Evidence map›Paper›PMID 27758870›Full record

ArticleThe Journal of biological chemistry2016

Serine/Threonine Protein Phosphatase PstP of Mycobacterium tuberculosis Is Necessary for Accurate Cell Division and Survival of Pathogen.

Aditya K Sharma, Divya Arora, Lalit K Singh, Aakriti Gangwal, Andaleeb Sajid, Virginie Molle, Yogendra Singh, Vinay Kumar Nandicoori

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
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  12. An Epistatic Network DescribesFrontiers in molecular biosciences · 2022
    Article
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  15. Journal of bacteriology · 2021
    Article
  16. Review
  17. Article
  18. Frontiers in microbiology · 2021
    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 2 countries.

Aditya K SharmaCSIR-Institute of Genomics and Integrative Biology, Mall Road, Delhi-110007, India.
Divya AroraFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi-110067, India.
Lalit K SinghCSIR-Institute of Genomics and Integrative Biology, Mall Road, Delhi-110007, India.
Aakriti Gangwalthe Department of Zoology, University of Delhi Delhi-110007, India.
Andaleeb SajidCSIR-Institute of Genomics and Integrative Biology, Mall Road, Delhi-110007, India.
Virginie Mollethe Laboratoire de Dynamique des Interactions Membranaires Normales et Pathologiques, Université Montpellier 2, CNRS, UMR 5235, Montpellier, France, and.
Yogendra SinghCSIR-Institute of Genomics and Integrative Biology, Mall Road, Delhi-110007, India, ysingh@igib.res.in.
Vinay Kumar NandicooriFrom the National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi-110067, India, vinaykn@nii.ac.in.
Institute of Genomics and Integrative Biology · INNational Institute of Immunology · INUniversité de Montpellier · FRUniversity of Delhi · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphatases play vital roles in phosphorylation-mediated cellular signaling. Although there are 11 serine/threonine protein kinases in Mycobacterium tuberculosis, only one serine/threonine phosphatase, PstP, has been identified. Although PstP has been biochemically characterized and multiple in vitro substrates have been identified, its physiological role has not yet been elucidated. In this study, we have investigated the impact of PstP on cell growth and survival of the pathogen in the host. Overexpression of PstP led to elongated cells and partially compromised survival. We find that depletion of PstP is detrimental to cell survival, eventually leading to cell death. PstP depletion results in elongated multiseptate cells, suggesting a role for PstP in regulating cell division events. Complementation experiments performed with PstP deletion mutants revealed marginally compromised survival, suggesting that all of the domains, including the extracellular domain, are necessary for complete rescue. On the other hand, the catalytic activity of PstP is absolutely essential for the in vitro growth. Mice infection experiments establish a definitive role for PstP in pathogen survival within the host. Depletion of PstP from established infections causes pathogen clearance, indicating that the continued presence of PstP is necessary for pathogen survival. Taken together, our data suggest an important role for PstP in establishing and maintaining infection, possibly via the modulation of cell division events.

Indexed as

Microbial ViabilityAnimalsBacterial ProteinsCell DivisionGene DeletionMiceMycobacterium tuberculosisPhosphoprotein PhosphatasesTuberculosisBacterial ProteinsPhosphoprotein Phosphatasescell divisioncell signalingmycobacteriaMycobacterium tuberculosisphosphatasephosphorylationprotein serine/threonine phosphatase (PSP)PstP

Identifiers

PMID27758870
PMCPMC5104944
OpenAlexW2527752834

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.