Evidence map›Paper›PMID 40465776›Full record

ArticlePLoS pathogens2025

The Pseudomonas aeruginosa Tse4 toxin assembles ion-selective and voltage-sensitive ion channels to couple membrane depolarisation with K+ efflux.

Jessica Rojas-Palomino, Carmen Velázquez, Jon Altuna-Alvarez, Amaia González-Magaña, Maialen Zabala-Zearreta, Matthias Müller, María Queralt-Martín, Antonio Alcaraz, David Albesa-Jové

Abstract read
In one paragraph

Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. TseCurrent research in microbial sciences · 2026
    Article
  4. Article
  5. Two cysteines control Tse1 secretion by H1-T6SS in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2025
    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

9 authors.

Jessica Rojas-PalominoLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, Castellón, Spain.
Carmen VelázquezInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Leioa, Spain.
Jon Altuna-AlvarezInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Leioa, Spain.
Amaia González-MagañaInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Leioa, Spain.
Maialen Zabala-ZearretaInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Leioa, Spain.
Matthias MüllerInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Leioa, Spain.
María Queralt-MartínLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, Castellón, Spain.
Antonio AlcarazLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, Castellón, Spain.ORCID 0000-0002-7830-3189
David Albesa-JovéInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), Leioa, Spain.ORCID 0000-0003-2904-8203

Funding

Basque GovernmentGeneralitat ValencianaSpanish Ministry of Science and InnovationUniversitat Jaume I
6 · The paper itself

Abstract

Pseudomonas aeruginosa employs the Type VI secretion system (T6SS) to outcompete other bacteria in its environment. Among the effectors secreted by the T6SS of P. aeruginosa PAO1, Tse4 is known for its potent antibacterial activity. This study elucidates the molecular function of Tse4, which promotes cell depolarization in competing bacteria. Our results show that Tse4 spontaneously incorporates into lipid monolayers and forms multi-ionic channels in planar bilayers, with either ohmic conduction or diode-like rectifying currents and a preference for cations over anions. These observations allow us to propose a model of action whereby Tse4 channels couple cell depolarization with K+ efflux. These insights into Tse4's pore-forming activity enhance our understanding of bacterial competition and exemplify a finely tuned antibacterial strategy, coupling its ability to cause membrane depolarization with potassium efflux that synergises with other T6SS effectors. These results highlight the sophistication of Pseudomonas aeruginosa's competitive arsenal.

Indexed as

Bacterial ProteinsBacterial ToxinsIon ChannelsPotassiumPseudomonas aeruginosaMembrane PotentialsType VI Secretion SystemsBacterial ProteinsBacterial ToxinsIon ChannelsPotassiumType VI Secretion Systems

Identifiers

PMID40465776
PMCPMC12169545

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.