ArticleThe Journal of biological chemistry2013
Ca2+-dependent structural changes in the B-cell receptor CD23 increase its affinity for human immunoglobulin E.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- 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
- Component-Resolved and Multiplex-Specific IgE Diagnostics: Utility in Anaphylaxis and Beyond.Children (Basel, Switzerland) · 2025Review
- A Comparison of Natural and Therapeutic Anti-IgE Antibodies.Antibodies (Basel, Switzerland) · 2024Review
- On the complexity of IgE: The role of structural flexibility and glycosylation for binding its receptors.Frontiers in allergy · 2023Review
- Reviving lost binding sites: Exploring calcium-binding site transitions between human and murine CD23.FEBS open bio · 2021Article
- Review
- The structure-based cancer-related single amino acid variation prediction.Scientific reports · 2021Article
- 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
- CD23 is a glycan-binding receptor in some mammalian species.The Journal of biological chemistry · 2019Article
- IgE Antibodies: From Structure to Function and Clinical Translation.Antibodies (Basel, Switzerland) · 2019Review
- Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.Scientific reports · 2018Article
- Thermal sensitivity and flexibility of the Cε3 domains in immunoglobulin E.Biochimica et biophysica acta. Proteins and proteomics · 2017Article
- Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab.The Journal of biological chemistry · 2017Article
- IgE binds asymmetrically to its B cell receptor CD23.Scientific reports · 2017Article
- 100 Years later: Celebrating the contributions of x-ray crystallography to allergy and clinical immunology.The Journal of allergy and clinical immunology · 2015Review
- Structural and Physical Basis for Anti-IgE Therapy.Scientific reports · 2015Article
- Types and effects of protein variations.Human genetics · 2015Article
- CD69 is the crucial regulator of intestinal inflammation: a new target molecule for IBD treatment?Journal of immunology research · 2015Review
- A range of Cℇ3-Cℇ4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Immunoglobulin E (IgE) antibodies play a fundamental role in allergic disease and are a target for therapeutic intervention. IgE functions principally through two receptors, FcεRI and CD23 (FcεRII). Minute amounts of allergen trigger mast cell or basophil degranulation by cross-linking IgE-bound FcεRI, leading to an inflammatory response. The interaction between IgE and CD23 on B-cells regulates IgE synthesis. CD23 is unique among Ig receptors in that it belongs to the C-type (calcium-dependent) lectin-like superfamily. Although the interaction of CD23 with IgE is carbohydrate-independent, calcium has been reported to increase the affinity for IgE, but the structural basis for this activity has previously been unknown. We have determined the crystal structures of the human lectin-like head domain of CD23 in its Ca(2+)-free and Ca(2+)-bound forms, as well as the crystal structure of the Ca(2+)-bound head domain of CD23 in complex with a subfragment of IgE-Fc consisting of the dimer of Cε3 and Cε4 domains (Fcε3-4). Together with site-directed mutagenesis, the crystal structures of four Ca(2+) ligand mutants, isothermal titration calorimetry, surface plasmon resonance, and stopped-flow analysis, we demonstrate that Ca(2+) binds at the principal and evolutionarily conserved binding site in CD23. Ca(2+) binding drives Pro-250, at the base of an IgE-binding loop (loop 4), from the trans to the cis configuration with a concomitant conformational change and ordering of residues in the loop. These Ca(2+)-induced structural changes in CD23 lead to additional interactions with IgE, a more entropically favorable interaction, and a 30-fold increase in affinity of a single head domain of CD23 for IgE. Taken together, these results suggest that binding of Ca(2+) brings an extra degree of modulation to CD23 function.
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