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Critical and direct involvement of the CD23 stalk region in IgE binding.

Title: Critical and direct involvement of the CD23 stalk region in IgE binding.
Name(s): Selb, Regina, author
Eckl-Dorna, Julia, author
Twaroch, Teresa E, author
Lupinek, Christian, author
Teufelberger, Andrea, author
Hofer, Gerhard, author
Focke-Tejkl, Margarete, author
Gepp, Barbara, author
Linhart, Birgit, author
Breiteneder, Heimo, author
Ellinger, Adolf, author
Keller, Walter, author
Roux, Kenneth H, author
Valenta, Rudolf, author
Niederberger, Verena, author
Type of Resource: text
Genre: Journal Article
Date Issued: 2017-01-01
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: The low-affinity receptor for IgE, FcεRII (CD23), contributes to allergic inflammation through allergen presentation to T cells, regulation of IgE responses, and enhancement of transepithelial allergen migration. We sought to investigate the interaction between CD23, chimeric monoclonal human IgE, and the corresponding birch pollen allergen Bet v 1 at a molecular level. We expressed 4 CD23 variants. One variant comprised the full extracellular portion of CD23, including the stalk and head domain; 1 variant was identical with the first, except for an amino acid exchange in the stalk region abolishing the N-linked glycosylation site; and 2 variants represented the head domain, 1 complete and 1 truncated. The 4 CD23 variants were purified as monomeric and structurally folded proteins, as demonstrated by gel filtration and circular dichroism. By using a human IgE mAb, the corresponding allergen Bet v 1, and a panel of antibodies specific for peptides spanning the CD23 surface, both binding and inhibition assays and negative stain electron microscopy were performed. A hitherto unknown IgE-binding site was mapped on the stalk region of CD23, and the non-N-glycosylated monomeric version of CD23 was superior in IgE binding compared with glycosylated CD23. Furthermore, we demonstrated that a therapeutic anti-IgE antibody, omalizumab, which inhibits IgE binding to FcεRI, also inhibited IgE binding to CD23. Our results provide a new model for the CD23-IgE interaction. We show that the stalk region of CD23 is crucially involved in IgE binding and that the interaction can be blocked by the therapeutic anti-IgE antibody omalizumab.
Identifier: FSU_pmch_27343203 (IID), 10.1016/j.jaci.2016.04.015 (DOI), PMC5321597 (PMCID), 27343203 (RID), 27343203 (EID), S0091-6749(16)30261-5 (PII)
Keywords: B cell, CD23, IgE, Allergen, Allergy, Low-affinity IgE receptor
Grant Number: F 4605
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at
Subject(s): Animals
Antigens, Plant/immunology
Binding Sites
Cell Line
Immunoglobulin E/immunology
Protein Binding/drug effects
Receptors, IgE/chemistry
Receptors, IgE/immunology
Persistent Link to This Record:
Host Institution: FSU
Is Part Of: The Journal of allergy and clinical immunology.
Issue: iss. 1, vol. 139

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Selb, R., Eckl-Dorna, J., Twaroch, T. E., Lupinek, C., Teufelberger, A., Hofer, G., … Niederberger, V. (2017). Critical and direct involvement of the CD23 stalk region in IgE binding. The Journal Of Allergy And Clinical Immunology. Retrieved from