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HLA-B27 has a striking association with inflammatory arthritis. We show that free HLA-B27 heavy chains can form a disulfide-bonded homodimer, dependent on residue Cys67 in their extracellular alpha 1 domain. Despite the absence of beta 2-microglobulin, HLA-B27 heavy chain homodimers (termed HC-B27) were stabilized by a known peptide epitope. HC-B27 complexes were recognized by the conformation-specific Ab W6/32, but not the ME1 Ab. Surface labeling and immunoprecipitation demonstrated the presence of similar W6/32-reactive free heavy chains at the surface of HLA-B27-transfected T2 cells. HC-B27 homodimer formation might explain the ability of HLA-B27 to induce spondyloarthropathy in beta 2-microglobulin-deficient mice.


Journal article


Journal of immunology (Baltimore, Md. : 1950)

Publication Date





5045 - 5048


Human Immunology Unit, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, United Kingdom.


Cell Line, Cell Membrane, Humans, Disulfides, Cysteine, beta 2-Microglobulin, HLA-B27 Antigen, Precipitin Tests, Transfection, Antibody Specificity, Antigen-Antibody Reactions, Protein Conformation, Dimerization