Structural basis of omalizumab therapy and omalizumab-mediated IgE exchange

Luke F. Pennington; Svetlana Tarchevskaya; Daniel Brigger; Karthik Sathiyamoorthy; Michelle T. Graham; Kari Christine Nadeau; Alexander Eggel; Theodore S. Jardetzky

doi:10.1038/ncomms11610

Nature Communications (May 2016)

Structural basis of omalizumab therapy and omalizumab-mediated IgE exchange

Luke F. Pennington,
Svetlana Tarchevskaya,
Daniel Brigger,
Karthik Sathiyamoorthy,
Michelle T. Graham,
Kari Christine Nadeau,
Alexander Eggel,
Theodore S. Jardetzky

Affiliations

Luke F. Pennington: Department of Structural Biology, Stanford University School of Medicine
Svetlana Tarchevskaya: Department of Structural Biology, Stanford University School of Medicine
Daniel Brigger: Department of Rheumatology, Immunology and Allergology, University Hospital Bern
Karthik Sathiyamoorthy: Department of Structural Biology, Stanford University School of Medicine
Michelle T. Graham: Sean N. Parker Center for Allergy Research at Stanford University, Stanford University School of Medicine
Kari Christine Nadeau: Progam in Immunology, Stanford University School of Medicine
Alexander Eggel: Department of Rheumatology, Immunology and Allergology, University Hospital Bern
Theodore S. Jardetzky: Department of Structural Biology, Stanford University School of Medicine

DOI: https://doi.org/10.1038/ncomms11610
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 12

Abstract

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Omalizumab is an antibody against IgE that is used to treat patients with asthma and chronic idiopathic urticaria. Here, the authors report the structure of omalizumab in complex with an IgE fragment and develop an approach to exchange rather than deplete IgE on human basophils to block their activation.

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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