The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab

The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab

Immunoglobulin E (IgE) plays a central role in allergic responses, yet therapeutic targeting of IgE with antibodies such as omalizumab is met with various limitations. Here the authors characterize the molecular properties and crystal structure of a new anti-IgE antibody, ligelizumab, for mechanisti...

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Autores principales: Pascal Gasser, Svetlana S. Tarchevskaya, Pascal Guntern, Daniel Brigger, Rahel Ruppli, Noemi Zbären, Silke Kleinboelting, Christoph Heusser, Theodore S. Jardetzky, Alexander Eggel
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Q
Acceso en línea:https://doaj.org/article/e445acdbe9e24d959b171d05c7983a61
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spelling oai:doaj.org-article:e445acdbe9e24d959b171d05c7983a612021-12-02T15:37:13ZThe mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab10.1038/s41467-019-13815-w2041-1723https://doaj.org/article/e445acdbe9e24d959b171d05c7983a612020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13815-whttps://doaj.org/toc/2041-1723Immunoglobulin E (IgE) plays a central role in allergic responses, yet therapeutic targeting of IgE with antibodies such as omalizumab is met with various limitations. Here the authors characterize the molecular properties and crystal structure of a new anti-IgE antibody, ligelizumab, for mechanistic insights related to its enhanced suppression activity.Pascal GasserSvetlana S. TarchevskayaPascal GunternDaniel BriggerRahel RuppliNoemi ZbärenSilke KleinboeltingChristoph HeusserTheodore S. JardetzkyAlexander EggelNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Pascal Gasser
Svetlana S. Tarchevskaya
Pascal Guntern
Daniel Brigger
Rahel Ruppli
Noemi Zbären
Silke Kleinboelting
Christoph Heusser
Theodore S. Jardetzky
Alexander Eggel
The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
description Immunoglobulin E (IgE) plays a central role in allergic responses, yet therapeutic targeting of IgE with antibodies such as omalizumab is met with various limitations. Here the authors characterize the molecular properties and crystal structure of a new anti-IgE antibody, ligelizumab, for mechanistic insights related to its enhanced suppression activity.
format article
author Pascal Gasser
Svetlana S. Tarchevskaya
Pascal Guntern
Daniel Brigger
Rahel Ruppli
Noemi Zbären
Silke Kleinboelting
Christoph Heusser
Theodore S. Jardetzky
Alexander Eggel
author_facet Pascal Gasser
Svetlana S. Tarchevskaya
Pascal Guntern
Daniel Brigger
Rahel Ruppli
Noemi Zbären
Silke Kleinboelting
Christoph Heusser
Theodore S. Jardetzky
Alexander Eggel
author_sort Pascal Gasser
title The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
title_short The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
title_full The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
title_fullStr The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
title_full_unstemmed The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
title_sort mechanistic and functional profile of the therapeutic anti-ige antibody ligelizumab differs from omalizumab
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/e445acdbe9e24d959b171d05c7983a61
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