Evidence map›Paper›PMID 19767432›Full record

ArticleJournal of bacteriology2009

Functional analysis of the Helicobacter pylori flagellar switch proteins.

Andrew C Lowenthal, Marla Hill, Laura K Sycuro, Khalid Mehmood, Nina R Salama, Karen M Ottemann

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 71 citations in OpenAlex.

  1. TheJournal of bacteriology · 2026
    Article
  2. Article
  3. FlgY, PflA, and PflB form a spoke-ring network in the high-torque flagellar motor ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. World journal of gastroenterology · 2021
    Review
  10. Article
  11. A Mouse Model of Helicobacter pylori Infection.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  12. Cells · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
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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 2 countries.

Andrew C LowenthalDepartment of Microbiology and Environmental Toxicology, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.
Marla Hill
Laura K Sycuro
Khalid Mehmood
Nina R Salama
Karen M Ottemann
University of California, Santa Cruz · USFred Hutch Cancer Center · USQuaid-i-Azam University · PK

Funding

GENETIC REQUIREMENTS OF HELICOBACTER PYLORI INFECTIONR01AI054423 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Nina Salama · 2004 to 2026
$9.5M
Roles for Motility in Helicobactor pylori pathogenesisR01AI050000 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI OTTEMANN, KAREN M · 2002 to 2011
$3.6M
NIAID NIH HHS AI050000NIAID NIH HHS AI054423NIAID NIH HHS R01 AI050000NIAID NIH HHS R01 AI054423
6 · The paper itself

Abstract

Helicobacter pylori uses flagellum-mediated chemotaxis to promote infection. Bacterial flagella change rotational direction by changing the state of the flagellar motor via a subcomplex referred to as the switch. Intriguingly, the H. pylori genome encodes four switch complex proteins, FliM, FliN, FliY, and FliG, instead of the more typical three of Escherichia coli or Bacillus subtilis. Our goal was to examine whether and how all four switch proteins participate in flagellation. Previous work determined that FliG was required for flagellation, and we extend those findings to show that all four switch proteins are necessary for normal numbers of flagellated cells. Furthermore, while fliY and fliN are partially redundant with each other, both are needed for wild-type levels of flagellation. We also report the isolation of an H. pylori strain containing an R54C substitution in fliM, resulting in bacteria that swim constantly and do not change direction. Along with data demonstrating that CheY-phosphate interacts with FliM, these findings suggest that FliM functions in H. pylori much as it does in other organisms.

Indexed as

Amino Acid SequenceBacterial ProteinsFlagellaGene Expression Regulation, BacterialGenetic Complementation TestHelicobacter pyloriMembrane ProteinsMicroscopy, Electron, TransmissionMolecular Sequence DataMutationProtein BindingSequence AlignmentSignal TransductionBacterial ProteinsFlig protein, BacteriaFliM protein, BacteriaFliN protein, BacteriaFliY protein, BacteriaMembrane Proteins

Identifiers

PMID19767432
PMCPMC2786559
OpenAlexW2118065377

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.