Evidence map›Paper›PMID 26109032›Full record

ArticleProteomics. Clinical applications2015

Alteration of the Helicobacter pylori membrane proteome in response to changes in environmental salt concentration.

Bradley J Voss, John T Loh, Salisha Hill, Kristie L Rose, W Hayes McDonald, Timothy L Cover

Open access · greenAbstract read
In one paragraph

Article in Proteomics. Clinical applications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.4field-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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. A Positively SelectedInfection and immunity · 2023
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  3. Article
  4. Clinical Pathogenesis, Molecular Mechanisms of Gastric Cancer Development.Current topics in microbiology and immunology · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Impact of Dietary Patterns onPathogens (Basel, Switzerland) · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Role of a Stem-Loop Structure inInfection and immunity · 2019
    Article
  16. CarcinogenicMolecular & cellular proteomics : MCP · 2019
    Article
  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

6 authors at 1 institution in 1 country.

Bradley J VossDepartment of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN, USA.
John T LohDepartment of Medicine, Vanderbilt University School of Medicine, Nashville, TN, USA.
Salisha HillProteomics Laboratory, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, USA.
Kristie L RoseProteomics Laboratory, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, USA.
W Hayes McDonaldProteomics Laboratory, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, USA.
Timothy L CoverDepartment of Pathology, Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN, USA.
Vanderbilt University · US

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Role of Iron and B-Catenin Activation in Gastric CarcinogenesisP01CA116087 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Kevin L Schey · 2009 to 2026
$27.5M
Structure-function analysis of H. pylori VacAR01AI039657 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI TIMOTHY L COVER · 1996 to 2026
$8.3M
Pathogenesis of Helicobacter pylori infectionI01BX000627 · VA · VETERANS HEALTH ADMINISTRATION · PI COVER, TIMOTHY L · 2011 to 2018
–
BLRD VA I01 BX000627NCI NIH HHS CA116087NCI NIH HHS P01 CA116087NIAID NIH HHS AI039657NIAID NIH HHS R01 AI039657NIDDK NIH HHS P30 DK058404NIDDK NIH HHS P30DK058404
6 · The paper itself

Abstract

purposeHelicobacter pylori infection and a high dietary salt intake are each risk factors for the development of gastric cancer. We hypothesize that changes in environmental salt concentrations lead to alterations in the H. pylori membrane proteome. EXPERIMENTAL

designLabel-free and iTRAQ methods were used to identify H. pylori proteins that change in abundance in response to alterations in environmental salt concentrations. In addition, we biotinylated intact bacteria that were grown under high- or low-salt conditions, and thereby analyzed salt-induced changes in the abundance of surface-exposed proteins.

resultsProteins with increased abundance in response to high salt conditions included CagA, the outer membrane protein HopQ, and fibronectin domain-containing protein HP0746. Proteins with increased abundance in response to low salt conditions included VacA, two VacA-like proteins (ImaA and FaaA), outer-membrane iron transporter FecA3, and several proteins involved in flagellar activity. Consistent with the proteomic data, bacteria grown in high salt conditions exhibited decreased motility compared to bacteria grown in lower salt conditions. CONCLUSION AND CLINICAL RELEVANCE: Alterations in the H. pylori membrane proteome in response to high salt conditions may contribute to the increased risk of gastric cancer associated with a high salt diet.

Indexed as

Dose-Response Relationship, DrugHelicobacter pyloriMembrane ProteinsMovementProteomeProteomicsSodium Chloride, DietarySpecies SpecificityMembrane ProteinsProteomeSodium Chloride, DietaryGastric cancerMass spectrometryMotilityOuter membrane proteins

Identifiers

PMID26109032
PMCPMC4690801
OpenAlexW1898522767

What OpenQuestion holds

Textmetadata
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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.