Two potential therapeutic antibodies bind to a peptide segment of membrane-bound IgE in different conformations

Hsing-Mao Chu, Jon Wright, Yueh-Hsuan Chan, Chien-Jen Lin, Tse Wen Chang () and Carmay Lim ()
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Hsing-Mao Chu: The Genomics Research Center, Academia Sinica
Jon Wright: The Genomics Research Center, Academia Sinica
Yueh-Hsuan Chan: Fountain Biopharma Inc. Taipei
Chien-Jen Lin: The Genomics Research Center, Academia Sinica
Tse Wen Chang: The Genomics Research Center, Academia Sinica
Carmay Lim: Institute of Biomedical Sciences, Academia Sinica

Nature Communications, 2014, vol. 5, issue 1, 1-7

Abstract: Abstract IgE mediates hypersensitivity reactions responsible for most allergic diseases, which affect 20–40% of the population in developed countries. A 52-residue domain of membrane-bound IgE (mIgE) called CεmX is currently a target for developing therapeutic antibodies; however, its structure is unknown. Here we show that two antibodies with therapeutic potential in IgE-mediated allergic diseases, which can cause cytolytic effects on mIgE-expressing B lymphocytes and downregulate IgE production, target different conformations of an intrinsically disordered region (IDR) in the extracellular CεmX domain. We provide an important example of antibodies targeting an extracellular IDR of a receptor on the surface of intended target cells. We also provide fundamental structural characteristics unique to human mIgE, which may stimulate further studies to investigate whether other monoclonal antibodies (mAbs) targeting intrinsically disordered peptide segments or vaccine-like products targeting IDRs of a membrane protein can be developed.

Date: 2014
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DOI: 10.1038/ncomms4139

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