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CUTTING EDGE |
Human Immunology Unit, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, United Kingdom.
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 
1 domain. Despite the absence of
ß2-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
ß2-microglobulin-deficient mice.
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A. N. Antoniou, S. Ford, J. D. Taurog, G. W. Butcher, and S. J. Powis Formation of HLA-B27 Homodimers and Their Relationship to Assembly Kinetics J. Biol. Chem., March 5, 2004; 279(10): 8895 - 8902. [Abstract] [Full Text] [PDF]
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L. H. Boyle and J. S. Hill Gaston Breaking the rules: the unconventional recognition of HLA-B27 by CD4+ T lymphocytes as an insight into the pathogenesis of the spondyloarthropathies Rheumatology, March 1, 2003; 42(3): 404 - 412. [Abstract] [Full Text] [PDF]
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E. May, M. L. Dorris, N. Satumtira, I. Iqbal, M. I. Rehman, E. Lightfoot, and J. D. Taurog CD8{alpha}{beta} T Cells Are Not Essential to the Pathogenesis of Arthritis or Colitis in HLA-B27 Transgenic Rats J. Immunol., January 15, 2003; 170(2): 1099 - 1105. [Abstract] [Full Text] [PDF]
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J. E. Boyson, R. Erskine, M. C. Whitman, M. Chiu, J. M. Lau, L. A. Koopman, M. M. Valter, P. Angelisova, V. Horejsi, and J. L. Strominger Disulfide bond-mediated dimerization of HLA-G on the cell surface PNAS, December 10, 2002; 99(25): 16180 - 16185. [Abstract] [Full Text] [PDF]
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A. Cauli, G. Dessole, M. T. Fiorillo, A. Vacca, A. Mameli, P. Bitti, G. Passiu, R. Sorrentino, and A. Mathieu Increased level of HLA-B27 expression in ankylosing spondylitis patients compared with healthy HLA-B27-positive subjects: a possible further susceptibility factor for the development of disease Rheumatology, December 1, 2002; 41(12): 1375 - 1379. [Abstract] [Full Text] [PDF]
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M. Hulsmeyer, R. C. Hillig, A. Volz, M. Ruhl, W. Schroder, W. Saenger, A. Ziegler, and B. Uchanska-Ziegler HLA-B27 Subtypes Differentially Associated with Disease Exhibit Subtle Structural Alterations J. Biol. Chem., November 27, 2002; 277(49): 47844 - 47853. [Abstract] [Full Text] [PDF]
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P. Malik, P. Klimovitsky, L.-W. Deng, J. E. Boyson, and J. L. Strominger Uniquely Conformed Peptide-Containing {beta}2-Microglobulin- Free Heavy Chains of HLA-B2705 on the Cell Surface J. Immunol., October 15, 2002; 169(8): 4379 - 4387. [Abstract] [Full Text] [PDF]
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P. Bowness HLA B27 in health and disease: a double-edged sword? Rheumatology, August 1, 2002; 41(8): 857 - 868. [Abstract] [Full Text] [PDF]
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N. S. Dangoria, M. L. DeLay, D. J. Kingsbury, J. P. Mear, B. Uchanska-Ziegler, A. Ziegler, and R. A. Colbert HLA-B27 Misfolding Is Associated with Aberrant Intermolecular Disulfide Bond Formation (Dimerization) in the Endoplasmic Reticulum J. Biol. Chem., June 21, 2002; 277(26): 23459 - 23468. [Abstract] [Full Text] [PDF]
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L. Sesma, V. Montserrat, J. R. Lamas, A. Marina, J. Vazquez, and J. A. L. de Castro The Peptide Repertoires of HLA-B27 Subtypes Differentially Associated to Spondyloarthropathy (B*2704 and B*2706) Differ by Specific Changes at Three Anchor Positions J. Biol. Chem., May 3, 2002; 277(19): 16744 - 16749. [Abstract] [Full Text] [PDF]
