Evidence map›Paper›PMID 29295972›Full record

ArticleNature communications2018

Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction.

Frederic Jabs, Melanie Plum, Nick S Laursen, Rasmus K Jensen, Brian Mølgaard, Michaela Miehe, Marco Mandolesi, Michèle M Rauber, Wolfgang Pfützner, Thilo Jakob and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 123 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
  3. Review
  4. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Single-Domain Antibodies-Novel Tools to Study and Treat Allergies.International journal of molecular sciences · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

13 authors at 4 institutions in 2 countries.

Frederic JabsImmunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark.
Melanie PlumImmunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark.
Nick S LaursenDepartment of Molecular Biology and Genetics, Aarhus University, 8000, Aarhus, Denmark. nsl@mbg.au.dk.
Rasmus K JensenDepartment of Molecular Biology and Genetics, Aarhus University, 8000, Aarhus, Denmark.
Brian MølgaardImmunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark.
Michaela MieheImmunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark.
Marco MandolesiImmunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark.ORCID http://orcid.org/0000-0003-2927-7831
Michèle M RauberClinical & Experimental Allergology, Department of Dermatology and Allergology, Philipps University Marburg, 35043, Marburg, Germany.
Wolfgang PfütznerClinical & Experimental Allergology, Department of Dermatology and Allergology, Philipps University Marburg, 35043, Marburg, Germany.
Thilo JakobDepartment of Dermatology and Allergology University Medical Center Giessen and Marburg, Justus-Liebig University Giessen, 35385, Giessen, Germany.
Christian MöbsClinical & Experimental Allergology, Department of Dermatology and Allergology, Philipps University Marburg, 35043, Marburg, Germany.ORCID http://orcid.org/0000-0002-5197-7669
Gregers R AndersenDepartment of Molecular Biology and Genetics, Aarhus University, 8000, Aarhus, Denmark.
Edzard SpillnerImmunological Engineering, Department of Engineering, Aarhus University, 8000, Aarhus, Denmark. e.spillner@eng.au.dk.ORCID http://orcid.org/0000-0003-0999-5254
Aarhus University · DKPhilipps University of Marburg · DEJustus-Liebig-Universität Gießen · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anti-IgE therapeutics interfere with the ability of IgE to bind to its receptors on effector cells. Here we report the crystal structure of an anti-IgE single-domain antibody in complex with an IgE Fc fragment, revealing how the antibody inhibits interactions between IgE and the two receptors FcεRI and CD23. The epitope overlaps only slightly with the FcεRI-binding site but significantly with the CD23-binding site. Solution scattering studies of the IgE Fc reveal that antibody binding induces a half-bent conformation in between the well-known bent and extended IgE Fc conformations. The antibody acts as functional homolog of CD23 and induces a closed conformation of IgE Fc incompatible with FcεRI binding. Notably the antibody displaces IgE from both CD23 and FcεRI, and abrogates allergen-mediated basophil activation and facilitated allergen binding. The inhibitory mechanism might facilitate strategies for the future development of anti-IgE therapeutics for treatment of allergic diseases.

Indexed as

Antibodies, Anti-IdiotypicBinding SitesCrystallography, X-RayEpitopesHumansImmunoglobulin EImmunoglobulin Fc FragmentsModels, MolecularProtein BindingProtein ConformationReceptors, IgESingle-Domain AntibodiesAntibodies, Anti-Idiotypicanti-IgE antibodiesEpitopesImmunoglobulin EImmunoglobulin Fc FragmentsReceptors, IgESingle-Domain Antibodies

Identifiers

PMID29295972
PMCPMC5750235
OpenAlexW2779357254

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.