Evidence map›Paper›PMID 24706757›Full record

ArticleThe Journal of biological chemistry2014

Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host.

Yogesh Chawla, Sandeep Upadhyay, Shazia Khan, Sathya Narayanan Nagarajan, Francesca Forti, Vinay Kumar Nandicoori

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

71 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Microorganisms · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Large-scale Pan Genomic Analysis ofEvolutionary bioinformatics online · 2024
    Article
  13. Review
  14. Article
  15. PeerJ · 2023
    Article
  16. Protocol forSTAR protocols · 2022
    Article
  17. Microorganisms · 2022
    Review
  18. Article
  19. Review
  20. Article

11 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Yogesh ChawlaFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India and.
Sandeep UpadhyayFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India and.
Shazia KhanFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India and.
Sathya Narayanan NagarajanFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India and.
Francesca Fortithe Dipartimento di Scienze Biomolecolari e Biotecnologie, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.
Vinay Kumar NandicooriFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India and Vinaykn@nii.ac.in.
National Institute of Immunology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Mycobacterium tuberculosis protein kinase B (PknB) comprises an intracellular kinase domain, connected through a transmembrane domain to an extracellular region that contains four PASTA domains. The present study describes the comprehensive analysis of different domains of PknB in the context of viability in avirulent and virulent mycobacteria. We find stringent regulation of PknB expression necessary for cell survival, with depletion or overexpression of PknB leading to cell death. Although PknB-mediated kinase activity is essential for cell survival, active kinase lacking the transmembrane or extracellular domain fails to complement conditional mutants not expressing PknB. By creating chimeric kinases, we find that the intracellular kinase domain has unique functions in the virulent strain, which cannot be substituted by other kinases. Interestingly, we find that although the presence of the C-terminal PASTA domain is dispensable in the avirulent M. smegmatis, all four PASTA domains are essential in M. tuberculosis. The differential behavior of PknB vis-à-vis the number of essential PASTA domains and the specificity of kinase domain functions suggest that PknB-mediated growth and signaling events differ in virulent compared with avirulent mycobacteria. Mouse infection studies performed to determine the role of PknB in mediating pathogen survival in the host demonstrate that PknB is not only critical for growth of the pathogen in vitro but is also essential for the survival of the pathogen in the host.

Indexed as

AnimalsCell MembraneCell ProliferationExtracellular SpaceGene Expression Regulation, BacterialIntracellular SpaceMiceMicrobial ViabilityMycobacterium tuberculosisProtein Serine-Threonine KinasesProtein Structure, TertiaryProtein TransportPknB protein, Mycobacterium tuberculosisProtein Serine-Threonine KinasesBacterial Protein KinasesCell GrowthCell SignalingMycobacteriaPASTA DomainPknBProtein Phosphorylation

Identifiers

PMID24706757
PMCPMC4022859
OpenAlexW1997882784

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.