DARPins against a functional IgE epitope

Baumann, Michael J; Eggel, Alexander; Amstutz, Patrick; Stadler, Beda M; Vogel, Monique (2010). DARPins against a functional IgE epitope. Immunology letters, 133(2), pp. 78-84. Amsterdam: Elsevier 10.1016/j.imlet.2010.07.005

Full text not available from this repository.

The monoclonal anti-IgE antibody omalizumab (Xolair is mostly used for the treatment of severe allergic asthma. However, the requirement of high doses and suboptimal cost-effectiveness limits the use of the treatment. Here we propose to use a new drug format based on non-immunoglobulin structures, potentially offering increased clinical efficacy while being more cost-effective. For this purpose, DARPins (designed ankyrin repeat proteins) against the constant heavy chain region of IgE have been isolated. DARPins were binding to IgE with high specificity and affinities in the low nanomolar range. Selected DARPins antagonized the interaction between IgE and its high-affinity receptor in inhibition assays. Furthermore, anti-IgE DARPins were shown to inhibit proinflammatory mediator release from rat basophilic leukemia cells expressing human high-affinity IgE receptors with higher efficacy than the monoclonal anti-IgE antibody omalizumab. DARPins may thus represent promising future drug candidates for the treatment of allergy.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Institute for Immunology [discontinued]
UniBE Contributor:	Stadler, Beda Martin, Vogel, Monique
ISSN:	0165-2478
Publisher:	Elsevier
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:11
Last Modified:	05 Dec 2022 14:01
Publisher DOI:	10.1016/j.imlet.2010.07.005
PubMed ID:	20673836
Web of Science ID:	000283396700004
URI:	https://boris.unibe.ch/id/eprint/1760 (FactScience: 203734)