Evidence map›Paper›PMID 23437241›Full record

ArticlePloS one2013

LegC3, an effector protein from Legionella pneumophila, inhibits homotypic yeast vacuole fusion in vivo and in vitro.

Terry L Bennett, Shannon M Kraft, Barbara J Reaves, Joji Mima, Kevin M O'Brien, Vincent J Starai

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Knowledge to Predict Pathogens:Microorganisms · 2022
    Review
  4. Article
  5. Article
  6. Affecting the Effectors: Regulation ofPathogens (Basel, Switzerland) · 2021
    Review
  7. Review
  8. Review
  9. TheFrontiers in plant science · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Direct targeting of membrane fusion by SNARE mimicry: Convergent evolution of Legionella effectors.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Space: A Final Frontier for Vacuolar Pathogens.Traffic (Copenhagen, Denmark) · 2016
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors at 2 institutions in 2 countries.

Terry L BennettDepartment of Microbiology University of Georgia, Athens, GA, USA.
Shannon M Kraft
Barbara J Reaves
Joji Mima
Kevin M O'Brien
Vincent J Starai
University of Georgia · USOsaka University · JP

Funding

Bacterial inhibitors of eukaryotic membrane fusionR01AI100913 · NIAID · UNIVERSITY OF GEORGIA · PI STARAI, VINCENT JOSEPH · 2013 to 2017
$1.7M
NIAID NIH HHS R01 AI100913
6 · The paper itself

Abstract

During infection, the intracellular pathogenic bacterium Legionella pneumophila causes an extensive remodeling of host membrane trafficking pathways, both in the construction of a replication-competent vacuole comprised of ER-derived vesicles and plasma membrane components, and in the inhibition of normal phagosome:endosome/lysosome fusion pathways. Here, we identify the LegC3 secreted effector protein from L. pneumophila as able to inhibit a SNARE- and Rab GTPase-dependent membrane fusion pathway in vitro, the homotypic fusion of yeast vacuoles (lysosomes). This vacuole fusion inhibition appeared to be specific, as similar secreted coiled-coiled domain containing proteins from L. pneumophila, LegC7/YlfA and LegC2/YlfB, did not inhibit vacuole fusion. The LegC3-mediated fusion inhibition was reversible by a yeast cytosolic extract, as well as by a purified soluble SNARE, Vam7p. LegC3 blocked the formation of trans-SNARE complexes during vacuole fusion, although we did not detect a direct interaction of LegC3 with the vacuolar SNARE protein complexes required for fusion. Additionally, LegC3 was incapable of inhibiting a defined synthetic model of vacuolar SNARE-driven membrane fusion, further suggesting that LegC3 does not directly inhibit the activity of vacuolar SNAREs, HOPS complex, or Sec17p/18p during membrane fusion. LegC3 is likely utilized by Legionella to modulate eukaryotic membrane fusion events during pathogenesis.

Indexed as

Bacterial ProteinsGene ExpressionLegionella pneumophilaLysosomesMembrane FusionMutationProtein BindingProtein Interaction Domains and MotifsSaccharomyces cerevisiaeSNARE ProteinsVacuolesBacterial ProteinsSNARE Proteins

Identifiers

PMID23437241
PMCPMC3577674
OpenAlexW2076081302

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.