Evidence map›Paper›PMID 22815482›Full record

ArticleThe Journal of biological chemistry2012

Mapping of the CD23 binding site on immunoglobulin E (IgE) and allosteric control of the IgE-Fc epsilonRI interaction.

Susmita Borthakur, Richard G Hibbert, Marie O Y Pang, Norhakim Yahya, Heather J Bax, Michael W Kao, Alison M Cooper, Andrew J Beavil, Brian J Sutton, Hannah J Gould and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. 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 · 2026
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  4. Review
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  11. Thermal sensitivity and flexibility of the Cε3 domains in immunoglobulin E.Biochimica et biophysica acta. Proteins and proteomics · 2017
    Article
  12. Article
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  15. A range of Cℇ3-Cℇ4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  16. Article
  17. General mechanism for modulating immunoglobulin effector function.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Susmita BorthakurRandall Division of Cell and Molecular Biophysics, King's College London, Guy's Campus, London SE1 1UL, United Kingdom.
Richard G Hibbert
Marie O Y Pang
Norhakim Yahya
Heather J Bax
Michael W Kao
Alison M Cooper
Andrew J Beavil
Brian J Sutton
Hannah J Gould
James M McDonnell
Asthma UK · GBKing's College London · GBUniversity of Oxford · GB

Funding

Medical Research Council G0001352Medical Research Council G0400106Medical Research Council G1000758Medical Research Council MR/J006742/1Wellcome Trust
6 · The paper itself

Abstract

IgE, the antibody that mediates allergic responses, acts as part of a self-regulating protein network. Its unique effector functions are controlled through interactions of its Fc region with two cellular receptors, FcεRI on mast cells and basophils and CD23 on B cells. IgE cross-linked by allergen triggers mast cell activation via FcεRI, whereas IgE-CD23 interactions control IgE expression levels. We have determined the CD23 binding site on IgE, using a combination of NMR chemical shift mapping and site-directed mutagenesis. We show that the CD23 and FcεRI interaction sites are at opposite ends of the Cε3 domain of IgE, but that receptor binding is mutually inhibitory, mediated by an allosteric mechanism. This prevents CD23-mediated cross-linking of IgE bound to FcεRI on mast cells and resulting antigen-independent anaphylaxis. The mutually inhibitory nature of receptor binding provides a degree of autonomy for the individual activities mediated by IgE-FcεRI and IgE-CD23 interactions.

Indexed as

Allosteric RegulationBasophilsCell LineHumansImmunoglobulin EMast CellsMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPeptide MappingProtein BindingProtein Structure, TertiaryReceptors, IgEImmunoglobulin EReceptors, IgE

Identifiers

PMID22815482
PMCPMC3438978
OpenAlexW2025712675

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

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.