Evidence map›Paper›PMID 24961693›Full record

ArticlemBio2014

Novel components of the flagellar system in epsilonproteobacteria.

Beile Gao, Maria Lara-Tejero, Matthew Lefebre, Andrew L Goodman, Jorge E Galán

Abstract read
In one paragraph

Article in mBio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. TheProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026
    Review
  6. Impact of flagellar filament length onJournal of bacteriology · 2025
    Article
  7. FliO is an evolutionarily conserved yet diversified core component of the bacterial flagellar type III secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. 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
  10. Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Molecular model of a bacterial flagellar motorbioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Broadly conserved FlgV controls flagellar assembly andbioRxiv : the preprint server for biology · 2024
    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

5 authors.

Beile GaoDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA.
Maria Lara-TejeroDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA.
Matthew LefebreDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA.
Andrew L Goodman
Jorge E GalánDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut, USA jorge.galan@yale.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledMotility is essential for the pathogenesis of many bacterial species. Most bacteria move using flagella, which are multiprotein filaments that rotate propelled by a cell wall-anchored motor using chemical energy. Although some components of the flagellar apparatus are common to many bacterial species, recent studies have shown significant differences in the flagellar structures of different bacterial species. The molecular bases for these differences, however, are not understood. The flagella from epsilonproteobacteria, which include the bacterial pathogens Campylobacter jejuni and Helicobacter pylori, are among the most divergent. Using next-generation sequencing combined with transposon mutagenesis, we have conducted a comprehensive high-throughput genetic screen in Campylobacter jejuni, which identified several novel components of its flagellar system. Biochemical analyses detected interactions between the identified proteins and known components of the flagellar machinery, and in vivo imaging located them to the bacterial poles, where flagella assemble. Most of the identified new components are conserved within but restricted to epsilonproteobacteria. These studies provide insight into the divergent flagella of this group of bacteria and highlight the complexity of this remarkable structure, which has adapted to carry out its conserved functions in the context of widely diverse bacterial species. IMPORTANCE: Motility is essential for the normal physiology and pathogenesis of many bacterial species. Most bacteria move using flagella, which are multiprotein filaments that rotate propelled by a motor that uses chemical energy as fuel. Although some components of the flagellar apparatus are common to many bacterial species, recent studies have shown significant divergence in the flagellar structures across bacterial species. However, the molecular bases for these differences are not understood. The flagella from epsilonproteobacteria, which include the bacterial pathogens Campylobacter jejuni and Helicobacter pylori, are among the most divergent. We conducted a comprehensive genetic screen in Campylobacter jejuni and identified several novel components of the flagellar system. These studies provide important information to understand how flagella have adapted to function in the context of widely diverse sets of bacterial species and bring unique insight into the evolution and function of this remarkable bacterial organelle.

Indexed as

Bacterial ProteinsCampylobacter jejuniFlagellaHelicobacter pyloriBacterial Proteins

Identifiers

PMID24961693
PMCPMC4073491

What OpenQuestion holds

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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.