Literature DB >> 2512043

A monoclonal anti-HLA-B27 antibody which is reactive with a linear sequence of the HLA-B27 protein is useful for the study of molecular mimicry.

Z Yong1, J J Zhang, T Schaack, S Chen, A Nakayama, D T Yu.   

Abstract

In the search for cross-reactivity between bacteria and HLA-B27, three groups of investigators have identified several bacterial envelope proteins which are reactive with the monoclonal anti-HLA-B27 antibodies B27.M1 and B27.M2. Since these two antibodies react poorly with HLA-B27-derived synthetic peptides, it is not possible to locate the reactive epitopes on the HLA-B27 using synthetic peptides. Here, we introduce Ye-2, a monoclonal anti-HLA-B27 antibody which, unlike B27.M1 and B27.M2, is reactive with a synthetic peptide derived from residues 63-84 of HLA-B27.1. Analysis with a cross-reactive peptide derived from residues 226-244 of bovine carbonic anhydrase suggests that only a few of the amino acid residues in the HLA-B27-derived peptide are responsible for the reactivity. This antibody should be a useful adjunct in a preliminary assessment of whether a bacterial protein mimics HLA-B27 in primary structure.

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Year:  1989        PMID: 2512043

Source DB:  PubMed          Journal:  Clin Exp Rheumatol        ISSN: 0392-856X            Impact factor:   4.473


  3 in total

1.  Analysis of the molecular mimicry between HLA-B27 and a bacterial OmpA protein using synthetic peptides.

Authors:  D T Yu; T Hamachi; M Hamachi; G Tribbick
Journal:  Clin Exp Immunol       Date:  1991-09       Impact factor: 4.330

Review 2.  Molecular mimicry: any role in the pathogenesis of spondyloarthropathies?

Authors:  R Lahesmaa; M Skurnik; P Toivanen
Journal:  Immunol Res       Date:  1993       Impact factor: 2.829

3.  HLA-B27/microbial mimicry: an in vivo analysis.

Authors:  K Kapasi; B Chui; R D Inman
Journal:  Immunology       Date:  1992-11       Impact factor: 7.397

  3 in total

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