Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0003864 (arthritis)
 69,039 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

HLA-B*2705 transgenic mice were continuously backcrossed to mice of the B10 background with various haplotypes. A high level of expression of the HLA-B27 protein was detected on peripheral blood lymphocytes (PBLs) from mice homozygous for H-2b, H-2f, H-2s, H-2p, H-2r, and H-2k haplotypes by FACS analysis with the ME-1 antibody. A lower level of expression of B27 was observed on PBLs from H-2v mice. Little or no expression of B27 was detected on PBLs from H-2 or H-2d mice. We hypothesize that the HLA-B27 heavy chain is analogous to and competes with endogenous class I heavy chains in the H-2d, H-2q and H-2v haplotypes. Interestingly, other studies in our laboratory have demonstrated that mice with the H-2d and H-2q haplotypes with deletions of certain T cell receptor subsets are more prone to Yersinia-induced arthritis (YIA). Therefore, the mouse model of YIA may provide insights into the mechanisms of HLA-B27-linked spondyloarthropathies in man.
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PMID:Effect of H-2 genes on expression of HLA-B27 and Yersinia-induced arthritis. 225 92

A unique feature of patients with ankylosing spondylitis and reactive arthritis is that almost all share the HLA type B27. The primary structures of the HLA-B27 antigens have been determined. At least six variants exist. However, disease predisposition does not appear to be restricted to a particular variant. One hypothesis about the pathogenesis of arthritis is that the bacteria that cause the arthritis carry components that are cross-reactive with HLA-B27 antigens. Several reactive bacterial components have indeed been identified using monoclonal anti-HLA-B27 antibodies. Even more striking is the identification, through a computerized search, of a Klebsiella protein. This protein carries a stretch of six amino acids identical to residues 72 to 77 of two of the HLA-B27 variants. A synthetic peptide carrying these six amino acids of HLA-B27 protein is reactive with serum antibodies in some patients with arthritis. With this knowledge, investigators will be able to formulate new approaches for examining the pathogenesis of HLA-B27-associated arthritis.
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PMID:Molecular mimicry in HLA-B27-related arthritis. 234 16

Immunologic cross-reactivity between enteric bacteria and the HLA-B27 protein may play a role in the etiology of Reiter's syndrome and reactive arthritis. The reactivity of two anti-B27 mAb (B27M1 and B27M2) with envelope proteins of Shigella flexneri isolated from Reiter's syndrome patients was studied by Western blot analysis. Proteins with an apparent Mr of approximately 36 and 23 kDa reacted with both mAb in ascites. mAb against related HLA class I Ag B7 and B40 did not react with the 23 kDa protein. Relatively high concentrations of antibody were required for reactivity, suggesting a low affinity interaction. Additional evidence for cross-reactive epitopes was obtained by ELISA against whole envelope and by using unsolubilized envelope to inhibit binding of M1 and M2 to B27-positive cell lines, as measured by quantitative flow microfluorimetry. The presence of cross-reactive proteins was not related to the presence of the intact virulence-associated plasmid or the invasive phenotype. Two Shigella sonnei isolates not implicated as causative agents of Reiter's syndrome or reactive arthritis showed a similar pattern of cross-reactivity. These results indicate that cross-reactive epitopes may be present on "arthritogenic" bacteria, but their presence is not a unique feature of such strains and is not the sole factor in induction of arthritis in B27-positive individuals.
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PMID:Reaction of anti-HLA-B monoclonal antibodies with envelope proteins of Shigella species. Evidence for molecular mimicry in the spondyloarthropathies. 328 36