Evidence map›Paper›PMID 39478197›Full record

ArticleCommunications biology2024

Deciphering the role of VapBC13 and VapBC26 toxin antitoxin systems in the pathophysiology of Mycobacterium tuberculosis.

Arun Sharma, Neelam Singh, Munmun Bhasin, Prabhakar Tiwari, Pankaj Chopra, Raghavan Varadarajan, Ramandeep Singh

Abstract read
In one paragraph

Article in Communications biology, 2024. 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
–field-weighted citation impact
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

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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.

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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.

Arun SharmaCentre for Tuberculosis Research, Tuberculosis Research Laboratory, Translational Health Science and Technology Institute, Faridabad-Gurugram expressway, Faridabad, Haryana, India.
Neelam Singh *Centre for Tuberculosis Research, Tuberculosis Research Laboratory, Translational Health Science and Technology Institute, Faridabad-Gurugram expressway, Faridabad, Haryana, India.
Munmun Bhasin *Molecular Biophysics Unit, Indian Institute of Science, Bangalore, Karnataka, India.
Prabhakar TiwariCentre for Tuberculosis Research, Tuberculosis Research Laboratory, Translational Health Science and Technology Institute, Faridabad-Gurugram expressway, Faridabad, Haryana, India.
Pankaj ChopraCentre for Tuberculosis Research, Tuberculosis Research Laboratory, Translational Health Science and Technology Institute, Faridabad-Gurugram expressway, Faridabad, Haryana, India.
Raghavan VaradarajanMolecular Biophysics Unit, Indian Institute of Science, Bangalore, Karnataka, India.
Ramandeep SinghCentre for Tuberculosis Research, Tuberculosis Research Laboratory, Translational Health Science and Technology Institute, Faridabad-Gurugram expressway, Faridabad, Haryana, India. ramandeep@thsti.res.in.ORCID 0000-0003-2705-3826

Funding

DBT India Alliance (Wellcome Trust/DBT India Alliance) IA/S/19/2/504646Wellcome Trust
6 · The paper itself

Abstract

The expansion of VapBC TA systems in M. tuberculosis has been linked with its fitness and survival upon exposure to stress conditions. Here, we have functionally characterized VapBC13 and VapBC26 TA modules of M. tuberculosis. We report that overexpression of VapC13 and VapC26 toxins in M. tuberculosis results in growth inhibition and transcriptional reprogramming. We have also identified various regulatory proteins as hub nodes in the top response network of VapC13 and VapC26 overexpression strains. Further, analysis of RNA protection ratios revealed potential tRNA targets for VapC13 and VapC26. Using in vitro ribonuclease assays, we demonstrate that VapC13 and VapC26 degrade serT and leuW tRNA, respectively. However, no significant changes in rRNA cleavage profiles were observed upon overexpression of VapC13 and VapC26 in M. tuberculosis. In order to delineate the role of these TA systems in M. tuberculosis physiology, various mutant strains were constructed. We show that in comparison to the parental strain, ΔvapBC13 and ΔvapBC26 strains were mildly susceptible to oxidative stress. Surprisingly, the growth patterns of parental and mutant strains were comparable in aerosol-infected guinea pigs. These observations imply that significant functional redundancy exists for some TA systems from M. tuberculosis.

Indexed as

Bacterial ProteinsMycobacterium tuberculosisToxin-Antitoxin SystemsAnimalsBacterial ToxinsGene Expression Regulation, BacterialGuinea PigsOxidative StressRNA, TransferTuberculosisBacterial ProteinsBacterial ToxinsRNA, Transfer

Identifiers

PMID39478197
PMCPMC11525840

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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.