Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-20T13:43:20.986Z Has data issue: false hasContentIssue false

HLA-B27 and disease pathogenesis: new structural and functional insights

Published online by Cambridge University Press:  11 February 2004

Paul Bowness
Affiliation:
MRC Human Immunology Unit, Institute of Molecular Medicine, Headington, Oxford, OX3 9DS, UK.
Nathan Zaccai
Affiliation:
Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Headington, Oxford, OX3 7BN, UK.
Lucy Bird
Affiliation:
MRC Human Immunology Unit, Institute of Molecular Medicine, Headington, Oxford, OX3 9DS, UK.
E. Yvonne Jones
Affiliation:
Wellcome Trust Centre for Human Genetics, Roosevelt Drive, Headington, Oxford, OX3 7BN, UK.

Abstract

The human leukocyte antigen class I allele HLA-B27 is a major histocompatibility complex (MHC) antigen that is strongly associated with the spondyloarthritic group of human rheumatic diseases, the most commmon of which is ankylosing spondylitis. Although the mechanism underlying this disease association remains unknown, numerous theories have been proposed. Much more is known of the natural role of HLA-B27 in binding and presenting antigenic peptides to T cells. The ‘arthritogenic peptide hypothesis’ suggests that the role of HLA-B27 in disease relates to its specificity for binding certain peptides. Recently, it has also been shown that HLA-B27 has an unusual cell biology and can adopt a novel homodimeric structure. In this review, a molecular model of the HLA-B27 homodimer is presented and the possible pathogenic significance of such a structure is discussed.

Type
Review Article
Copyright
© Cambridge University Press 1999

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)