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R. L. Allen, T. Raine, A. Haude, J. Trowsdale, and M. J. Wilson Cutting Edge: Leukocyte Receptor Complex-Encoded Immunomodulatory Receptors Show Differing Specificity for Alternative HLA-B27 Structures J. Immunol., November 15, 2001; 167(10): 5543 - 5547. [Abstract] [Full Text] [PDF]
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W. Kuon, H.-G. Holzhutter, H. Appel, M. Grolms, S. Kollnberger, A. Traeder, P. Henklein, E. Weiss, A. Thiel, R. Lauster, et al. Identification of HLA-B27-Restricted Peptides from the Chlamydia trachomatis Proteome with Possible Relevance to HLA-B27-Associated Diseases J. Immunol., October 15, 2001; 167(8): 4738 - 4746. [Abstract] [Full Text] [PDF]
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M. R. Harris, L. Lybarger, N. B. Myers, C. Hilbert, J. C. Solheim, T. H. Hansen, and Y. Y. L. Yu Interactions of HLA-B27 with the peptide loading complex as revealed by heavy chain mutations Int. Immunol., October 1, 2001; 13(10): 1275 - 1282. [Abstract] [Full Text] [PDF]
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L. H. Boyle, J. C. Goodall, S. S. Opat, and J. S. H. Gaston The Recognition of HLA-B27 by Human CD4+ T Lymphocytes J. Immunol., September 1, 2001; 167(5): 2619 - 2624. [Abstract] [Full Text] [PDF]
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J. A. Urvater, H. Hickman, J. L. Dzuris, K. Prilliman, T. M. Allen, K. J. Schwartz, D. Lorentzen, C. Shufflebotham, E. J. Collins, D. L. Neiffer, et al. Gorillas with Spondyloarthropathies Express an MHC Class I Molecule with Only Limited Sequence Similarity to HLA-B27 that Binds Peptides with Arginine at P2 J. Immunol., March 1, 2001; 166(5): 3334 - 3344. [Abstract] [Full Text] [PDF]
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A. W. Purcell, J. J. Gorman, M. Garcia-Peydro, A. Paradela, S. R. Burrows, G. H. Talbo, N. Laham, C. A. Peh, E. C. Reynolds, J. A. Lopez de Castro, et al. Quantitative and Qualitative Influences of Tapasin on the Class I Peptide Repertoire J. Immunol., January 15, 2001; 166(2): 1016 - 1027. [Abstract] [Full Text] [PDF]
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E. Zanelli, F. C. Breedveld, and R. R. P. de Vries HLA association with autoimmune disease: a failure to protect? Rheumatology, October 1, 2000; 39(10): 1060 - 1066. [Abstract] [Full Text] [PDF]
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J. P. Mear, K. L. Schreiber, C. Munz, X. Zhu, S. Stevanovic, H.-G. Rammensee, S. L. Rowland-Jones, and R. A. Colbert Misfolding of HLA-B27 as a Result of Its B Pocket Suggests a Novel Mechanism for Its Role in Susceptibility to Spondyloarthropathies J. Immunol., December 15, 1999; 163(12): 6665 - 6670. [Abstract] [Full Text] [PDF]
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S. Dedier, S. Reinelt, T. Reitinger, G. Folkers, and D. Rognan Thermodynamic Stability of HLA-B*2705{middle dot}Peptide Complexes. EFFECT OF PEPTIDE AND MAJOR HISTOCOMPATIBILITY COMPLEX PROTEIN MUTATIONS J. Biol. Chem., August 25, 2000; 275(35): 27055 - 27061. [Abstract] [Full Text] [PDF]
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S. Reinelt, S. Dedier, G. Asuni, G. Folkers, and D. Rognan Mutation of Cys-67 Alters the Thermodynamic Stability of the Human Leukocyte Antigen HLA-B*2705 J. Biol. Chem., May 18, 2001; 276(21): 18472 - 18477. [Abstract] [Full Text] [PDF]
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I. Alvarez, M. Marti, J. Vazquez, E. Camafeita, S. Ogueta, and J. A. Lopez de Castro The Cys-67 Residue of HLA-B27 Influences Cell Surface Stability, Peptide Specificity, and T-cell Antigen Presentation J. Biol. Chem., December 21, 2001; 276(52): 48740 - 48747. [Abstract] [Full Text] [PDF]
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