Evidence map›Paper›PMID 30323254›Full record

ArticleNature microbiology2018

Biogenesis and structure of a type VI secretion baseplate.

Yassine Cherrak, Chiara Rapisarda, Riccardo Pellarin, Guillaume Bouvier, Benjamin Bardiaux, Fabrice Allain, Christian Malosse, Martial Rey, Julia Chamot-Rooke, Eric Cascales and 2 more

Abstract read
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In one paragraph

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 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Dissecting the antibacterial functions of the T6SS-2 cluster inApplied and environmental microbiology · 2025
    Article
  9. Science advances · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Yassine CherrakLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université - CNRS, Marseille, France.
Chiara RapisardaInstitut Européen de Chimie et Biologie, University of Bordeaux, Pessac, France.ORCID http://orcid.org/0000-0002-1867-1385
Riccardo PellarinInstitut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.
Guillaume BouvierInstitut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.
Benjamin BardiauxInstitut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.ORCID http://orcid.org/0000-0003-4014-9195
Fabrice AllainInstitut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.
Christian MalosseUSR 2000, CNRS, Institut Pasteur, Paris, France.
Martial ReyUSR 2000, CNRS, Institut Pasteur, Paris, France.
Julia Chamot-RookeUSR 2000, CNRS, Institut Pasteur, Paris, France.
Eric CascalesLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université - CNRS, Marseille, France.ORCID http://orcid.org/0000-0003-0611-9179
Rémi FronzesInstitut Européen de Chimie et Biologie, University of Bordeaux, Pessac, France. r.fronzes@iecb.u-bordeaux.fr.ORCID http://orcid.org/0000-0003-3031-9824
Eric DurandLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université - CNRS, Marseille, France. eric.durand@inserm.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To support their growth in a competitive environment and cause pathogenesis, bacteria have evolved a broad repertoire of macromolecular machineries to deliver specific effectors and toxins. Among these multiprotein complexes, the type VI secretion system (T6SS) is a contractile nanomachine that targets both prokaryotic and eukaryotic cells. The T6SS comprises two functional subcomplexes: a bacteriophage-related tail structure anchored to the cell envelope by a membrane complex. As in other contractile injection systems, the tail is composed of an inner tube wrapped by a sheath and built on the baseplate. In the T6SS, the baseplate is not only the tail assembly platform, but also docks the tail to the membrane complex and hence serves as an evolutionary adaptor. Here we define the biogenesis pathway and report the cryo-electron microscopy (cryo-EM) structure of the wedge protein complex of the T6SS from enteroaggregative Escherichia coli (EAEC). Using an integrative approach, we unveil the molecular architecture of the whole T6SS baseplate and its interaction with the tail sheath, offering detailed insights into its biogenesis and function. We discuss architectural and mechanistic similarities but also reveal key differences with the T4 phage and Mu phage baseplates.

Indexed as

BacteriophagesCell MembraneCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsModels, MolecularMultiprotein ComplexesProtein ConformationProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsType VI Secretion SystemsEscherichia coli ProteinsMultiprotein ComplexesTssF protein, E coliTssG protein, E coliTssK protein, E coliType VI Secretion Systems

Identifiers

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.