Evidence map›Paper›PMID 21042406›Full record

ArticlePloS one2010

Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa.

Yun Kang, Jan Zarzycki-Siek, Chad B Walton, Michael H Norris, Tung T Hoang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. 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
1.2field-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, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of systematic and evolutionary microbiology · 2026
    Article
  4. Review
  5. mLife · 2025
    Article
  6. Article
  7. The fatty acid synthesis geneMicrobiology spectrum · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Bacterial acquisition of host fatty acids has far-reaching implications on virulence.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  12. The puzzle of two tandem acyl-CoA ligases ofApplied and environmental microbiology · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. The great divide: rhamnolipids mediate separation betweenFrontiers in cellular and infection microbiology · 2023
    Article
  17. Article
  18. Article
  19. Review
  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

5 authors at 1 institution in 1 country.

Yun KangDepartment of Molecular Biosciences and Bioengineering, University of Hawaii at Manoa, Honolulu, Hawaii, United States of America.
Jan Zarzycki-Siek
Chad B Walton
Michael H Norris
Tung T Hoang
University of Hawaiʻi at Mānoa · US

Funding

WORLDWIDE EPIDEMIOLOGY &EPIZOOTIOLOGY OF HANTAVIRUSG12RR003061 · NCRR · UNIVERSITY OF HAWAII AT MANOA · PI NERURKAR, VIVEK RAMCHANDRA · 1986 to 2011
$32.3M
Regulation of Fatty Acid Biosynthesis and Degradation in Pseudomonas aeruginosaR21AI073816 · NIAID · UNIVERSITY OF HAWAII AT MANOA · PI HOANG, TUNG T · 2007 to 2008
$377k
NCRR NIH HHS G12 RR003061NCRR NIH HHS G12RR003061NCRR NIH HHS P20RR01872NIAID NIH HHS R21 AI073816NIAID NIH HHS R21-AI073816
6 · The paper itself

Abstract

A close interconnection between nutrient metabolism and virulence factor expression contributes to the pathophysiology of Pseudomonas aeruginosa as a successful pathogen. P. aeruginosa fatty acid (FA) degradation is complicated with multiple acyl-CoA synthetase homologs (FadDs) expressed in vivo in lung tissue during cystic fibrosis infections. The promoters of two genetically linked P. aeruginosa fadD genes (fadD1 and fadD2) were mapped and northern blot analysis indicated they could exist on two different transcripts. These FadDs contain ATP/AMP signature and FA-binding motifs highly homologous to those of the Escherichia coli FadD. Upon introduction into an E. coli fadD(-)/fadR(-) double mutant, both P. aeruginosa fadDs functionally complemented the E. coli fadD(-)/fadR(-) mutant, allowing degradation of different chain-length FAs. Chromosomal mutagenesis, growth analysis, induction studies, and determination of kinetic parameters suggested that FadD1 has a substrate preference for long-chain FAs while FadD2 prefers shorter-chain FAs. When compared to the wild type strain, the fadD2 mutant exhibited decreased production of lipase, protease, rhamnolipid and phospholipase, and retardation of both swimming and swarming motilities. Interestingly, fadD1 mutant showed only increased swarming motility. Growth analysis of the fadD mutants showed noticeable deficiencies in utilizing FAs and phosphatidylcholine (major components of lung surfactant) as the sole carbon source. This defect translated into decreased in vivo fitness of P. aeruginosa in a BALB/c mouse lung infection model, supporting the role of lipids as a significant nutrient source for this bacterium in vivo.

Indexed as

Amino Acid SequenceBase SequenceCoenzyme A LigasesDNA, BacterialEscherichia coliFatty AcidsHydrolysisKineticsMolecular Sequence DataMutationPseudomonas aeruginosaRNA, MessengerSequence Homology, Amino AcidSubstrate SpecificityVirulenceCoenzyme A LigasesDNA, BacterialFatty AcidsRNA, Messenger

Identifiers

PMID21042406
PMCPMC2958839
OpenAlexW2063009041

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.