Evidence map›Paper›PMID 22645285›Full record

ArticleInfection and immunity2012

Urease activity represents an alternative pathway for Mycobacterium tuberculosis nitrogen metabolism.

Wenwei Lin, Vanessa Mathys, Emily Lei Yin Ang, Vanessa Hui Qi Koh, Julia María Martínez Gómez, Michelle Lay Teng Ang, Siti Zarina Zainul Rahim, Mai Ping Tan, Kevin Pethe, Sylvie Alonso

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Review
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  8. Proteomics ofJournal of fungi (Basel, Switzerland) · 2023
    Article
  9. Article
  10. Review
  11. Inhibition of Urease by Hydroquinones: A Structural and Kinetic Study.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  12. Microorganisms · 2022
    Article
  13. Article
  14. Structural characterization of the urease accessory protein UreF from Klebsiella pneumoniae.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The structure-based reaction mechanism of urease, a nickel dependent enzyme: tale of a long debate.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Review
  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

10 authors at 4 institutions in 5 countries.

Wenwei LinDepartment of Microbiology, Immunology Programme, Yong Loo Lin School of Medicine, National University of Singapore, Singapore.
Vanessa Mathys
Emily Lei Yin Ang
Vanessa Hui Qi Koh
Julia María Martínez Gómez
Michelle Lay Teng Ang
Siti Zarina Zainul Rahim
Mai Ping Tan
Kevin Pethe
Sylvie Alonso
National University of Singapore · SGCardiff University · GBInstitut Pasteur Korea · KRInstitut Scientifique de Santé Publique · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Urease represents a critical virulence factor for some bacterial species through its alkalizing effect, which helps neutralize the acidic microenvironment of the pathogen. In addition, urease serves as a nitrogen source provider for bacterial growth. Pathogenic mycobacteria express a functional urease, but its role during infection has yet to be characterized. In this study, we constructed a urease-deficient Mycobacterium tuberculosis strain and confirmed the alkalizing effect of the urease activity within the mycobacterium-containing vacuole in resting macrophages but not in the more acidic phagolysosomal compartment of activated macrophages. However, the urease-mediated alkalizing effect did not confer any growth advantage on M. tuberculosis in macrophages, as evidenced by comparable growth profiles for the mutant, wild-type (WT), and complemented strains. In contrast, the urease-deficient mutant exhibited impaired in vitro growth compared to the WT and complemented strains when urea was the sole source of nitrogen. Substantial amounts of ammonia were produced by the WT and complemented strains, but not with the urease-deficient mutant, which represents the actual nitrogen source for mycobacterial growth. However, the urease-deficient mutant displayed parental colonization profiles in the lungs, spleen, and liver in mice. Together, our data demonstrate a role for the urease activity in M. tuberculosis nitrogen metabolism that could be crucial for the pathogen's survival in nutrient-limited microenvironments where urea is the sole nitrogen source. Our work supports the notion that M. tuberculosis virulence correlates with its unique metabolic versatility and ability to utilize virtually any carbon and nitrogen sources available in its environment.

Indexed as

AnimalsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHydrogen-Ion ConcentrationMacrophagesMiceMice, Inbred BALB CMutationMycobacterium tuberculosisNitrogenRNA, BacterialTime FactorsTuberculosisUreaseNitrogenRNA, BacterialUrease

Identifiers

PMID22645285
PMCPMC3434571
OpenAlexW1966452070

What OpenQuestion holds

Textmetadata
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.