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Related Experiment Videos

IgM rheumatoid factors react with human class I HLA molecules

R C Williams1, C C Malone, K J Kao

  • 1Department of Medicine, University of Florida School of Medicine, Gainesville 32610, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|February 15, 1996
PubMed
Summary

Half of human IgM rheumatoid factors (RF) reacted with human class I molecules, suggesting cross-reactivity beyond beta 2 microglobulin. Specific epitopes and immunodominant residues on class I HLA regions were identified, indicating potential antigenic overlap in the Ig gene superfamily.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Rheumatology

Background:

  • Rheumatoid factors (RFs) are autoantibodies commonly found in rheumatoid arthritis.
  • Class I molecules, including HLA-A2 and HLA-B7, are crucial for immune responses.
  • The potential cross-reactivity between RFs and class I molecules is not fully understood.

Purpose of the Study:

  • To investigate the reactivity of human IgM RFs with human class I molecules.
  • To identify specific epitopes and residues on class I molecules targeted by RFs.
  • To explore the implications of this cross-reactivity in autoimmune diseases.

Main Methods:

  • Enzyme-linked immunosorbent assay (ELISA) was used to detect RF reactivity with isolated class I molecules and heavy chains.
  • ELISA inhibition assays were performed to demonstrate cross-reactivity.

Related Experiment Videos

  • Overlapping heptamers of A2 alpha 2 exons were synthesized to identify RF-reactive epitopes.
  • Site-directed mutagenesis (glycine-alanine substitution) was employed to pinpoint immunodominant residues.
  • Flow cytometry was used to assess RF binding to cell lines expressing class I molecules.

    • Main Results:

    • 50% of polyclonal IgM RFs showed positive ELISA reactions with isolated human class I molecules (A2 and B7).
    • RF reactivity was not solely due to anti-beta 2 microglobulin specificity.
    • Six RF-reactive epitopes within solvent-accessible regions of class I HLA molecules were identified.
    • Specific residues (R48, W51, E55, Y107, R108, W147, Q155, E172) were identified as immunodominant for RF binding.
    • RFs from rheumatoid arthritis patients' synovial B cells recognized these class I epitopes.
    • Patient sera exhibited significant binding to IgG and HLA-A2, unlike normal sera.

    Conclusions:

    • Human IgM RFs recognize specific determinants on human class I molecules.
    • The identified epitopes and immunodominant residues suggest structural similarities or shared antigenic determinants.
    • This cross-reactivity may contribute to the pathogenesis of rheumatoid arthritis and other autoimmune conditions.
    • Antigenic overlap among Ig gene superfamily products could explain the observed RF reactivity.