Evidence map›Paper›PMID 33452244›Full record

ArticleNature communications2021

Pore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis.

Uday Tak, Terje Dokland, Michael Niederweis

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. 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
2.3field-weighted citation impact, top 10% 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, 44 citations in OpenAlex.

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  17. Impact of MSMEG5257 Deletion onMicroorganisms · 2024
    Article
  18. Article
  19. The C-terminus is essential for the stability of the mycobacterial channel protein MspA.Protein science : a publication of the Protein Society · 2024
    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

3 authors at 1 institution in 1 country.

Uday TakDepartment of Microbiology, University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL, 35294, USA.
Terje DoklandDepartment of Microbiology, University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL, 35294, USA.ORCID http://orcid.org/0000-0001-5655-4123
Michael NiederweisDepartment of Microbiology, University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL, 35294, USA. mnieder@uab.edu.ORCID http://orcid.org/0000-0003-4068-8092
University of Alabama at Birmingham · US

Funding

The necrosis-inducing toxin of Mycobacterium tuberculosisR01AI121354 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NIEDERWEIS, MICHAEL · 2016 to 2020
$2.5M
NIAID NIH HHS R01 AI121354
6 · The paper itself

Abstract

Mycobacterium tuberculosis secretes the tuberculosis necrotizing toxin (TNT) to kill host cells. Here, we show that the WXG100 proteins EsxE and EsxF are essential for TNT secretion. EsxE and EsxF form a water-soluble heterodimer (EsxEF) that assembles into oligomers and long filaments, binds to membranes, and forms stable membrane-spanning channels. Electron microscopy of EsxEF reveals mainly pentameric structures with a central pore. Mutations of both WXG motifs and of a GXW motif do not affect dimerization, but abolish pore formation, membrane deformation and TNT secretion. The WXG/GXW mutants are locked in conformations with altered thermostability and solvent exposure, indicating that the WXG/GXW motifs are molecular switches controlling membrane interaction and pore formation. EsxF is accessible on the bacterial cell surface, suggesting that EsxEF form an outer membrane channel for toxin export. Thus, our study reveals a protein secretion mechanism in bacteria that relies on pore formation by small WXG proteins.

Indexed as

Amino Acid MotifsBacterial ProteinsBacterial ToxinsCell MembraneHumansLipid BilayersMicroscopy, ElectronMutationMycobacterium tuberculosisPorinsProtein MultimerizationTHP-1 CellsTuberculosisType VII Secretion SystemsBacterial ProteinsBacterial ToxinsLipid BilayersPorinsType VII Secretion Systems

Identifiers

PMID33452244
PMCPMC7810871
OpenAlexW3123875335

What OpenQuestion holds

Textmetadata
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.