ArticleProceedings of the National Academy of Sciences of the United States of America2012
Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor FcεRI.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.
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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.
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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.
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Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it, 90 citations in OpenAlex.
- Studies on allergic diseases and B cells in the past 20 years: a bibliometric analysis via CiteSpace and VOSviewer.Frontiers in immunology · 2026Pooled it
- Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Case for Anti-IgE Vaccination.Allergy · 2026Review
- High-affinity omalizumab variants with optimized disruptive potency prevent anaphylaxis in vivo.The Journal of allergy and clinical immunology · 2025Article
- Anti-IgD nanobodies as novel tools for studying human IgD biology.Scientific reports · 2025Article
- Maternal IgE Influence on Fetal and Infant Health.Immunological reviews · 2025Review
- Structural and Functional Insights Into IgE Receptor Interactions and Disruptive Inhibition.Immunological reviews · 2025Review
- The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.Proteins · 2025Article
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- The evolution of flexibility and function in the Fc domains of IgM, IgY, and IgE.Frontiers in immunology · 2024Article
- On the complexity of IgE: The role of structural flexibility and glycosylation for binding its receptors.Frontiers in allergy · 2023Review
- IgE-neutralizing UB-221 mAb, distinct from omalizumab and ligelizumab, exhibits CD23-mediated IgE downregulation and relieves urticaria symptoms.The Journal of clinical investigation · 2022Article
- Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex.Nature communications · 2021Article
- Review
- Structure-guided design of ultrapotent disruptive IgE inhibitors to rapidly terminate acute allergic reactions.The Journal of allergy and clinical immunology · 2021Article
- Tissues: the unexplored frontier of antibody mediated immunity.Current opinion in virology · 2021Review
- Past, present, and future of anti-IgE biologics.Allergy · 2020Review
- Immunoglobulins or Antibodies: IMGTBiomedicines · 2020Review
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab.Nature communications · 2020Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
The role of IgE in allergic disease mechanisms is performed principally through its interactions with two receptors, FcεRI on mast cells and basophils, and CD23 (FcεRII) on B cells. The former mediates allergic hypersensitivity, the latter regulates IgE levels, and both receptors, also expressed on antigen-presenting cells, contribute to allergen uptake and presentation to the immune system. We have solved the crystal structure of the soluble lectin-like "head" domain of CD23 (derCD23) bound to a subfragment of IgE-Fc consisting of the dimer of Cε3 and Cε4 domains (Fcε3-4). One CD23 head binds to each heavy chain at the interface between the two domains, explaining the known 2:1 stoichiometry and suggesting mechanisms for cross-linking membrane-bound trimeric CD23 by IgE, or membrane IgE by soluble trimeric forms of CD23, both of which may contribute to the regulation of IgE synthesis by B cells. The two symmetrically located binding sites are distant from the single FcεRI binding site, which lies at the opposite ends of the Cε3 domains. Structural comparisons with both free IgE-Fc and its FcεRI complex reveal not only that the conformational changes in IgE-Fc required for CD23 binding are incompatible with FcεRI binding, but also that the converse is true. The two binding sites are allosterically linked. We demonstrate experimentally the reciprocal inhibition of CD23 and FcεRI binding in solution and suggest that the mutual exclusion of receptor binding allows IgE to function independently through its two receptors.
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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.