Evidence map›Paper›PMID 16677312›Full record

ArticleMolecular microbiology2006

Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa.

Barbara I Kazmierczak, Maria B Lebron, Thomas S Murray

Abstract read
In one paragraph

Article in Molecular microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

121 citing papers in PubMed, 200 citations in OpenAlex.

  1. Article
  2. Article
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  4. Transcriptional profiling ofFrontiers in microbiology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. A Library of Promoter-Applied and environmental microbiology · 2023
    Article
  16. Article
  17. Review
  18. Controlling Biofilm Development Through Cyclic di-GMP Signaling.Advances in experimental medicine and biology · 2022
    Review
  19. Genome characterization of a uropathogenicFrontiers in cellular and infection microbiology · 2022
    Article
  20. Article

61 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Barbara I KazmierczakDepartment of Internal Medicine, Yale University School of Medicine, New Haven, CT 06520, USA. barbara.kazmierczak@yale.edu
Maria B Lebron
Thomas S Murray
Yale University · US

Funding

Research Training in Pediatric Infectious DiseasesT32AI007210 · NIAID · YALE UNIVERSITY · PI MURRAY, THOMAS SCOT, SHAPIRO, EUGENE DAVID · 1986 to 2023
$2.6M
Molecular Basis for Pseudomonas Recognition of EpitheliaR01AI054920 · NIAID · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 2004 to 2007
$1.3M
NIAID NIH HHS R01 AI054920NIAID NIH HHS T32 AI007210NIAID NIH HHS T32 AI07210
6 · The paper itself

Abstract

Type IV pili (Tfp) are polar surface structures of Pseudomonas aeruginosa required for twitching motility, biofilm formation and adherence. One protein required for the assembly of tfp is FimX, which possesses both GGDEF and EAL domains characteristic of diguanylate cyclases and phosphodiesterases respectively. In this work we demonstrate that FimX has phosphodiesterase activity towards bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP), but does not show diguanylate cyclase activity. Instead, the imperfect GGDEF domain of FimX likely serves to activate phosphodiesterase activity when bound to GTP, as has recently been described for the Caulobacter crescentus composite GGDEF-EAL protein, CC3396. Bacteria expressing FimX in which either the GGDEF or EAL domain is deleted or mutated have phenotypes indistinguishable from a DeltafimX strain, demonstrating the importance of both domains to function. Previous work has shown that FimX localizes to the bacterial pole. In this work we show that restriction of FimX to a single pole requires intact GGDEF and EAL domains. Deletion of the amino-terminal REC domain of FimX, which contains a putative polar localization signal, results in a protein that still supports intermediate levels of pilus assembly and function. RFP-FimXDeltaREC, unlike RFP-FimX, is no longer localized to the bacterial pole, while transmission electron microscopy shows that surface pili can originate from non-polar sites in this mutant. Although DeltafimX mutants show limited in vitro cytotoxicity, they are as virulent as the wild-type strain in a murine model of acute pneumonia.

Indexed as

AnimalsBacterial ProteinsCell MovementCyclic GMPEscherichia coli ProteinsFemaleFimbriae, BacterialHeLa CellsHumansMiceMice, Inbred C57BLPhosphoric Diester HydrolasesPhosphorus-Oxygen LyasesPneumonia, BacterialPoint MutationProtein Structure, TertiaryBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPdiguanylate cyclaseEscherichia coli ProteinsPhosphoric Diester HydrolasesPhosphorus-Oxygen Lyases

Identifiers

PMID16677312
PMCPMC3609419
OpenAlexW2017555326

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.