2701). Protein Sci 1999, 8:1393–1399.

5. Zhou M, Sayad A, Simmos WA, et al.: The specificity of peptides bound to HLA-B 27 influences the prevalence of arthritis in HLA-B27 transgenic rats. J Exp Med 1998, 188:877–886. High-affinity binding of an influenza nucleoprotein to HLA-B 27 in the B27 transgenic rat decreases these ratés tendency to spontaneously develop spondyloarthropathy. This study confirms the need for binding of a peptide to B27 to trigger disease and suggests future treatment strategies.

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