Evidence map›Paper›PMID 23552891›Full record

ArticleNature2013

Diverse type VI secretion phospholipases are functionally plastic antibacterial effectors.

Alistair B Russell, Michele LeRoux, Krisztina Hathazi, Danielle M Agnello, Takahiko Ishikawa, Paul A Wiggins, Sun Nyunt Wai, Joseph D Mougous

Abstract read
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 259 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
259citing papers in PubMed, 1 pooled it
30.0field-weighted citation impact, top 1% 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

259 citing papers in PubMed, 1 synthesis or guideline pooled it, 413 citations in OpenAlex.

  1. Pooled it
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  13. Article
  14. TseCurrent research in microbial sciences · 2026
    Article
  15. Virulence regulation in the fish pathogenFrontiers in cellular and infection microbiology · 2026
    Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

199 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

8 authors at 3 institutions in 2 countries.

Alistair B RussellDepartment of Microbiology, University of Washington, Seattle, Washington 98195, USA.
Michele LeRoux
Krisztina Hathazi
Danielle M Agnello
Takahiko Ishikawa
Paul A Wiggins
Sun Nyunt Wai
Joseph D Mougous
Umeå University · SEUniversity of Washington · USSeattle University · US

Funding

Variation in Human Innate ImmunityU54AI057141 · NIAID · UNIVERSITY OF WASHINGTON · PI COOKSON, BRAD T · 2003 to 2013
$102.3M
TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
Type VI secretion effectors and interbacterial competition in vivoR01AI080609 · NIAID · YALE UNIVERSITY · PI MOUGOUS, JOSEPH DAVID · 2009 to 2025
$6.7M
Linking apparatus dynamics to interbacterial intoxication by type VI secretionR21AI105268 · NIAID · UNIVERSITY OF WASHINGTON · PI MOUGOUS, JOSEPH DAVID, WIGGINS, PAUL A · 2013 to 2014
$412k
NIAID NIH HHS AI057141NIAID NIH HHS AI080609NIAID NIH HHS AI105268NIAID NIH HHS R01 AI080609NIAID NIH HHS R21 AI105268NIAID NIH HHS U54 AI057141NIGMS NIH HHS GM07270NIGMS NIH HHS T32 GM007270
6 · The paper itself

Abstract

Membranes allow the compartmentalization of biochemical processes and are therefore fundamental to life. The conservation of the cellular membrane, combined with its accessibility to secreted proteins, has made it a common target of factors mediating antagonistic interactions between diverse organisms. Here we report the discovery of a diverse superfamily of bacterial phospholipase enzymes. Within this superfamily, we defined enzymes with phospholipase A1 and A2 activity, which are common in host-cell-targeting bacterial toxins and the venoms of certain insects and reptiles. However, we find that the fundamental role of the superfamily is to mediate antagonistic bacterial interactions as effectors of the type VI secretion system (T6SS) translocation apparatus; accordingly, we name these proteins type VI lipase effectors. Our analyses indicate that PldA of Pseudomonas aeruginosa, a eukaryotic-like phospholipase D, is a member of the type VI lipase effector superfamily and the founding substrate of the haemolysin co-regulated protein secretion island II T6SS (H2-T6SS). Although previous studies have specifically implicated PldA and the H2-T6SS in pathogenesis, we uncovered a specific role for the effector and its secretory machinery in intra- and interspecies bacterial interactions. Furthermore, we find that this effector achieves its antibacterial activity by degrading phosphatidylethanolamine, the major component of bacterial membranes. The surprising finding that virulence-associated phospholipases can serve as specific antibacterial effectors suggests that interbacterial interactions are a relevant factor driving the continuing evolution of pathogenesis.

Indexed as

AntibiosisBacterial Secretion SystemsAnti-Bacterial AgentsCell MembraneEvolution, MolecularPhosphatidylethanolaminesPhospholipase DPhylogenyPseudomonas aeruginosaSpecies SpecificitySubstrate SpecificityVirulence FactorsAnti-Bacterial AgentsBacterial Secretion SystemsphosphatidylethanolaminePhosphatidylethanolaminesPhospholipase DVirulence Factors

Identifiers

PMID23552891
PMCPMC3652678
OpenAlexW2031271762

What OpenQuestion holds

Textmetadata
LicenceTDM
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.