Evidence map›Paper›PMID 27288401›Full record

ArticleThe EMBO journal2016

TssA forms a gp6-like ring attached to the type VI secretion sheath.

Sara Planamente, Osman Salih, Eleni Manoli, David Albesa-Jové, Paul S Freemont, Alain Filloux

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
14.9field-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

53 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. International journal of molecular sciences · 2021
    Review
  14. Article
  15. A novel stabilization mechanism for the type VI secretion system sheath.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Article
  18. Solving the Puzzle: Connecting a HeterologousFrontiers in cellular and infection microbiology · 2020
    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.

Sara PlanamenteMRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London, UK.
Osman SalihSection of Structural Biology, Department of Medicine, Imperial College London, London, UK.
Eleni ManoliMRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London, UK.
David Albesa-JovéUnidad de Biofísica, Departamento de Bioquímica, Consejo Superior de Investigaciones Científicas - Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC-UPV/EHU) Universidad del País Vasco, Leioa, Bizkaia, Spain Structural Biology Unit, CIC bioGUNE Bizkaia Technology Park, Derio, Spain.
Paul S FreemontSection of Structural Biology, Department of Medicine, Imperial College London, London, UK p.freemont@imperial.ac.uk a.filloux@imperial.ac.uk.
Alain FillouxMRC Centre for Molecular Bacteriology and Infection (CMBI), Department of Life Sciences, Imperial College London, London, UK p.freemont@imperial.ac.uk a.filloux@imperial.ac.uk.ORCID 0000-0003-1307-0289
Imperial College London · GBConsejo Superior de Investigaciones Científicas · ES

Funding

Medical Research Council MR/J006874/1Medical Research Council MR/K001930/1Medical Research Council MR/N023250/1
6 · The paper itself

Abstract

The type VI secretion system (T6SS) is a supra-molecular bacterial complex that resembles phage tails. It is a killing machine which fires toxins into target cells upon contraction of its TssBC sheath. Here, we show that TssA1 is a T6SS component forming dodecameric ring structures whose dimensions match those of the TssBC sheath and which can accommodate the inner Hcp tube. The TssA1 ring complex binds the T6SS sheath and impacts its behaviour in vivo In the phage, the first disc of the gp18 sheath sits on a baseplate wherein gp6 is a dodecameric ring. We found remarkable sequence and structural similarities between TssA1 and gp6 C-termini, and propose that TssA1 could be a baseplate component of the T6SS Furthermore, we identified similarities between TssK1 and gp8, the former interacting with TssA1 while the latter is found in the outer radius of the gp6 ring. These observations, combined with similarities between TssF and gp6N-terminus or TssG and gp53, lead us to propose a comparative model between the phage baseplate and the T6SS.

Indexed as

Protein MultimerizationBacterial ProteinsMicroscopy, Electron, TransmissionModels, BiologicalModels, MolecularProtein BindingProtein ConformationPseudomonas aeruginosaSequence Homology, Amino AcidType VI Secretion SystemsBacterial ProteinsType VI Secretion Systemsbacteriophage baseplategp6T6SSTssAtype VI secretion system

Identifiers

PMID27288401
PMCPMC4969574
OpenAlexW2415879631

What OpenQuestion holds

Textmetadata
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.