Evidence map›Paper›PMID 15123808›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Helicobacter pylori interacts with the human single-domain trefoil protein TFF1.

Marguerite Clyne, Paul Dillon, Stephen Daly, Richard O'Kennedy, Felicity E B May, Bruce R Westley, Brendan Drumm

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

35 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. TFF1 Induces Aggregation and Reduces Motility ofInternational journal of molecular sciences · 2021
    Article
  11. Review
  12. Article
  13. The Interaction ofInternational journal of molecular sciences · 2019
    Review
  14. Article
  15. Binding ofMicroorganisms · 2018
    Article
  16. Review
  17. Mouse models for gastric cancer: Matching models to biological questions.Journal of gastroenterology and hepatology · 2016
    Review
  18. Article
  19. Article
  20. 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

7 authors at 5 institutions in 2 countries.

Marguerite ClyneChildren's Research Centre, Our Lady's Hospital for Sick Children, Dublin 12, Ireland. marguerite.clyne@ucd.ie
Paul Dillon
Stephen Daly
Richard O'Kennedy
Felicity E B May
Bruce R Westley
Brendan Drumm
Molecular Medicine Ireland · IEUniversity College Dublin · IEChildren's Health Ireland at Crumlin · IEDublin City University · IERoyal Victoria Infirmary · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 could explain the tropism of this bacteria for gastric tissue. Recombinant human TFF1 expressed in Escherichia coli was purified by affinity chromatography, ion-exchange chromatography, and gel filtration. Binding of H. pylori was assessed by using flow cytometry and the BIAcore system, which allows real-time monitoring of molecular interactions. In flow cytometry, H. pylori bound to the TFF1 dimer, but Campylobacter jejuni strains and the laboratory strain of E. coli, HB101, did not bind. When the BIAcore system was used, H. pylori bound strongly to TFF1-coated dextran chips compared with uncoated chips. Binding was inhibited by a TFF1 monoclonal antibody and by soluble TFF1. H. pylori bound to porcine gastric mucin only if it was pretreated with TFF1. In conclusion, H. pylori interacts avidly with the dimeric form of TFF1, and this interaction enables binding to gastric mucin, suggesting that TFF1 may act as a receptor for the organism in vivo. This interaction may underline the previously unexplained tropism of this organism for gastric tissue and its colocalization with the gastric mucin MUC5AC.

Indexed as

DimerizationGastric MucosaHelicobacter pyloriHumansLewis Blood Group AntigensProteinsRecombinant ProteinsSurface Plasmon ResonanceTrefoil Factor-1Tumor Suppressor ProteinsLewis Blood Group AntigensProteinsRecombinant ProteinsTFF1 protein, humanTrefoil Factor-1Tumor Suppressor Proteins

Identifiers

PMID15123808
PMCPMC409932
OpenAlexW2100172636

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.