Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction

IgE is linked to allergic diseases and there is a great interest in developing anti-IgE therapeutics. Here the authors characterize the binding of human IgE Fc to a single domain antibody (sdab) and show that the sdab induces a closed conformation, which prevents and disrupts IgE binding to its rece...

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Bibliographic Details
Main Authors: Frederic Jabs, Melanie Plum, Nick S. Laursen, Rasmus K. Jensen, Brian Mølgaard, Michaela Miehe, Marco Mandolesi, Michèle M. Rauber, Wolfgang Pfützner, Thilo Jakob, Christian Möbs, Gregers R. Andersen, Edzard Spillner
Format: Article
Language:English
Published: Nature Publishing Group 2018-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02312-7
Description
Summary:IgE is linked to allergic diseases and there is a great interest in developing anti-IgE therapeutics. Here the authors characterize the binding of human IgE Fc to a single domain antibody (sdab) and show that the sdab induces a closed conformation, which prevents and disrupts IgE binding to its receptor FcεRI and abrogates allergen mediated activation.
ISSN:2041-1723