HLA-B27

Possession of the human leukocyte antigen (HLA) class I molecule B27 is strongly associated with ankylosing spondylitis (AS), but the pathogenic role of HLA-B27 is unknown. Two broad theories most likely explain the role of HLA-B27 in AS pathogenesis. The first is based on the natural immunological...

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主要作者: Bowness, P
格式: Journal article
语言:English
出版: Annual Reviews 2015
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author Bowness, P
author_facet Bowness, P
author_sort Bowness, P
collection OXFORD
description Possession of the human leukocyte antigen (HLA) class I molecule B27 is strongly associated with ankylosing spondylitis (AS), but the pathogenic role of HLA-B27 is unknown. Two broad theories most likely explain the role of HLA-B27 in AS pathogenesis. The first is based on the natural immunological function of HLA-B27 of presenting antigenic peptides to cytotoxic T cells. Thus, HLA-B27-restricted immune responses to self-antigens, or arthritogenic peptides, might drive immunopathology. B27 can also "behave badly," misfolding during assembly and leading to endoplasmic reticulum stress and autophagy responses. β2m-free B27 heavy chain structures including homodimers (B272) can also be expressed at the cell surface following endosomal recycling of cell surface heterotrimers. Cell surface free heavy chains and B272 bind to innate immune receptors on T, NK, and myeloid cells with proinflammatory effects. This review describes the natural function of HLA-B27, its disease associations, and the current theories as to its pathogenic role.
first_indexed 2024-03-06T22:27:29Z
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spelling oxford-uuid:572356a2-a2fd-4efc-bbfa-e03f789f6e252022-03-26T16:54:51ZHLA-B27Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:572356a2-a2fd-4efc-bbfa-e03f789f6e25EnglishSymplectic Elements at OxfordAnnual Reviews2015Bowness, PPossession of the human leukocyte antigen (HLA) class I molecule B27 is strongly associated with ankylosing spondylitis (AS), but the pathogenic role of HLA-B27 is unknown. Two broad theories most likely explain the role of HLA-B27 in AS pathogenesis. The first is based on the natural immunological function of HLA-B27 of presenting antigenic peptides to cytotoxic T cells. Thus, HLA-B27-restricted immune responses to self-antigens, or arthritogenic peptides, might drive immunopathology. B27 can also "behave badly," misfolding during assembly and leading to endoplasmic reticulum stress and autophagy responses. β2m-free B27 heavy chain structures including homodimers (B272) can also be expressed at the cell surface following endosomal recycling of cell surface heterotrimers. Cell surface free heavy chains and B272 bind to innate immune receptors on T, NK, and myeloid cells with proinflammatory effects. This review describes the natural function of HLA-B27, its disease associations, and the current theories as to its pathogenic role.
spellingShingle Bowness, P
HLA-B27
title HLA-B27
title_full HLA-B27
title_fullStr HLA-B27
title_full_unstemmed HLA-B27
title_short HLA-B27
title_sort hla b27
work_keys_str_mv AT bownessp hlab27