ArticleThe Journal of allergy and clinical immunology2017
Critical and direct involvement of the CD23 stalk region in IgE binding.
Article in The Journal of allergy and clinical immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT05042830 (Contribution of Local Nasal IgE Production to the Boost of Systemic Allergen-specific IgE Production Upon Nasal Allergen Contact - an Explorative Pilot Study), which is not on this map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Contribution of Local Nasal IgE Production to the Boost of Systemic Allergen-specific IgE Production Upon Nasal Allergen Contact - an Explorative Pilot Study
Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Glycosylation as an intricate post-translational modification process takes part in glycoproteins related immunity.Cell communication and signaling : CCS · 2025Review
- Structural and Functional Insights Into IgE Receptor Interactions and Disruptive Inhibition.Immunological reviews · 2025Review
- Therapeutic monoclonal antibodies in allergy: Targeting IgE, cytokine, and alarmin pathways.Immunological reviews · 2024Review
- On the complexity of IgE: The role of structural flexibility and glycosylation for binding its receptors.Frontiers in allergy · 2023Review
- Review
- Antibody glycosylation in autoimmune diseases.Autoimmunity reviews · 2021Review
- Tracing Human IgE B Cell Antigen Receptor-Bearing Cells With a Monoclonal Anti-Human IgE Antibody That Specifically Recognizes Non-Receptor-Bound IgE.Frontiers in immunology · 2021Article
- Anti-IgE for the Treatment of Chronic Urticaria.ImmunoTargets and therapy · 2021Review
- The anti-IgE mAb omalizumab induces adverse reactions by engaging Fcγ receptors.The Journal of clinical investigation · 2020Article
- Allergen-specific IgE levels and the ability of IgE-allergen complexes to cross-link determine the extent of CD23-mediated T-cell activation.The Journal of allergy and clinical immunology · 2020Article
- Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction.Nature communications · 2018Article
- Allergen-Specific Antibodies Regulate Secondary Allergen-Specific Immune Responses.Frontiers in immunology · 2018Review
- Oral immunotherapy for food allergy.Seminars in immunology · 2017Review
- Serum free IgE guided dose reduction of omalizumab: a case report.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2017Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundThe 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.
objectiveWe sought to investigate the interaction between CD23, chimeric monoclonal human IgE, and the corresponding birch pollen allergen Bet v 1 at a molecular level.
methodsWe 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.
resultsA 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.
conclusionOur 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.