Evidence map›Paper›PMID 31201321›Full record

ArticleNature communications2019

The hydrolase LpqI primes mycobacterial peptidoglycan recycling.

Patrick J Moynihan, Ian T Cadby, Natacha Veerapen, Monika Jankute, Marialuisa Crosatti, Galina V Mukamolova, Andrew L Lovering, Gurdyal S Besra

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Patrick J MoynihanInstitute of Microbiology and Infection, School of Biological Sciences, University of Birmingham, Birmingham, B15 2TT, UK. p.j.moynihan@bham.ac.uk.ORCID http://orcid.org/0000-0003-4182-6223
Ian T CadbyInstitute of Microbiology and Infection, School of Biological Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Natacha VeerapenInstitute of Microbiology and Infection, School of Biological Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Monika JankuteInstitute of Microbiology and Infection, School of Biological Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Marialuisa CrosattiLeicester Tuberculosis Research group, Department of Respiratory Sciences, University of Leicester, Leicester, LE1 9HN, UK.
Galina V MukamolovaLeicester Tuberculosis Research group, Department of Respiratory Sciences, University of Leicester, Leicester, LE1 9HN, UK.
Andrew L LoveringInstitute of Microbiology and Infection, School of Biological Sciences, University of Birmingham, Birmingham, B15 2TT, UK.
Gurdyal S BesraInstitute of Microbiology and Infection, School of Biological Sciences, University of Birmingham, Birmingham, B15 2TT, UK.ORCID http://orcid.org/0000-0002-5605-0395
University of Birmingham · GBUniversity of Leicester · GB

Funding

Medical Research Council MR/K012118/1Medical Research Council MR/S000542/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/J015229/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/N011945/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/P001513/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S010122/1RCUK | MRC | Medical Research Foundation MR/S000542/1
6 · The paper itself

Abstract

Growth and division by most bacteria requires remodelling and cleavage of their cell wall. A byproduct of this process is the generation of free peptidoglycan (PG) fragments known as muropeptides, which are recycled in many model organisms. Bacteria and hosts can harness the unique nature of muropeptides as a signal for cell wall damage and infection, respectively. Despite this critical role for muropeptides, it has long been thought that pathogenic mycobacteria such as Mycobacterium tuberculosis do not recycle their PG. Herein we show that M. tuberculosis and Mycobacterium bovis BCG are able to recycle components of their PG. We demonstrate that the core mycobacterial gene lpqI, encodes an authentic NagZ β-N-acetylglucosaminidase and that it is essential for PG-derived amino sugar recycling via an unusual pathway. Together these data provide a critical first step in understanding how mycobacteria recycle their peptidoglycan.

Indexed as

AcetylglucosaminidaseAntibiotics, AntitubercularBacterial ProteinsCell WallDrug Resistance, BacterialMicrobial Sensitivity TestsMuramic AcidsMuramidaseMycobacterium bovisMycobacterium tuberculosisPeptidoglycanAcetylglucosaminidaseAntibiotics, AntitubercularBacterial ProteinsMuramic AcidsMuramidaseN-acetylmuramic acidPeptidoglycan

Identifiers

PMID31201321
PMCPMC6572805
OpenAlexW2951720000

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.