title: Structural polymorphism and function of HLA-B27.
abstract: Over the past year, new subtypes have been described and significant advances have been made in understanding peptide binding to HLA-B27. These developments help in interpreting how antigen presentation is modulated by HLA-B27 polymorphism, in determining the similarities and differences in T cell antigenicity among subtypes, and in finding the basis of HLA-B27 evolution. New insights into the pathogenetic link between enteric bacteria and HLA-B27 come from demonstration of a direct relationship between gut flora and joint inflammation in transgenic rats and from involvement of HLA-B27 in modulating bacterial invasion of mammalian cells. The association between HLA-B27 and spondyloarthropathy may be related to antigen-presenting specificity, but a different mechanism, presentation of a B27-derived peptide by class II antigens, may contribute to the pathogenesis of acute anterior uveitis, emphasizing the need for a comprehensive understanding of the structure, antigenicity, and function of HLA-B27.
authors.affiliation: Universidad Autónoma de Madrid, Facultad de Ciencas, Cantoblanco, Spain.
authors.forename: J A
authors.initials: JA
authors.lastname: López de Castro
mesh_terms: D000818:Animals; D001168:Arthritis / Q000276:immunology; D016918:Arthritis, Reactive / Q000276:immunology / Q000382:microbiology; D001324:Autoantigens; D000939:Epitopes; D015796:HLA-B27 Antigen / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D006801:Humans; D051379:Mice; D011110:Polymorphism, Genetic; D011485:Protein Binding; D013601:T-Lymphocytes / Q000276:immunology
chemical_list: D001324:Autoantigens; D000939:Epitopes; D015796:HLA-B27 Antigen