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

Pascal Gasser; Svetlana S. Tarchevskaya; Pascal Guntern; Daniel Brigger; Rahel Ruppli; Noemi Zbären; Silke Kleinboelting; Christoph Heusser; Theodore S. Jardetzky; Alexander Eggel

doi:10.1038/s41467-019-13815-w

Nature Communications (Jan 2020)

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

Pascal Gasser,
Svetlana S. Tarchevskaya,
Pascal Guntern,
Daniel Brigger,
Rahel Ruppli,
Noemi Zbären,
Silke Kleinboelting,
Christoph Heusser,
Theodore S. Jardetzky,
Alexander Eggel

Affiliations

Pascal Gasser: Department of BioMedical Research, University of Bern
Svetlana S. Tarchevskaya: Department of Structural Biology, Stanford University School of Medicine
Pascal Guntern: Department of BioMedical Research, University of Bern
Daniel Brigger: Department of BioMedical Research, University of Bern
Rahel Ruppli: Department of BioMedical Research, University of Bern
Noemi Zbären: Department of BioMedical Research, University of Bern
Silke Kleinboelting: Department of Structural Biology, Stanford University School of Medicine
Christoph Heusser: Pharmaceutical Research, Novartis AG
Theodore S. Jardetzky: Department of Structural Biology, Stanford University School of Medicine
Alexander Eggel: Department of BioMedical Research, University of Bern

DOI: https://doi.org/10.1038/s41467-019-13815-w
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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