Evidence map›Paper›PMID 26489015›Full record

ArticlePLoS pathogens2015

Depletion of M. tuberculosis GlmU from Infected Murine Lungs Effects the Clearance of the Pathogen.

Vijay Soni, Sandeep Upadhayay, Priyanka Suryadevara, Ganesh Samla, Archana Singh, Perumal Yogeeswari, Dharmarajan Sriram, Vinay Kumar Nandicoori

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

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  12. Review
  13. The Inhibitory Effect of GlmU Acetyltransferase Inhibitor TPSA onFrontiers in cellular and infection microbiology · 2019
    Article
  14. Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018
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  15. Article
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  17. Protein kinase G confers survival advantage toThe Journal of biological chemistry · 2017
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  18. The Journal of biological chemistry · 2017
    Article
  19. 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

8 authors at 4 institutions in 1 country.

Vijay SoniNational Institute of Immunology, New Delhi, India; Department of Pharmacy, Birla Institute of Technology and Science-Pilani, Hyderabad Campus, Hyderabad, India.
Sandeep UpadhayayNational Institute of Immunology, New Delhi, India.
Priyanka SuryadevaraDepartment of Pharmacy, Birla Institute of Technology and Science-Pilani, Hyderabad Campus, Hyderabad, India.
Ganesh SamlaDepartment of Pharmacy, Birla Institute of Technology and Science-Pilani, Hyderabad Campus, Hyderabad, India.
Archana SinghCSIR-Institute of Genomics and Integrative Biology, New Delhi, India.
Perumal YogeeswariDepartment of Pharmacy, Birla Institute of Technology and Science-Pilani, Hyderabad Campus, Hyderabad, India.
Dharmarajan SriramDepartment of Pharmacy, Birla Institute of Technology and Science-Pilani, Hyderabad Campus, Hyderabad, India.
Vinay Kumar NandicooriNational Institute of Immunology, New Delhi, India.
National Institute of Immunology · INBirla Institute of Technology and Science - Hyderabad Campus · INBirla Institute of Technology and Science, Pilani · INInstitute of Genomics and Integrative Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

M. tuberculosis N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmUMtb) is a bi-functional enzyme engaged in the synthesis of two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc, catalyzed by the C- and N-terminal domains respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols. While glmUMtb was predicted to be an essential gene, till date the role of GlmUMtb in modulating the in vitro growth of Mtb or its role in survival of pathogen ex vivo / in vivo have not been deciphered. Here we present the results of a comprehensive study dissecting the role of GlmUMtb in arbitrating the survival of the pathogen both in vitro and in vivo. We find that absence of GlmUMtb leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. Complementation studies show that the acetyl- and uridyl- transferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also found to be essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmUMtb from infected murine lungs, four weeks post infection, led to significant reduction in the bacillary load. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice resulted in significant decrease in the bacillary load. Thus our study establishes GlmUMtb as a strong candidate for intervention measures against established tuberculosis infections.

Indexed as

Mycobacterium tuberculosisAnimalsBacterial ProteinsBenzylidene CompoundsBlotting, WesternDisease Models, AnimalGuinea PigsMiceMice, Inbred BALB CMultienzyme ComplexesMutagenesis, Site-DirectedNaphthalenesOxazolesTuberculosisBacterial ProteinsBenzylidene CompoundsGlmU protein, Mycobacterium tuberculosisMultienzyme ComplexesNaphthalenesOxazoles

Identifiers

PMID26489015
PMCPMC4619583
OpenAlexW2267688187

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.