Evidence map›Paper›PMID 30282038›Full record

ArticleCell reports2018

Two Faces of CwlM, an Essential PknB Substrate, in Mycobacterium tuberculosis.

Obolbek Turapov, Francesca Forti, Baleegh Kadhim, Daniela Ghisotti, Jad Sassine, Anna Straatman-Iwanowska, Andrew R Bottrill, Patrick J Moynihan, Russell Wallis, Philippe Barthe and 4 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. An activator of a two-component system controls cell separation and intrinsic drug resistance inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026
    Review
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  11. TheFrontiers in microbiology · 2025
    Article
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  17. Identification and characterization of a novel lytic peptidoglycan transglycosylase (MltC) in Shigella dysenteriae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  18. Article
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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

14 authors at 6 institutions in 4 countries.

Obolbek TurapovLeicester Tuberculosis Research Group, Department of Infection, Immunity and Inflammation, University of Leicester, Leicester LE1 9HN, UK.
Francesca FortiDepartment of Biosciences, University of Milan, Milan 20133, Italy.
Baleegh KadhimLeicester Tuberculosis Research Group, Department of Infection, Immunity and Inflammation, University of Leicester, Leicester LE1 9HN, UK; Biology Department, College of Science, University of Al-Qadisiyah, Al-Diwaniyah 58002, Iraq.
Daniela GhisottiDepartment of Biosciences, University of Milan, Milan 20133, Italy.
Jad SassineCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4AX, UK.
Anna Straatman-IwanowskaElectron Microscopy Facility, Core Biotechnology Services, University of Leicester, Leicester LE1 7RH, UK.
Andrew R BottrillProtein Nucleic Acid Laboratory, University of Leicester, Leicester LE1 7RH, UK.
Patrick J MoynihanSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Russell WallisLeicester Tuberculosis Research Group, Department of Infection, Immunity and Inflammation, University of Leicester, Leicester LE1 9HN, UK; The Leicester Institute of Structural and Chemical Biology, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester LE1 7HB, UK.
Philippe BartheCentre de Biochimie Structurale, CNRS, INSERM, University of Montpellier, Montpellier 34090, France.
Martin Cohen-GonsaudCentre de Biochimie Structurale, CNRS, INSERM, University of Montpellier, Montpellier 34090, France.
Paul AjuhGemini Biosciences, Liverpool Science Park, Liverpool L3 5TF, UK.
Waldemar VollmerCentre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4AX, UK.
Galina V MukamolovaLeicester Tuberculosis Research Group, Department of Infection, Immunity and Inflammation, University of Leicester, Leicester LE1 9HN, UK. Electronic address: gvm4@le.ac.uk.
University of Leicester · GBNewcastle University · GBUniversity of Milan · ITCentre de Biologie Structurale · FRUniversité de Montpellier · FRUniversity of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H008586/1Biotechnology and Biological Sciences Research Council BB/P001513/1
6 · The paper itself

Abstract

Tuberculosis claims >1 million lives annually, and its causative agent Mycobacterium tuberculosis is a highly successful pathogen. Protein kinase B (PknB) is reported to be critical for mycobacterial growth. Here, we demonstrate that PknB-depleted M. tuberculosis can replicate normally and can synthesize peptidoglycan in an osmoprotective medium. Comparative phosphoproteomics of PknB-producing and PknB-depleted mycobacteria identify CwlM, an essential regulator of peptidoglycan synthesis, as a major PknB substrate. Our complementation studies of a cwlM mutant of M. tuberculosis support CwlM phosphorylation as a likely molecular basis for PknB being essential for mycobacterial growth. We demonstrate that growing mycobacteria produce two forms of CwlM: a non-phosphorylated membrane-associated form and a PknB-phosphorylated cytoplasmic form. Furthermore, we show that the partner proteins for the phosphorylated and non-phosphorylated forms of CwlM are FhaA, a fork head-associated domain protein, and MurJ, a proposed lipid II flippase, respectively. From our results, we propose a model in which CwlM potentially regulates both the biosynthesis of peptidoglycan precursors and their transport across the cytoplasmic membrane.

Indexed as

Amino Acid SequenceCell WallMycobacterium tuberculosisN-Acetylmuramoyl-L-alanine AmidasePhosphorylationProto-Oncogene Proteins c-aktN-Acetylmuramoyl-L-alanine AmidaseProto-Oncogene Proteins c-aktcellular localizationCwlMMurJMycobacterium tuberculosispeptidoglycanphosphoproteomicsprotein kinase Bserine/threonine protein kinase

Identifiers

PMID30282038
PMCPMC6180346
OpenAlexW2891069378

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.