Evidence map›Paper›PMID 21097635›Full record

ArticleJournal of bacteriology2011

The peptidoglycan-binding protein FimV promotes assembly of the Pseudomonas aeruginosa type IV pilus secretin.

Hania Wehbi, Eder Portillo, Hanjeong Harvey, Anthony E Shimkoff, Edie M Scheurwater, P Lynne Howell, Lori L Burrows

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

52 citing papers in PubMed, 90 citations in OpenAlex.

  1. The polar landscape of bacterial pathogens and predators.Current opinion in microbiology · 2026
    Review
  2. Role of cell-associated and secretion-independent virulence factors of Pseudomonas aeruginosa in microbial keratitis and anti-virulence therapeutic strategies.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Observational
  11. Peptidoglycan deacetylation controls type IV secretion and the intracellular survival of the bacterial pathogenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020
    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 2 institutions in 1 country.

Hania WehbiDepartment of Biochemistry and Biomedical Sciences, Michael G. DeGroote Institute for Infectious Diseases Research, University McMaster University, Hamilton, ON, Canada.
Eder Portillo
Hanjeong Harvey
Anthony E Shimkoff
Edie M Scheurwater
P Lynne Howell
Lori L Burrows
McMaster University · CAHospital for Sick Children · CA

Funding

Canadian Institutes of Health Research MOP 93585
6 · The paper itself

Abstract

The Pseudomonas aeruginosa inner membrane protein FimV is among several proteins of unknown function required for type IV pilus-mediated twitching motility, arising from extension and retraction of pili from their site of assembly in the inner membrane. The pili transit the periplasm and peptidoglycan (PG) layer, ultimately exiting the cell through the PilQ secretin. Although fimV mutants are nonmotile, they are susceptible to killing by pilus-specific bacteriophage, a hallmark of retractable surface pili. Here we show that levels of recoverable surface pili were markedly decreased in fimV pilT retraction-deficient mutants compared with levels in the pilT control, demonstrating that FimV acts at the level of pilus assembly. Levels of inner membrane assembly subcomplex proteins PilM/N/O/P were decreased in fimV mutants, but supplementation of these components in trans did not restore pilus assembly or motility. Loss of FimV dramatically reduced the levels of the PilQ secretin multimer through which pili exit the cell, in part due to decreased levels of PilQ monomers, while PilF pilotin levels were unchanged. Expression of pilQ in trans in the wild type or fimV mutants increased total PilQ monomer levels but did not alter secretin multimer levels or motility. PG pulldown assays showed that the N terminus of FimV bound PG in a LysM motif-dependent manner, and a mutant with an in-frame chromosomal deletion of the LysM motif had reduced motility, secretin levels, and surface piliation. Together, our data show that FimV's role in pilus assembly is to promote secretin formation and that this function depends upon its PG-binding domain.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsFimbriae, BacterialFimbriae ProteinsGene Knockout TechniquesGenetic Complementation TestLocomotionPeptidoglycanProtein BindingProtein MultimerizationPseudomonas aeruginosaBacterial ProteinsFimbriae ProteinsPeptidoglycanpilQ protein, bacteria

Identifiers

PMID21097635
PMCPMC3019827
OpenAlexW2130561341

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.