Evidence map›Paper›PMID 30810776›Full record

ReviewApplied microbiology and biotechnology2019

Function, essentiality, and expression of cytochrome P450 enzymes and their cognate redox partners in Mycobacterium tuberculosis: are they drug targets?

Sandra Ortega Ugalde, Maikel Boot, Jan N M Commandeur, Paul Jennings, Wilbert Bitter, J Chris Vos

Open access · hybridAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  8. Frontiers in cellular and infection microbiology · 2023
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  11. Dissecting theVaccines · 2022
    Article
  12. Article
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  15. Complete Genome Sequence of OvineMicroorganisms · 2020
    Article
  16. Article
  17. Microbiology spectrum · 2019
    Review
  18. Article
  19. 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

6 authors at 2 institutions in 2 countries.

Sandra Ortega UgaldeDivision of Molecular Toxicology, Amsterdam Institute for Molecules Medicines and Systems (AIMMS), Faculty of Sciences, Vrije Universiteit, De Boelelaan 1108, 1081 HZ, Amsterdam, The Netherlands. s.ortegaugalde@vu.nl.
Maikel BootDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Jan N M CommandeurDivision of Molecular Toxicology, Amsterdam Institute for Molecules Medicines and Systems (AIMMS), Faculty of Sciences, Vrije Universiteit, De Boelelaan 1108, 1081 HZ, Amsterdam, The Netherlands.
Paul JenningsDivision of Molecular Toxicology, Amsterdam Institute for Molecules Medicines and Systems (AIMMS), Faculty of Sciences, Vrije Universiteit, De Boelelaan 1108, 1081 HZ, Amsterdam, The Netherlands.
Wilbert BitterSection of Molecular Microbiology, AIMMS, Faculty of Sciences, Vrije Universiteit, Amsterdam, The Netherlands.
J Chris VosDivision of Molecular Toxicology, Amsterdam Institute for Molecules Medicines and Systems (AIMMS), Faculty of Sciences, Vrije Universiteit, De Boelelaan 1108, 1081 HZ, Amsterdam, The Netherlands.
Vrije Universiteit Amsterdam · NLYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This review covers the current knowledge of the cytochrome P450 enzymes (CYPs) of the human pathogen Mycobacterium tuberculosis (Mtb) and their endogenous redox partners, focusing on their biological function, expression, regulation, involvement in antibiotic resistance, and suitability for exploitation as antitubercular targets. The Mtb genome encodes twenty  CYPs and nine associated redox partners required for CYP catalytic activity. Transposon insertion mutagenesis studies have established the (conditional) essentiality of several of these enzymes for in vitro growth and host infection. Biochemical characterization of a handful of Mtb CYPs has revealed that they have specific physiological functions in bacterial virulence and persistence in the host. Analysis of the transcriptional response of Mtb CYPs and redox partners to external insults and to first-line antibiotics used to treat tuberculosis showed a diverse expression landscape, suggesting for some enzymes a potential role in drug resistance. Combining the knowledge about the physiological roles and expression profiles indicates that, at least five Mtb CYPs, CYP121A1, CYP125A1, CYP139A1, CYP142A1, and CYP143A1, as well as two ferredoxins, FdxA and FdxC, can be considered promising novel therapeutic targets.

Indexed as

AnimalsAntitubercular AgentsBacterial ProteinsBiocatalysisCytochrome P-450 Enzyme SystemHumansMycobacterium tuberculosisOxidation-ReductionTuberculosisAntitubercular AgentsBacterial ProteinsCytochrome P-450 Enzyme SystemAntibiotic exposure responseCytochrome P450EssentialityMycobacterium tuberculosisRedox partnersStress response

Identifiers

PMID30810776
PMCPMC6469627
OpenAlexW2916389839

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.