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Circulating human IgG autoanti-IgE antibodies in asthma patients block the binding of IgE to its high affinity receptor
  1. S J Smith,
  2. A Galvin,
  3. I Hall,
  4. F Shakib
  1. Division of Molecular and Clinical Immunology, University of Nottingham Medical School, Nottingham
  2. Department of Therapeutics, University of Nottingham Medical School, Nottingham

    Abstract

    Aims—To investigate the ability of circulating human IgG autoanti-IgE antibodies from asthma patients to block the binding of IgE to the α chain of the high affinity receptor (FcεRI).

    Methods—This involved the use of a well validated flow cytometric method to detect inhibition of FITC labelled IgE binding to a fibroblast cell line (CHK1E1) transfected with the α chain of FcεRI.

    Results—IgG autoanti-IgE-containing sera blocked the binding of IgE-FITC to the CHK1E1 cells. No such inhibition was demonstrable with rheumatoid sera containing autoanti-IgG (that is, rheumatoid factor) but lacking autoanti-IgE. Percentage inhibition (up to 50%) of IgE binding to the CHK1E1 cells was directly related to the titre of IgG1, but not IgG4, autoanti-IgE in the sera tested (correlation coefficient 0·66, probability 0·003).

    Conclusions—The capacity of anti-IgE to block the binding of IgE to FcεRI has important clinical implications, particularly in terms of downregulation of allergic reactions.

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