title: HLA-B27 structure, function, and disease association.
abstract: The polymorphism of HLA-B27 alleles is located in the peptide-anchoring motif. In recent years, fundamental insights have been made into the molecular aspects of HLA-B27-restricted presentation. Subtle differences in peptide binding fine specificity are especially interesting for closely related HLA-B27 alleles that have differential association with ankylosing spondylitis. Bacterial infection has been suggested to play a role in the pathogenesis of HLA-B27-associated disease. Remarkable progress has been made in identifying peptides derived from bacteria that can be presented by HLA-B27. Despite the mechanisms proposed to explain B27-associated diseases, there are no clear correlations between peptide sequence, differential binding to B27 subtypes, and recognition by peptide-specific T cell receptors. Furthermore, new transgenic models have now been developed that we hope will allow a clearer view of the function of B27 and the mechanisms involved in the pathogenesis of spondyloarthropathies.
authors.affiliation: Servicio de Inmunologia, Hospital Central de Asturias, Oviedo, Spain.
authors.forename: C
authors.initials: C
authors.lastname: López-Larrea
authors.forename: S
authors.initials: S
authors.lastname: Gonzalez-Roces
authors.forename: V
authors.initials: V
authors.lastname: Alvarez
mesh_terms: D015796:HLA-B27 Antigen / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D006801:Humans; D013167:Spondylitis, Ankylosing / Q000276:immunology* / Q000503:physiopathology
chemical_list: D015796:HLA-B27 Antigen