Evidence map›Paper›PMID 21212271›Full record

ArticleThe Journal of biological chemistry2011

A novel inhibitory domain of Helicobacter pylori protein CagA reduces CagA effects on host cell biology.

Christiane Pelz, Sylvia Steininger, Claudia Weiss, Fabian Coscia, Roger Vogelmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Science advances · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Helicobacter pylori in gastric carcinogenesis: mechanisms.Gastroenterology clinics of North America · 2013
    Review
  8. Article
  9. Article
  10. Article
  11. Structural insights into Helicobacter pylori oncoprotein CagA interaction with β1 integrin.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Article
  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Christiane PelzSecond Department of Internal Medicine, Klinikum rechts der Isar, Technical University Munich, 81675 Munich, Germany.
Sylvia Steininger
Claudia Weiss
Fabian Coscia
Roger Vogelmann
Klinikum rechts der Isar · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Helicobacter pylori protein CagA (cytotoxin-associated gene A) is associated with an increased risk for gastric cancer formation. After attachment to epithelial cells, the bacteria inject CagA via a type IV secretion apparatus into host cells, where it exerts its biological activity. Host cell responses to intracellular CagA have been linked exclusively to signaling motifs in the C terminus of the CagA protein. Little is known about the functional role of the remaining CagA protein. Using transgenic expression of CagA mutants in epithelial cells, we were able to identify a novel CagA inhibitory domain at the N terminus consisting of the first 200 amino acids. This domain localizes to cell-cell contacts and increases the rate and strength of cell-cell adhesion in epithelial cells. Thus, it compensates for the loss of cell-cell adhesion induced by the C terminus of the CagA protein. Consistent with its stabilizing role on cell-cell adhesion, the CagA N terminus domain reduces the CagA-induced β-catenin transcriptional activity in the nucleus. Furthermore, it inhibits apical surface constriction and cell elongations, host cell phenotypes induced by the C terminus in polarized epithelia. Therefore, our study suggests that CagA contains an intrinsic inhibitory domain that reduces host cell responses to CagA, which have been associated with the formation of cancer.

Indexed as

Host-Pathogen InteractionsSignal TransductionAmino Acid MotifsAnimalsAntigens, BacterialBacterial Proteinsbeta CateninCell LineCell NucleusDogsEpithelial CellsHelicobacter pyloriMutationProtein Structure, TertiaryRisk FactorsStomach NeoplasmsAntigens, BacterialBacterial Proteinsbeta CatenincagA protein, Helicobacter pylori

Identifiers

PMID21212271
PMCPMC3059056
OpenAlexW2002619010

What OpenQuestion holds

Textmetadata
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.