Evidence map›Paper›PMID 32295519›Full record

ArticleBMC microbiology2020

Protein-protein interaction of Rv0148 with Htdy and its predicted role towards drug resistance in Mycobacterium tuberculosis.

Gunapati Bhargavi, Sameer Hassan, Subramanyam Balaji, Srikanth Prasad Tripathy, Kannan Palaniyandi

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.1field-weighted citation impact, top 43% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. A Pilot Proteomics Analysis ofInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. A putative short-chain dehydrogenase Rv0148 ofCurrent research in microbial sciences · 2022
    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

5 authors at 2 institutions in 2 countries.

Gunapati BhargaviDepartment of Immunology, ICMR-National Institute for Research in Tuberculosis, #1, Mayor Sathyamoorthy Road, Chetpet, Chennai, 600031, India.
Sameer HassanDepartment of Biological and Environmental Sciences, University of Gothenburg, Gothenburg, Sweden.
Subramanyam BalajiDepartment of Immunology, ICMR-National Institute for Research in Tuberculosis, #1, Mayor Sathyamoorthy Road, Chetpet, Chennai, 600031, India.
Srikanth Prasad TripathyDepartment of Immunology, ICMR-National Institute for Research in Tuberculosis, #1, Mayor Sathyamoorthy Road, Chetpet, Chennai, 600031, India.
Kannan PalaniyandiDepartment of Immunology, ICMR-National Institute for Research in Tuberculosis, #1, Mayor Sathyamoorthy Road, Chetpet, Chennai, 600031, India. kannanvet@rediffmail.com.
National Institute of Research in Tuberculosis · INUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMycobacterium tuberculosis resides inside host macrophages during infection and adapts to resilient stresses generated by the host immune system. As a response, M. tuberculosis codes for short-chain dehydrogenases/reductases (SDRs). These SDRs are nicotinamide adenine dinucleotide-reliant oxidoreductases involved in cell homeostasis. The precise function of oxidoreductases in bacteria especially M. tuberculosis were not fully explored. This study aimed to know the detail functional role of one of the oxidoreductase Rv0148 in M. tuberculosis.

resultsIn silico analysis revealed that Rv0148 interacts with Htdy (Rv3389) and the protein interactions were confirmed using far western blot. Gene knockout mutant of Rv0148 in M. tuberculosis was constructed by specialized transduction. Macrophage cell line infection with this knockout mutant showed increased expression of pro-inflammatory cytokines. This knockout mutant is sensitive to oxidative, nitrogen, redox and electron transport inhibitor stress agents. Drug susceptibility testing of the deletion mutant showed resistance to first-line drugs such as streptomycin and ethambutol and second-line aminoglycosides such as amikacin and kanamycin. Based on interactorme analysis for Rv0148 using STRING database, we identified 220 most probable interacting partners for Htdy protein. In the Rv0148 knockout mutants, high expression of htdy was observed and we hypothesize that this would have perturbed the interactome thus resulting in drug resistance. Finally, we propose that Rv0148 and Htdy are functionally interconnected and involved in drug resistance and cell homeostasis of M. tuberculosis.

conclusionsOur study suggests that Rv0148 plays a significant role in various functional aspects such as intermediatory metabolism, stress, homeostasis and also in drug resistance.

Indexed as

Drug Resistance, Multiple, BacterialAnti-Bacterial AgentsBacterial ProteinsCatalytic DomainComputer SimulationEnoyl-CoA HydrataseGene Knockout TechniquesHomeostasisHumansModels, MolecularMolecular Docking SimulationMycobacterium tuberculosisOxidoreductasesProtein ConformationProtein Interaction MappingProtein Interaction MapsAnti-Bacterial AgentsBacterial ProteinsEnoyl-CoA HydrataseOxidoreductasesDrug resistanceHtdyMycobacterium tuberculosisOxidoreductasesRv0148Stress responseTuberculosis

Identifiers

PMID32295519
PMCPMC7161113
OpenAlexW3017301615

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.