Evidence map›Paper›PMID 42336839›Full record

ArticleNature communications2026

A Type VII-secreted toxin enables inter-mycobacterial competition.

Samuel T Benedict, Kieran Bowran, Eunice K E Lee, Jean-Lou Reyre, Huda Ahmad, Aaron Franklin, Nicole A Mietrach, Cheng-Ruei Han, Jia Mun Chan, Abigail J Layton and 11 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

21 authors.

Samuel T BenedictSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0000-0002-8941-3703
Kieran BowranNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Eunice K E LeeNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Jean-Lou ReyreNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Huda AhmadSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
Aaron FranklinSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0009-0006-0472-5895
Nicole A MietrachNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Cheng-Ruei HanInstitute of Biological Chemistry, Academia Sinica, Nangang, Taipei, Taiwan.
Jia Mun ChanNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Abigail J LaytonSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0009-0003-2785-8971
Emmanuele SeveriNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.ORCID http://orcid.org/0000-0001-9750-5539
Eleanor R BoardmanNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.ORCID http://orcid.org/0000-0001-7439-8304
Kamilla AnochshenkoSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
Gregory GoudgeSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.
Simon G CaultonSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0000-0001-7509-9728
Todd L LowaryInstitute of Biological Chemistry, Academia Sinica, Nangang, Taipei, Taiwan.ORCID http://orcid.org/0000-0002-8331-8211
Andrew L LoveringSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0000-0002-1856-7975
Manuel BanzhafNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Elisabeth C LoweNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Tracy PalmerNewcastle University Biosciences Institute, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK. tracy.palmer@newcastle.ac.uk.ORCID http://orcid.org/0000-0001-9043-2592
Patrick J MoynihanSchool of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK. pmoyniha@uwo.ca.ORCID http://orcid.org/0000-0003-4182-6223

Funding

Academy of Medical Sciences SBF005/1112EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 101167433RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S010122/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X006298/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X00841X/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/X016749/1Wellcome TrustWellcome Trust (Wellcome) 224151/Z/21/ZWellcome Trust (Wellcome) 226644/Z/22/Z
6 · The paper itself

Abstract

Most bacteria have evolved mechanisms to compete with other bacteria, often through the specialised secretion of proteinaceous toxins. However, mycobacteria have not previously been reported to engage in this form of competition. The thick and unusual mycobacterial cell wall, comprised of peptidoglycan, arabinogalactan and mycolic acids, is generally thought to be highly protective to these bacteria. Here, we show that some mycobacteria can use endo-D-arabinanases of the GH183 family for inter-bacterial competition. These microorganisms secrete an endo-D-arabinanase effector via the type VII secretion system (T7SS) that cleaves the arabinogalactan layer of the mycobacterial cell envelope. We describe the molecular basis for this activity using structural biology and biochemistry, and identify a protein family that protects the bacterium from the activity of this toxin. The widespread presence of genes potentially encoding similar T7SS-secreted toxins in the Mycobacteriales suggests extensive inter-mycobacterial competition.

Indexed as

Bacterial ProteinsBacterial ToxinsMycobacteriumType VII Secretion SystemsCell WallGalactansMycobacterium smegmatisPeptidoglycanarabinogalactanBacterial ProteinsBacterial ToxinsGalactansPeptidoglycanType VII Secretion Systems

Identifiers

PMID42336839
PMCPMC13444075

What OpenQuestion holds

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Registered trials

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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.