DpsA protects the human pathogen Burkholderia pseudomallei against organic hydroperoxide

The human pathogen, Burkholderia pseudomalle, is able to survive and multiply in hostile environments such as within macrophages. In an attempt to understand its strategy to cope with oxidative stress, the physiological role and gene regulation of a nonspecific DNA-binding protein (DpsA) was investi...

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Bibliographic Details
Published in:Archives of microbiology 2004-09, Vol.182 (1), p.96-101
Main Authors: LOPRASERT, Suvit, WHANGSUK, Wirongrong, SALLABHAN, Ratiboot, MONGKOLSUK, Skorn
Format: Article
Language:English
Subjects:
Bacteria
Bacterial diseases
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
Burkholderia pseudomallei
Burkholderia pseudomallei - drug effects
Burkholderia pseudomallei - genetics
Burkholderia pseudomallei - physiology
DNA-Binding Proteins - physiology
E coli
Escherichia coli
Fundamental and applied biological sciences. Psychology
Human bacterial diseases
Humans
Hydrogen Peroxide - pharmacology
Infectious diseases
Medical sciences
Melioidosis
Microbiology
Miscellaneous
Oxidants - metabolism
Oxidants - pharmacology
Oxidative Stress
Oxidizing agents
Pathogens
Tropical bacterial diseases
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Summary:The human pathogen, Burkholderia pseudomalle, is able to survive and multiply in hostile environments such as within macrophages. In an attempt to understand its strategy to cope with oxidative stress, the physiological role and gene regulation of a nonspecific DNA-binding protein (DpsA) was investigated. Expression of dpsA increases in response to oxidative stress through increased transcription from the upstream katG (catalase-peroxidase) promoter, which is OxyR dependent. dpsA is also transcribed from its own promoter, which is activated by osmotic stress in an OxyR-independent manner. DpsA-deficient mutants are hypersensitive to tert-butyl hydroperoxide, while overexpression of DpsA leads to increased resistance to organic oxidants. B. pseudomallei DpsA can also protect Escherichia coli against organic hydroperoxide toxicity. The mechanism of DpsA-mediated resistance to organic hydroperoxides was shown to differ from that of alkyl hydroperoxide reductase.
ISSN:0302-8933
1432-072X
DOI:10.1007/s00203-004-0694-0