Evidence map›Paper›PMID 26228622›Full record

ArticleScientific reports2015

RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth and intracellular survival of mycobacteria.

Pramod K Singh, Richa Saxena, Sameer Tiwari, Diwakar K Singh, Susmita K Singh, Ruma Kumari, Kishore K Srivastava

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Macrophage states and polarization duringFrontiers in cellular and infection microbiology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Modular Organization of the ESX-5 Secretion System in Mycobacterium tuberculosis.Frontiers in cellular and infection microbiology · 2016
    Review
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

7 authors at 2 institutions in 1 country.

Pramod K SinghDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Richa SaxenaDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Sameer TiwariDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Diwakar K SinghDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Susmita K SinghDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Ruma KumariDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Kishore K SrivastavaDivision of Microbiology and Academy of Scientific and Innovative Research, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Academy of Scientific and Innovative Research · INCentral Drug Research Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacterium tuberculosis (MTB) synchronizes a number of processes and controls a series of events to subvert host defense mechanisms for the sake of residing inside macrophages. Besides these, MTB also possesses a wide range of signal enzyme systems, including eleven serine threonine protein kinases (STPKs). The present study describes STPK modulated modification in one of the hypothetical proteins of the RD1 region; EspJ (ESX-1 secretion associated protein), which is predicted to be involved in virulence of MTB. We have employed knock-out MTB, and M. bovis BCG as a surrogate strain to elaborate the consequence of the phosphorylation of EspJ. The molecular and mass spectrometric analyses in this study, confirmed EspJ as one of the substrates of STPKs. The ectopic expression of phosphoablative mutants of espJ in M. bovis BCG also articulated the effect of phosphorylation on the growth and in survival of mycobacteria. Importantly, the level of phosphorylation of EspJ also differed between pathogenic H37 Rv (Rv) and non pathogenic H37 Ra (Ra) strains of MTB. This further suggested that to a certain extent, the STPKs mediated phosphorylation may be accountable, in determining the growth and in intra-cellular survival of mycobacteria.

Indexed as

Bacterial ProteinsCell LineGene Expression Regulation, BacterialHumansMacrophagesMutationMycobacterium bovisMycobacterium tuberculosisPhagocytosisPhosphorylationPhylogenyProtein Serine-Threonine KinasesBacterial ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID26228622
PMCPMC4521147
OpenAlexW1038415639

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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.