Evidence map›Paper›PMID 29222345›Full record

ArticleEMBO reports2018

Type VI secretion system sheath inter-subunit interactions modulate its contraction.

Maximilian Brackmann, Jing Wang, Marek Basler

Abstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Maximilian BrackmannFocal Area Infection Biology, Biozentrum, University of Basel, Basel, Switzerland.ORCID 0000-0003-0079-1693
Jing WangFocal Area Infection Biology, Biozentrum, University of Basel, Basel, Switzerland.ORCID 0000-0001-8218-1981
Marek BaslerFocal Area Infection Biology, Biozentrum, University of Basel, Basel, Switzerland marek.basler@unibas.ch.ORCID 0000-0001-5414-2088

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretion systems are essential for bacteria to survive and manipulate their environment. The bacterial type VI secretion system (T6SS) generates the force needed for protein translocation by the contraction of a long polymer called sheath. The sheath is a six-start helical assembly of interconnected VipA/VipB subunits. The mechanism of T6SS sheath contraction is unknown. Here, we show that elongating the N-terminal VipA linker or eliminating charge of a specific VipB residue abolishes sheath contraction and delivery of effectors into target cells. Mass spectrometry analysis identified the inner tube protein Hcp, spike protein VgrG, and other components of the T6SS baseplate significantly enriched in samples of the stable non-contractile sheaths. The ability to lock the T6SS in the pre-firing state opens new possibilities for understanding its mode of action.

Indexed as

Bacterial Physiological PhenomenaType VI Secretion SystemsBacteriaBacterial ProteinsMass SpectrometryMicrobial ViabilityMicroscopy, FluorescenceMutationPhenotypeVirulence FactorsBacterial ProteinsType VI Secretion SystemsVirulence Factorscontractile tailsmicrobiologyphagestype VI secretion system

Identifiers

PMID29222345
PMCPMC5797969

What OpenQuestion holds

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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.