Abstract
The arthritogenic peptide hypothesis has inspired research aimed at defining the peptide-presenting properties of HLA-B27 subtypes and their relation to ankylosing spondylitis. Various studies have shed new light on the influence of HLA-B27 polymorphism in modulating peptide binding and T-cell antigen presentation. Moreover, multiple factors along the antigen processing-loading pathway, including tapasin, contribute to shaping the HLA-B27 repertoire. Other studies have revealed significant peptide-binding similarities between HLA-B27 and subtypes of HLA-B39, supporting a role of this antigen in spondyloarthropathy. A putative pathogenetic role of the HLA-B27 heavy chain, initially suggested from studies in transgenic mice, is claimed on the basis of novel, yet circumstantial, evidence concerning an apparently unusual capacity of the heavy chain to form stable homodimers or misfold after biosynthesis. Finally, it appears that arthritogenic infections might downregulate HLA-B27 expression, favoring bacterial survival. The specificity and mechanism of this phenomenon are yet to be defined.
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