Evidence map›Paper›PMID 12379686›Full record

ArticleInfection and immunity2002

Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine.

Antje Flieger, Birgid Neumeister, Nicholas P Cianciotto

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

55 citing papers in PubMed, 106 citations in OpenAlex.

  1. Mucin stimulates the growth ofMicrobiology (Reading, England) · 2026
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  3. Journal of bacteriology · 2024
    Review
  4. Cellular cholesterol licensesMicrobial cell (Graz, Austria) · 2023
    Article
  5. Article
  6. Article
  7. Plant physiology · 2020
    Article
  8. The phospholipase A effector PlaA from Legionella pneumophila: expression, purification and crystallization.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Maintenance of vacuole integrity by bacterial pathogens.Current opinion in microbiology · 2014
    Review
  20. 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

3 authors at 2 institutions in 2 countries.

Antje FliegerDepartment of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611, Germany.
Birgid Neumeister
Nicholas P Cianciotto
Northwestern University · USUniversitätsklinikum Tübingen · DE

Funding

TYPE II SECRETION AND LEGIONELLA PNEUMOPHILA INFECTIONR01AI043987 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CIANCIOTTO, NICHOLAS P · 1999 to 2017
$4.8M
NIAID NIH HHS AI 43987NIAID NIH HHS R01 AI043987
6 · The paper itself

Abstract

We previously showed that Legionella pneumophila secretes, via its type II secretion system, phospholipase A activities that are distinguished by their specificity for certain phospholipids. In this study, we identified and characterized plaA, a gene encoding a phospholipase A that cleaves fatty acids from lysophospholipids. The plaA gene encoded a 309-amino-acid protein (PlaA) which had homology to a group of lipolytic enzymes containing the catalytic signature GDSL. In Escherichia coli, the cloned gene conferred trypsin-resistant hydrolysis of lysophosphatidylcholine and lysophosphatidylglycerol. An L. pneumophila plaA mutant was generated by allelic exchange. Although the mutant grew normally in standard buffered yeast extract broth, its culture supernatants lost greater than 80% of their ability to release fatty acids from lysophosphatidylcholine and lysophosphatidylglycerol, implying that PlaA is the major secreted lysophospholipase A of L. pneumophila. The mutant's reduced lipolytic activity was confirmed by growth on egg yolk agar and thin layer chromatography and was complemented by reintroduction of an intact copy of plaA. Overexpression of plaA completely protected L. pneumophila from the toxic effects of lysophosphatidylcholine, suggesting a role for PlaA in bacterial detoxification of lysophospholipids. The plaA mutant grew like the wild type in U937 cell macrophages and Hartmannella vermiformis amoebae, indicating that PlaA is not essential for intracellular infection of L. pneumophila. In the course of characterizing plaA, we discovered that wild-type legionellae secrete a phospholipid cholesterol acyltransferase activity, highlighting the spectrum of lipolytic enzymes produced by L. pneumophila.

Indexed as

Genes, BacterialAcyltransferasesAmino Acid SequenceBacterial ProteinsEscherichia coliHumansLegionella pneumophilaLipolysisLysophosphatidylcholinesLysophospholipaseMetalloendopeptidasesMolecular Sequence DataMutationU937 CellsAcyltransferasesBacterial Proteinsglycerophospholipid-cholesterol acyltransferaseLysophosphatidylcholinesLysophospholipaseMetalloendopeptidasespseudolysin, Pseudomonas aeruginosa

Identifiers

PMID12379686
PMCPMC130422
OpenAlexW2144216327

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.