Elsevier

Immunology Today

Volume 11, 1990, Pages 137-142
Immunology Today

Review
Guilt by association: HLA-B27 and ankylosing spondylitis

https://doi.org/10.1016/0167-5699(90)90051-AGet rights and content

Abstract

The remarkable association between HLA-B27 and ankylosing spondylitis (AS) remains an enigma. While previous reviews have discussed the controversies surrounding the involvement of bacteria in the etiology of this disease and the sequence variability between subtypes of HLA-B27 (Ref. 3), concepts of disease mechanism remain ill-defined. In this article Richard Benjamin and Peter Parham synthesize new data on the structure and function of HLA class 1 molecules into possible mechanisms that might underly the pathogenesis of AS.

References (37)

  • A Keat

    Immunol. Today

    (1986)
  • J.A Lopez de Castro

    Immunol. Today

    (1989)
  • D.A Brewerton et al.

    Lancet

    (1973)
  • J.D Reveille et al.

    Am. J. Med.

    (1988)
  • M.B.A Oldstone

    Cell

    (1987)
  • J.S Sullivan et al.

    Am. J. Med.

    (1988)
  • H Von Boehmer et al.

    Immunol. Today

    (1989)
  • S.A Ellis et al.

    Hum. Immunol.

    (1982)
  • B.C Gilliland

    Harrison's Principles of Internal Medicine

  • L Schlosstein et al.

    New Engl. J. Med.

    (1973)
  • J.A Lochead et al.

    Arthritis Rheum.

    (1983)
  • J Welsh et al.

    Br. J. Exp. Pathol

    (1980)
  • J Chen et al.

    J. Immunol.

    (1987)
  • P.L Schwimmbeck et al.

    J. Exp. Med.

    (1987)
  • A.F Geczy et al.

    Nature

    (1980)
  • A.F Geczy et al.

    J. Exp. Med.

    (1986)
  • A van Leeuwen et al.
  • P.J Bjorkman et al.

    Nature

    (1987)
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      Explanatory difficulties connected with the fact that only certain HLA alleles are associated with a particular disease could be accounted for by assuming that conformational reorientations of a peptide as described here for the pVIPR-B*27:05 complex following exposure to Cu2+ or Ni2+ are less likely in subtypes that lack a disease association, such as B*27:09. As mentioned before, a particular arthritogenic peptide (24), possibly derived from a microorganism, would be superfluous in this scenario. A higher degree of molecular dynamics in the AS-associated subtypes B*27:05 and B*27:04 than in the nonassociated B*27:09 and B*27:06 molecules (15) supports the idea that HLA-B*27 polymorphisms, molecular flexibility, concomitant peculiarities in peptide repertoire, and presentation and ultimately AS association are intimately connected with each other.

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