Evidence map›Paper›PMID 38016939›Full record

ArticleNature communications2023

Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.

Amaia González-Magaña, Igor Tascón, Jon Altuna-Alvarez, María Queralt-Martín, Jake Colautti, Carmen Velázquez, Maialen Zabala, Jessica Rojas-Palomino, Marité Cárdenas, Antonio Alcaraz and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Journal of oral microbiology · 2025
    Article
  14. Article
  15. mBio · 2024
    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

13 authors.

Amaia González-Magaña *Instituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain.ORCID 0000-0002-6007-8390
Igor Tascón *Instituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain.ORCID 0000-0003-2526-6238
Jon Altuna-AlvarezInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain.ORCID 0000-0002-4993-7991
María Queralt-MartínLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, 12071, Castellón, Spain.ORCID 0000-0002-0644-6746
Jake ColauttiDepartment of Biochemistry and Biomedical Sciences, Michael DeGroote Institute for Infectious Disease Research, and David Braley Centre for Antibiotic Discovery, McMaster University, Hamilton, Canada.
Carmen VelázquezInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain.ORCID 0000-0002-0179-5533
Maialen ZabalaInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain.
Jessica Rojas-PalominoLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, 12071, Castellón, Spain.ORCID 0000-0003-4962-1193
Marité CárdenasInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain.ORCID 0000-0003-0392-3540
Antonio AlcarazLaboratory of Molecular Biophysics, Department of Physics, University Jaume I, 12071, Castellón, Spain.ORCID 0000-0002-7830-3189
John C WhitneyDepartment of Biochemistry and Biomedical Sciences, Michael DeGroote Institute for Infectious Disease Research, and David Braley Centre for Antibiotic Discovery, McMaster University, Hamilton, Canada.ORCID 0000-0002-4517-8836
Iban Ubarretxena-BelandiaInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain. ivan.ubarrechena@ehu.eus.ORCID 0000-0003-4082-4349
David Albesa-JovéInstituto Biofisika (CSIC, UPV/EHU), Fundación Biofísica Bizkaia/Biofisika Bizkaia Fundazioa (FBB), 48940, Leioa, Spain. david.albesa@ehu.eus.ORCID 0000-0003-2904-8203

Funding

Wellcome Trust
6 · The paper itself

Abstract

Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot (Rhs) proteins represent a widespread example of toxin polymorphism. Here, we present the 2.45 Å cryo-electron microscopy structure of Tse5, an Rhs protein central to Pseudomonas aeruginosa type VI secretion system-mediated bacterial competition. This structural insight, coupled with an extensive array of biophysical and genetic investigations, unravels the multifaceted functional mechanisms of Tse5. The data suggest that interfacial Tse5-membrane binding delivers its encapsulated pore-forming toxin fragment to the target bacterial membrane, where it assembles pores that cause cell depolarisation and, ultimately, bacterial death.

Indexed as

Bacterial ToxinsDermatitisBacterial ProteinsBase SequenceCell MembraneCryoelectron MicroscopyHumansMembranesBacterial ProteinsBacterial Toxins

Identifiers

PMID38016939
PMCPMC10684867

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.