Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex

Luke F. Pennington; Pascal Gasser; Silke Kleinboelting; Chensong Zhang; Georgios Skiniotis; Alexander Eggel; Theodore S. Jardetzky

doi:10.1038/s41467-021-27397-z

Nature Communications (Dec 2021)

Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex

Luke F. Pennington,
Pascal Gasser,
Silke Kleinboelting,
Chensong Zhang,
Georgios Skiniotis,
Alexander Eggel,
Theodore S. Jardetzky

Affiliations

Luke F. Pennington: Department of Structural Biology, Stanford University School of Medicine
Pascal Gasser: Department of Rheumatology and Immunology, University Hospital Bern
Silke Kleinboelting: Department of Structural Biology, Stanford University School of Medicine
Chensong Zhang: Department of Molecular and Cellular Physiology, Stanford University School of Medicine
Georgios Skiniotis: Department of Structural Biology, Stanford University School of Medicine
Alexander Eggel: Department of Rheumatology and Immunology, University Hospital Bern
Theodore S. Jardetzky: Department of Structural Biology, Stanford University School of Medicine

DOI: https://doi.org/10.1038/s41467-021-27397-z
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 16

Abstract

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Facilitated dissociation is a mechanism where antibody-mediated disruption of high-affinity complexes can enhance the therapeutic effects of a drug. Here the authors present a yeast display approach to select and engineer omalizumab variants that dissociate receptor-bound IgE to accelerate its inhibition of the allergic response.

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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