Evidence map›Paper›PMID 30275513›Full record

ArticleNature microbiology2018

In vivo TssA proximity labelling during type VI secretion biogenesis reveals TagA as a protein that stops and holds the sheath.

Yoann G Santin, Thierry Doan, Régine Lebrun, Leon Espinosa, Laure Journet, Eric Cascales

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Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. The multifunctional type VI secretion system ofApplied and environmental microbiology · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. BioID in Bacteria: Selection of a Suitable Biotin Ligase for Proxeome Mapping.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  14. Article
  15. Article
  16. Identification of Protein Partners by APEX2 Proximity Labeling.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  17. Review
  18. Article
  19. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Yoann G SantinLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université, Marseille, France.
Thierry DoanLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0002-5909-4289
Régine LebrunPlateforme Protéomique, Marseille Protéomique (MaP), Institut de Microbiologie de la Méditerranée, CNRS, Aix-Marseille Université, Marseille, France.
Leon EspinosaPlateforme de biophotonique appliquée à la microbiologie, Laboratoire de Chimie Bactérienne, Institut de Microbiologie de la Méditerranée, CNRS UMR7283, Aix-Marseille Université, Marseille, France.
Laure JournetLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0002-5847-2962
Eric CascalesLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, CNRS UMR7255, Aix-Marseille Université, Marseille, France. cascales@imm.cnrs.fr.ORCID http://orcid.org/0000-0003-0611-9179

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type VI secretion system (T6SS) is a multiprotein weapon used by bacteria to destroy competitor cells. The T6SS contractile sheath wraps an effector-loaded syringe that is injected into the target cell. This tail structure assembles onto the baseplate that is docked to the membrane complex. In enteroaggregative Escherichia coli, TssA plays a central role at each stage of the T6SS assembly pathway by stabilizing the baseplate and coordinating the polymerization of the tail. Here we adapted an assay based on APEX2-dependent biotinylation to identify the proximity partners of TssA in vivo. By using stage-blocking mutations, we define the temporal contacts of TssA during T6SS biogenesis. This proteomic mapping approach also revealed an additional partner of TssA, TagA. We show that TagA is a cytosolic protein tightly associated with the membrane. Analyses of sheath dynamics further demonstrate that TagA captures the distal end of the sheath to stop its polymerization and to maintain it under the extended conformation.

Indexed as

CytoplasmEscherichia coliEscherichia coli ProteinsMetalloendopeptidasesModels, MolecularPolymerizationProtein ConformationProtein Interaction MapsProteomicsType VI Secretion SystemsEscherichia coli ProteinsMetalloendopeptidasesStcE protein, E coliTssA protein, E coliType VI Secretion Systems

Identifiers

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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.