Interdependence of mycobacterial iron regulation, oxidative-stress response and isoniazid resistance. (Q54120901)

25 May 2018

review article

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title

Interdependence of mycobacterial iron regulation, oxidative-stress response and isoniazid resistance. (English)

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25 May 2018

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Dussurget O

1

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25 May 2018

Smith I

series ordinal

2

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25 May 2018

publication date

1 September 1998

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25 May 2018

published in

Trends in Microbiology

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25 May 2018

volume

6

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25 May 2018

issue

9

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25 May 2018

page(s)

354-358

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25 May 2018

Role of iron in regulation of virulence genes

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Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall

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Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae

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An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response.

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Loss of oxyR in Mycobacterium tuberculosis

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Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways.

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The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin

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Increased production of hydrogen peroxide and expression of CD11b/CD18 on alveolar macrophages in patients with active pulmonary tuberculosis

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Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis

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Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase

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Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: implications for sensitivity to isoniazid.

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Microbial glycolipids: possible virulence factors that scavenge oxygen radicals

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inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis

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Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis

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Enzymatic and nonenzymatic superoxide-generating reactions of isoniazid

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Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra

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Manganese-mediated oxidative damage of cellular and isolated DNA by isoniazid and related hydrazines: non-Fenton-type hydroxyl radical formation

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Role of superoxide in catalase-peroxidase-mediated isoniazid action against mycobacteria.

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Oxidative stress response and its role in sensitivity to isoniazid in mycobacteria: characterization and inducibility of ahpC by peroxides in Mycobacterium smegmatis and lack of expression in M. aurum and M. tuberculosis

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Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid

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7 January 2021

10.1016/S0966-842X(98)01307-9

Identifiers

DOI

1 reference

25 May 2018

PubMed ID

9778728

1 reference

25 May 2018