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Salmonella detoxifying enzymes are sufficient to cope with the host oxidative burst.
Mol Microbiol. 2011 May; 80(3):628-40
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23 May 2011
Martin Marinus
F1000 Microbiology
University of Massachusetts Medical School,
Worcester, Massachusetts, USA.
F1000 Microbiology
University of Massachusetts Medical School,
Worcester, Massachusetts, USA.
New Finding
DOI: 10.3410/f.10681956.11566054
Host cells produce bursts of reactive oxygen species (ROS) to kill invading bacterial pathogens. This study shows that the housekeeping arsenal of detoxifying enzymes is sufficient to help Salmonella resist ROS.
To study the effects of oxidative stress, the authors used a transcriptional green fluorescent...Continue reading
To study the effects of oxidative stress, the authors used a transcriptional green fluorescent...Continue reading
Host cells produce bursts of reactive oxygen species (ROS) to kill invading bacterial pathogens. This study shows that the housekeeping arsenal of detoxifying enzymes is sufficient to help Salmonella resist ROS.
To study the effects of oxidative stress, the authors used a transcriptional green fluorescent protein (GFP) fusion to the peroxide-inducible alkylhydroperoxide reductase (ahpC) gene, which is part of the OxyR regulon. This fusion responds to ROS produced in vitro and in vivo and is dependent on bacterial dismutases, catalases and peroxidases. Previously it had been suggested that Salmonella pathogenicity island 2 produced secreted proteins to cope with ROS from the host {1}. In this paper, however, loss of pathogenicity island 2 had no measurable effect on the amount of GFP fluorescence.
To study the effects of oxidative stress, the authors used a transcriptional green fluorescent protein (GFP) fusion to the peroxide-inducible alkylhydroperoxide reductase (ahpC) gene, which is part of the OxyR regulon. This fusion responds to ROS produced in vitro and in vivo and is dependent on bacterial dismutases, catalases and peroxidases. Previously it had been suggested that Salmonella pathogenicity island 2 produced secreted proteins to cope with ROS from the host {1}. In this paper, however, loss of pathogenicity island 2 had no measurable effect on the amount of GFP fluorescence.
References
1.
Salmonella pathogenicity island 2-encoded type III secretion system mediates exclusion of NADPH oxidase assembly from the phagosomal membrane.
J Immunol 2001 May 1; 9(166):5741-8
PMID: 11313417
Disclosures
None declared
Add Comment
Marinus M: F1000Prime Recommendation of [Aussel L et al., Mol Microbiol 2011, 80(3):628-40]. In F1000Prime, 23 May 2011; DOI: 10.3410/f.10681956.11566054. F1000Prime.com/10681956#eval11566054
F1000Prime Recommendations, Dissents and Comments for [Aussel L et al., Mol Microbiol 2011, 80(3):628-40]. In F1000Prime, 23 May 2013; F1000Prime.com/10681956
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The oxidative burst produced by the NADPH oxidase (Phox) is an essential weapon used by host cells to eradicate engulfed pathogens. In Salmonella typhimurium, oxidative stress resistance has been previously proposed to be mediated by the pathogenicity island 2 type III secretion system (T3SS-2), periplasmic superoxide dismutases and cytoplasmic catalases/peroxidases. Here, we fused an OxyR-dependent promoter to the gfp to build the ahpC-gfp transcriptional fusion. This reporter was used to monitor hydrogen peroxide levels as sensed by Salmonella during the course of an infection. We showed that the expression of this fusion was under the exclusive control of reactive oxygen species produced by the host. The ahpC-gfp expression was noticeably modified in the absence of bacterial periplasmic superoxide dismutases or cytoplasmic catalases/peroxidases. Surprisingly, inactivation of the T3SS-2 had no effect on the ahpC-gfp expression. All together, these results led to a model in which Salmonella resistance relies on its arsenal of detoxifying enzymes to cope with Phox-mediated oxidative stress.
© 2011 Blackwell Publishing Ltd.
DOI: 10.1111/j.1365-2958.2011.07611.x
PMID: 21362067
