Evidence map›Paper›PMID 32350888›Full record

ArticleThe EMBO journal2020

Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike.

Nicolas Flaugnatti, Chiara Rapisarda, Martial Rey, Solène G Beauvois, Viet Anh Nguyen, Stéphane Canaan, Eric Durand, Julia Chamot-Rooke, Eric Cascales, Rémi Fronzes and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  6. Review
  7. Molecular strategies ofFrontiers in cellular and infection microbiology · 2026
    Review
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  10. Review
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  19. Article
  20. Activity and Crystal Structure of the Adherent-InvasiveInternational journal of molecular sciences · 2023
    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

11 authors at 1 institution in 1 country.

Nicolas Flaugnatti *Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.
Chiara Rapisarda *Institut Européen de Chimie et Biologie, University of Bordeaux, Pessac, France.ORCID 0000-0002-1867-1385
Martial ReyMass Spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, CITECH, Paris, France.
Solène G BeauvoisLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.
Viet Anh NguyenLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.
Stéphane CanaanLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.ORCID 0000-0001-7478-300X
Eric DurandLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.ORCID 0000-0002-0577-8220
Julia Chamot-RookeMass Spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, CITECH, Paris, France.
Eric CascalesLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.ORCID 0000-0003-0611-9179
Rémi FronzesInstitut Européen de Chimie et Biologie, University of Bordeaux, Pessac, France.ORCID 0000-0003-3031-9824
Laure JournetLaboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université-CNRS UMR7255, Marseille, France.ORCID 0000-0002-5847-2962
Centre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche (ANR) ANR-10-BINF-03-13Agence Nationale de la Recherche (ANR) ANR-14-CE14-0006-02Agence Nationale de la Recherche (ANR) ANR-18-CE15-0013-01Aix-Marseille Université (AMU)Centre National de la Recherche Scientifique (CNRS)EC | Horizon 2020 Framework Programme (H2020) 653706Institut National de la Santé et de la Recherche Médicale (INSERM)Institut Pasteur
6 · The paper itself

Abstract

The bacterial type VI secretion system (T6SS) is a macromolecular machine that injects effectors into prokaryotic and eukaryotic cells. The mode of action of the T6SS is similar to contractile phages: the contraction of a sheath structure pushes a tube topped by a spike into target cells. Effectors are loaded onto the spike or confined into the tube. In enteroaggregative Escherichia coli, the Tle1 phospholipase binds the C-terminal extension of the VgrG trimeric spike. Here, we purify the VgrG-Tle1 complex and show that a VgrG trimer binds three Tle1 monomers and inhibits their activity. Using covalent cross-linking coupled to high-resolution mass spectrometry, we provide information on the sites of contact and further identify the requirement for a Tle1 N-terminal secretion sequence in complex formation. Finally, we report the 2.6-Å-resolution cryo-electron microscopy tri-dimensional structure of the (VgrG)

Indexed as

Escherichia coliEscherichia coli ProteinsPhospholipasesType VI Secretion SystemsEscherichia coli ProteinsPhospholipasesType VI Secretion Systemsbacterial competitionbacterial toxincryo-electron microscopyprotein secretiontype VI secretion system

Identifiers

PMID32350888
PMCPMC7265238
OpenAlexW3022597535

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.