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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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/100e1c2461b14a39be4cdf8caf230db8
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spelling	oai:doaj.org-article:100e1c2461b14a39be4cdf8caf230db82021-12-02T15:34:38ZTrapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction10.1038/s41467-017-02312-72041-1723https://doaj.org/article/100e1c2461b14a39be4cdf8caf230db82018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02312-7https://doaj.org/toc/2041-1723IgE 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.Frederic JabsMelanie PlumNick S. LaursenRasmus K. JensenBrian MølgaardMichaela MieheMarco MandolesiMichèle M. RauberWolfgang PfütznerThilo JakobChristian MöbsGregers R. AndersenEdzard SpillnerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
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 Portfolio
publishDate	2018
url	https://doaj.org/article/100e1c2461b14a39be4cdf8caf230db8
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Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction

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