Evidence map›Paper›PMID 36335275›Full record

ArticleCommunications biology2022

The P. aeruginosa effector Tse5 forms membrane pores disrupting the membrane potential of intoxicated bacteria.

Amaia González-Magaña, Jon Altuna, María Queralt-Martín, Eneko Largo, Carmen Velázquez, Itxaso Montánchez, Patricia Bernal, Antonio Alcaraz, David Albesa-Jové

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. 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
6.6field-weighted citation impact, top 3% 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, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Two cysteines control Tse1 secretion by H1-T6SS in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024
    Article
  17. Article
  18. Defining Membrane Protein Topology Using pho-lac Reporter Fusions.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  19. Article
  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

9 authors at 4 institutions in 1 country.

Amaia González-Magaña *Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, Instituto Biofisika (CSIC, UPV/EHU), University of the Basque Country, 48940, Leioa, Spain.
Jon Altuna *Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, Instituto Biofisika (CSIC, UPV/EHU), University of the Basque Country, 48940, Leioa, Spain.
María Queralt-MartínLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, 12071, Castellón, Spain.ORCID 0000-0002-0644-6746
Eneko LargoFundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, Instituto Biofisika (CSIC, UPV/EHU), University of the Basque Country, 48940, Leioa, Spain.ORCID 0000-0003-4400-3521
Carmen VelázquezFundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, Instituto Biofisika (CSIC, UPV/EHU), University of the Basque Country, 48940, Leioa, Spain.
Itxaso MontánchezDepartamento de Inmunología, Microbiología y Parasitología, University of the Basque Country, 48940, Leioa, Spain.
Patricia BernalDepartamento de Microbiología, Facultad de Biología, Universidad de Sevilla, 41012, Sevilla, Spain.ORCID 0000-0002-6228-0496
Antonio AlcarazLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, 12071, Castellón, Spain.ORCID 0000-0002-7830-3189
David Albesa-JovéFundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB) and Departamento de Bioquímica y Biología Molecular, Instituto Biofisika (CSIC, UPV/EHU), University of the Basque Country, 48940, Leioa, Spain. david.albesa@ehu.eus.ORCID 0000-0003-2904-8203
University of the Basque Country · ESUniversitat Jaume I · ESIkerbasque · ESUniversidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type VI secretion system (T6SS) of Pseudomonas aeruginosa injects effector proteins into neighbouring competitors and host cells, providing a fitness advantage that allows this opportunistic nosocomial pathogen to persist and prevail during the onset of infections. However, despite the high clinical relevance of P. aeruginosa, the identity and mode of action of most P. aeruginosa T6SS-dependent effectors remain to be discovered. Here, we report the molecular mechanism of Tse5-CT, the toxic auto-proteolytic product of the P. aeruginosa T6SS exported effector Tse5. Our results demonstrate that Tse5-CT is a pore-forming toxin that can transport ions across the membrane, causing membrane depolarisation and bacterial death. The membrane potential regulates a wide range of essential cellular functions; therefore, membrane depolarisation is an efficient strategy to compete with other microorganisms in polymicrobial environments.

Indexed as

Pseudomonas aeruginosaType VI Secretion SystemsBacterial ProteinsMembrane PotentialsBacterial ProteinsType VI Secretion Systems

Identifiers

PMID36335275
PMCPMC9637101
OpenAlexW4308292294

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.