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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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

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spelling	doaj-100e1c2461b14a39be4cdf8caf230db82021-05-11T09:31:22ZengNature Publishing GroupNature Communications2041-17232018-01-019111110.1038/s41467-017-02312-7Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interactionFrederic Jabs0Melanie Plum1Nick S. Laursen2Rasmus K. Jensen3Brian Mølgaard4Michaela Miehe5Marco Mandolesi6Michèle M. Rauber7Wolfgang Pfützner8Thilo Jakob9Christian Möbs10Gregers R. Andersen11Edzard Spillner12Immunological Engineering, Department of Engineering, Aarhus UniversityImmunological Engineering, Department of Engineering, Aarhus UniversityDepartment of Molecular Biology and Genetics, Aarhus UniversityDepartment of Molecular Biology and Genetics, Aarhus UniversityImmunological Engineering, Department of Engineering, Aarhus UniversityImmunological Engineering, Department of Engineering, Aarhus UniversityImmunological Engineering, Department of Engineering, Aarhus UniversityClinical & Experimental Allergology, Department of Dermatology and Allergology, Philipps University MarburgClinical & Experimental Allergology, Department of Dermatology and Allergology, Philipps University MarburgDepartment of Dermatology and Allergology University Medical Center Giessen and Marburg, Justus-Liebig University GiessenClinical & Experimental Allergology, Department of Dermatology and Allergology, Philipps University MarburgDepartment of Molecular Biology and Genetics, Aarhus UniversityImmunological Engineering, Department of Engineering, Aarhus UniversityIgE 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.https://doi.org/10.1038/s41467-017-02312-7
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	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
spellingShingle	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 Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction Nature Communications
author_facet	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
author_sort	Frederic Jabs
title	Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction
title_short	Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction
title_full	Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction
title_fullStr	Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction
title_full_unstemmed	Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction
title_sort	trapping ige in a closed conformation by mimicking cd23 binding prevents and disrupts fcεri interaction
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2018-01-01
description	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.
url	https://doi.org/10.1038/s41467-017-02312-7
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Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction

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