Evidence map›Paper›PMID 28361904›Full record

ArticleScientific reports2017

IgE binds asymmetrically to its B cell receptor CD23.

Balvinder Dhaliwal, Marie O Y Pang, Anthony H Keeble, Louisa K James, Hannah J Gould, James M McDonnell, Brian J Sutton, Andrew J Beavil

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 37 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
    Article
  2. Review
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  4. Article
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  8. Generation and Characterization of Native and Sialic Acid-Deficient IgE.International journal of molecular sciences · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Mapping of the binding site for FcμR in human IgM-Fc.Biochimica et biophysica acta. Proteins and proteomics · 2020
    Article
  17. Review
  18. Article
  19. Article
  20. Thermal sensitivity and flexibility of the Cε3 domains in immunoglobulin E.Biochimica et biophysica acta. Proteins and proteomics · 2017
    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

8 authors at 1 institution in 1 country.

Balvinder DhaliwalDivision of Infection, Immunity and Respiratory Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Sciences Centre and Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, U.K.
Marie O Y PangRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
Anthony H KeebleRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
Louisa K JamesRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
Hannah J GouldRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
James M McDonnellRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
Brian J SuttonRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
Andrew J BeavilRandall Division of Cell and Molecular Biophysics, Faculty of Life Sciences &Medicine, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, U.K.
King's College London · GB

Funding

Medical Research Council G0200486Medical Research Council G0501494Medical Research Council G1000758Medical Research Council G1100090Wellcome Trust 076343Wellcome Trust 085944
6 · The paper itself

Abstract

The antibody IgE plays a central role in allergic disease mechanisms. Its effector functions are controlled through interactions between the Fc region and two principal cell surface receptors FcεRI and CD23. The interaction with FcεRI is primarily responsible for allergic sensitization and the inflammatory response, while IgE binding to CD23 is involved in the regulation of IgE synthesis and allergen transcytosis. Here we present the crystal structure of a CD23/IgE-Fc complex and conduct isothermal titration calorimetric binding studies. Two lectin-like "head" domains of CD23 bind to IgE-Fc with affinities that differ by more than an order of magnitude, but the crystal structure reveals only one head bound to one of the two identical heavy-chains in the asymmetrically bent IgE-Fc. These results highlight the subtle interplay between receptor binding sites in IgE-Fc and their affinities, the understanding of which may be exploited for therapeutic intervention in allergic disease.

Indexed as

AllergensBinding SitesB-LymphocytesHumansImmunoglobulin EImmunoglobulin Fc FragmentsProtein BindingReceptors, IgETranscytosisAllergensImmunoglobulin EImmunoglobulin Fc FragmentsReceptors, IgE

Identifiers

PMID28361904
PMCPMC5374546
OpenAlexW2598514439

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.