Evidence map›Paper›PMID 27146306›Full record

ArticleScientific reports2016

Gluten-specific antibodies of celiac disease gut plasma cells recognize long proteolytic fragments that typically harbor T-cell epitopes.

Siri Dørum, Øyvind Steinsbø, Elin Bergseng, Magnus Ø Arntzen, Gustavo A de Souza, Ludvig M Sollid

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Trial
  2. Review
  3. Barley based gluten free beer - A blessing or an uncontrollable risk?Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2024
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. T Cells in Celiac Disease.Journal of immunology (Baltimore, Md. : 1950) · 2017
    Review
  14. Review
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

6 authors at 3 institutions in 1 country.

Siri DørumCentre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital - Rikshospitalet, 0424 Oslo, Norway.
Øyvind SteinsbøCentre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital - Rikshospitalet, 0424 Oslo, Norway.
Elin BergsengCentre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital - Rikshospitalet, 0424 Oslo, Norway.
Magnus Ø ArntzenNorwegian University of Life Sciences, NMBU, Department of Chemistry, Biotechnology and Food Science, 1432 Aas, Norway.
Gustavo A de SouzaCentre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital - Rikshospitalet, 0424 Oslo, Norway.
Ludvig M SollidCentre for Immune Regulation and Department of Immunology, University of Oslo and Oslo University Hospital - Rikshospitalet, 0424 Oslo, Norway.
University of Oslo · NOOslo University Hospital · NONorwegian University of Life Sciences · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study aimed to identify proteolytic fragments of gluten proteins recognized by recombinant IgG1 monoclonal antibodies generated from single IgA plasma cells of celiac disease lesions. Peptides bound by monoclonal antibodies in complex gut-enzyme digests of gluten treated with the deamidating enzyme transglutaminase 2, were identified by mass spectrometry after antibody pull-down with protein G beads. The antibody bound peptides were long deamidated peptide fragments that contained the substrate recognition sequence of transglutaminase 2. Characteristically, the fragments contained epitopes with the sequence QPEQPFP and variants thereof in multiple copies, and they typically also harbored many different gluten T-cell epitopes. In the pull-down setting where antibodies were immobilized on a solid phase, peptide fragments with multivalent display of epitopes were targeted. This scenario resembles the situation of the B-cell receptor on the surface of B cells. Conceivably, B cells of celiac disease patients select gluten epitopes that are repeated multiple times in long peptide fragments generated by gut digestive enzymes. As the fragments also contain many different T-cell epitopes, this will lead to generation of strong antibody responses by effective presentation of several distinct T-cell epitopes and establishment of T-cell help to B cells.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalB-LymphocytesCeliac DiseaseEpitopes, T-LymphocyteGliadinGlutensGTP-Binding ProteinsHumansIntestinal MucosaIntestinesMass SpectrometryPeptide FragmentsPlasma CellsProtein Glutamine gamma Glutamyltransferase 2ProteolysisAntibodies, MonoclonalEpitopes, T-LymphocyteGliadinGlutensGTP-Binding ProteinsPeptide FragmentsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID27146306
PMCPMC4857092
OpenAlexW2347023895

What OpenQuestion holds

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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.