Evidence map›Paper›PMID 31199818›Full record

ArticlePloS one2019

Immunoglobulin G structure and rheumatoid factor epitopes.

Sheila Lefoli Maibom-Thomsen, Nicole Hartwig Trier, Bettina Eide Holm, Kirsten Beth Hansen, Morten Ib Rasmussen, Anna Chailyan, Paolo Marcatili, Peter Højrup, Gunnar Houen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

  1. Molecular insights into phytochemicals exhibiting anti-arthritic activity: systematic review : John Di Battista.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2021
    Pooled it
  2. Trial
  3. Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026
    Article
  4. Review
  5. Ozoralizumab, a trivalent anti-TNFα NANOBODYFrontiers in immunology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Redox Pathogenesis in Rheumatic Diseases.ACR open rheumatology · 2024
    Review
  14. Article
  15. Next-Generation Anti-TNFα Agents: The Example of Ozoralizumab.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2024
    Review
  16. Review
  17. Review
  18. Article
  19. Review
  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

9 authors at 3 institutions in 1 country.

Sheila Lefoli Maibom-ThomsenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Nicole Hartwig TrierDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Bettina Eide HolmDepartment of Autoimmunology, Statens Serum Institut, Copenhagen, Denmark.
Kirsten Beth HansenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Morten Ib RasmussenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Anna ChailyanDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Paolo MarcatiliDepartment of Bioinformatics, Technical University of Denmark, Kongens Lyngby, Denmark.
Peter HøjrupDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Gunnar HouenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.ORCID 0000-0002-5948-4156
Statens Serum Institut · DKUniversity of Southern Denmark · DKTechnical University of Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies are important for immunity and exist in several classes (IgM, IgD, IgA, IgG, IgE). They are composed of symmetric dimeric molecules with two antigen binding regions (Fab) and a constant part (Fc), usually depicted as Y-shaped molecules. Rheumatoid factors found in patients with rheumatoid arthritis are autoantibodies binding to IgG and paradoxically appear to circulate in blood alongside with their antigen (IgG) without reacting with it. Here, it is shown that rheumatoid factors do not react with native IgG in solution, and that their epitopes only become accessible upon certain physico-chemical treatments (e.g. heat treatment at 57 °C), by physical adsorption on a hydrophobic surface or by antigen binding. Moreover, chemical cross-linking in combination with mass spectrometry showed that the native state of IgG is a compact (closed) form and that the Fab parts of IgG shield the Fc region and thereby control access of rheumatoid factors and presumably also some effector functions. It can be inferred that antibody binding to pathogen surfaces induces a conformational change, which exposes the Fc part with its effector sites and rheumatoid factor epitopes. This has strong implications for understanding antibody structure and physiology and necessitates a conceptual reformulation of IgG models.

Indexed as

Arthritis, RheumatoidEpitopesHumansImmunoglobulin Fc FragmentsImmunoglobulin GProtein Structure, QuaternaryRheumatoid FactorStructure-Activity RelationshipEpitopesImmunoglobulin Fc FragmentsImmunoglobulin GRheumatoid Factor

Identifiers

PMID31199818
PMCPMC6568389
OpenAlexW2952845819

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.