ArticleProceedings of the National Academy of Sciences of the United States of America1995
Disparate responses to oxidative stress in saprophytic and pathogenic mycobacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed.
- Prominent transcriptomic changes in Mycobacterium intracellulare under acidic and oxidative stress.BMC genomics · 2024Article
- In vitro Antibacterial Effect Study of Plasma-Activated Saline onInfection and drug resistance · 2024Article
- Structural and Biochemical Characterization of Thioredoxin-2 fromAntioxidants (Basel, Switzerland) · 2021Article
- Comparative Study of the Susceptibility to Oxidative Stress between Two Types of Mycobacterium bovis BCG Tokyo 172.mSphere · 2021Article
- HDAC3 inhibitor RGFP966 controls bacterial growth and modulates macrophage signaling during Mycobacterium tuberculosis infection.Tuberculosis (Edinburgh, Scotland) · 2021Article
- Genetic Variation/Evolution and Differential Host Responses Resulting from In-Patient Adaptation ofInfection and immunity · 2019Article
- Redox-dependent condensation of the mycobacterial nucleoid by WhiB4.Redox biology · 2018Article
- Elucidation of a mechanism of oxidative stress regulation in Francisella tularensis live vaccine strain.Molecular microbiology · 2016Article
- Article
- Mycobacterium tuberculosis has diminished capacity to counteract redox stress induced by elevated levels of endogenous superoxide.Free radical biology & medicine · 2015Article
- Thiol-based redox switches in prokaryotes.Biological chemistry · 2015Review
- FurA contributes to the oxidative stress response regulation of Mycobacterium avium ssp. paratuberculosis.Frontiers in microbiology · 2015Article
- Replication rates of Mycobacterium tuberculosis in human macrophages do not correlate with mycobacterial antibiotic susceptibility.PloS one · 2014Article
- An altered Mycobacterium tuberculosis metabolome induced by katG mutations resulting in isoniazid resistance.Antimicrobial agents and chemotherapy · 2014Article
- Antimicrobial strategies centered around reactive oxygen species--bactericidal antibiotics, photodynamic therapy, and beyond.FEMS microbiology reviews · 2013Review
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- Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.The Journal of biological chemistry · 2013Article
- Article
- Mycobacterium smegmatis RoxY is a repressor of oxyS and contributes to resistance to oxidative stress and bactericidal ubiquitin-derived peptides.Journal of bacteriology · 2011Article
- The response of mycobacterium tuberculosis to reactive oxygen and nitrogen species.Frontiers in microbiology · 2011Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
Abstract
To persist in macrophages and in granulomatous caseous lesions, pathogenic mycobacteria must be equipped to withstand the action of toxic oxygen metabolites. In Gram-negative bacteria, the OxyR protein is a critical component of the oxidative stress response. OxyR is both a sensor of reactive oxygen species and a transcriptional activator, inducing expression of detoxifying enzymes such as catalase/hydroperoxidase and alkyl hydroperoxidase. We have characterized the responses of various mycobacteria to hydrogen peroxide both phenotypically and at the levels of gene and protein expression. Only the saprophytic Mycobacterium smegmatis induced a protective oxidative stress response analogous to the OxyR response of Gram-negative bacteria. Under similar conditions, the pathogenic mycobacteria exhibited a limited, nonprotective response, which in the case of Mycobacterium tuberculosis was restricted to induction of a single protein, KatG. We have also isolated DNA sequences homologous to oxyR and ahpC from M. tuberculosis and Mycobacterium avium. While the M. avium oxyR appears intact, the oxyR homologue of M. tuberculosis contains numerous deletions and frameshifts and is probably nonfunctional. Apparently the response of pathogenic mycobacteria to oxidative stress differs significantly from the inducible OxyR response of other bacteria.
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