The pathogenesis of HLA-B27 associated arthritis: lessons from the B27 crystal |
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Authors: | H Kellnert D Yu |
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Institution: | (1) Medizinische Poliklinik, Klinikum Innenstadt, Universität Munchen, Pettenkoferstrasse 8a, D-80336, München, Germany;(2) Division of Rheumatology, University of California at Los Angeles, Los Angeles, USA |
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Abstract: | The most remarkable association between a major histocompatibility complex antigen and disease susceptibility - HLA-B27 and seronegative spondyloarthropathies, particularly ankylosing spondylitis - was discovered 20 years ago. During the two intervening decades advances in basic immunology and molecular biology have not only revealed the biosynthesis and structure of HLA-B27 but also given clues to the basic function of this molecule, the presentation of allele-specific peptides to CD8+ cytotoxic T cells. The recently reported three-dimensional structure of HLA-B27 and the identification of self-peptides bound to this major histocompatibility complex class I antigen can be viewed as a landmark in the understanding of the pathogenic role of HLA-B27. Based on crystallographic evidence, a peptide-binding motif can be postulated that should allow identification of HLA-B27 complexed peptides which may trigger an immune reaction causing arthritis.Abbreviations CTL
CD8+ cytotoxic T-cells
- TCR
T-cell receptor
- 2m
2-microglobulin
- LMP
low molecular mass polypeptide
Correspondence to: H. Kellner |
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Keywords: | HLA-B27 HLA class I antigens Spondyloarthropathies Ankylosing spondylitis HLA-B27 crystal |
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