This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cosgrove, K.
Right arrow Articles by Foster, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cosgrove, K.
Right arrow Articles by Foster, S. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2007, p. 1025-1035, Vol. 189, No. 3
0021-9193/07/$08.00+0     doi:10.1128/JB.01524-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Catalase (KatA) and Alkyl Hydroperoxide Reductase (AhpC) Have Compensatory Roles in Peroxide Stress Resistance and Are Required for Survival, Persistence, and Nasal Colonization in Staphylococcus aureus{triangledown}

Kate Cosgrove,1 Graham Coutts,1 Ing-Marie Jonsson,2 Andrej Tarkowski,2 John F. Kokai-Kun,3 James J. Mond,3 and Simon J. Foster*

Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, S10 2TN, United Kingdom,1 Department of Rheumatology and Inflammation Research, Göteborg University, Göteborg, Sweden,2 Biosynexus Incorporated, 9119 Gaither Road, Gaithersburg, Maryland 208773

Received 29 September 2006/ Accepted 8 November 2006

Oxidative-stress resistance in Staphylococcus aureus is linked to metal ion homeostasis via several interacting regulators. In particular, PerR controls the expression of a regulon of genes, many of which encode antioxidants. Two PerR regulon members, ahpC (alkylhydroperoxide reductase) and katA (catalase), show compensatory regulation, with independent and linked functions. An ahpC mutation leads to increased H2O2 resistance due to greater katA expression via relief of PerR repression. Moreover, AhpC provides residual catalase activity present in a katA mutant. Mutation of both katA and ahpC leads to a severe growth defect under aerobic conditions in defined media (attributable to lack of catalase activity). This results in the inability to scavenge exogenous or endogenously produced H2O2, resulting in accumulation of H2O2 in the medium. This leads to DNA damage, the likely cause of the growth defect. Surprisingly, the katA ahpC mutant is not attenuated in two independent models of infection, which implies reduced oxygen availability during infection. In contrast, both AhpC and KatA are required for environmental persistence (desiccation) and nasal colonization. Thus, oxidative-stress resistance is an important factor in the ability of S. aureus to persist in the hospital environment and so contribute to the spread of human disease.

* Corresponding author. Mailing address: Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, S10 2TN, United Kingdom. Phone: (44) 0114 222 4411. Fax: (44) 0114 222 2800. E-mail: S.foster{at}sheffield.ac.uk.

{triangledown} Published ahead of print on 17 November 2006.

Journal of Bacteriology, February 2007, p. 1025-1035, Vol. 189, No. 3
0021-9193/07/$08.00+0     doi:10.1128/JB.01524-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Doyle, M., Feuerbaum, E.-A., Fox, K. R., Hinds, J., Thurston, D. E., Taylor, P. W. (2009). Response of Staphylococcus aureus to subinhibitory concentrations of a sequence-selective, DNA minor groove cross-linking pyrrolobenzodiazepine dimer. J Antimicrob Chemother 64: 949-959 [Abstract] [Full Text]  
  • Hebrard, M., Viala, J. P. M., Meresse, S., Barras, F., Aussel, L. (2009). Redundant Hydrogen Peroxide Scavengers Contribute to Salmonella Virulence and Oxidative Stress Resistance. J. Bacteriol. 191: 4605-4614 [Abstract] [Full Text]  
  • Ballal, A., Manna, A. C. (2009). Regulation of Superoxide Dismutase (sod) Genes by SarA in Staphylococcus aureus. J. Bacteriol. 191: 3301-3310 [Abstract] [Full Text]  
  • Martinez-Pulgarin, S., Dominguez-Bernal, G., Orden, J. A., de la Fuente, R. (2009). Simultaneous lack of catalase and beta-toxin in Staphylococcus aureus leads to increased intracellular survival in macrophages and epithelial cells and to attenuated virulence in murine and ovine models. Microbiology 155: 1505-1515 [Abstract] [Full Text]  
  • Selva, L., Viana, D., Regev-Yochay, G., Trzcinski, K., Corpa, J. M., Lasa, i., Novick, R. P., Penades, J. R. (2009). Killing niche competitors by remote-control bacteriophage induction. Proc. Natl. Acad. Sci. USA 106: 1234-1238 [Abstract] [Full Text]  
  • Sorci, G., Faivre, B. (2009). Inflammation and oxidative stress in vertebrate host-parasite systems. Phil Trans R Soc B 364: 71-83 [Abstract] [Full Text]  
  • Hochgrafe, F., Wolf, C., Fuchs, S., Liebeke, M., Lalk, M., Engelmann, S., Hecker, M. (2008). Nitric Oxide Stress Induces Different Responses but Mediates Comparable Protein Thiol Protection in Bacillus subtilis and Staphylococcus aureus. J. Bacteriol. 190: 4997-5008 [Abstract] [Full Text]  
  • Nodop, A., Pietsch, D., Hocker, R., Becker, A., Pistorius, E. K., Forchhammer, K., Michel, K.-P. (2008). Transcript Profiling Reveals New Insights into the Acclimation of the Mesophilic Fresh-Water Cyanobacterium Synechococcus elongatus PCC 7942 to Iron Starvation. Plant Physiol. 147: 747-763 [Abstract] [Full Text]  
  • Park, B., Nizet, V., Liu, G. Y. (2008). Role of Staphylococcus aureus Catalase in Niche Competition against Streptococcus pneumoniae. J. Bacteriol. 190: 2275-2278 [Abstract] [Full Text]  
  • Schlag, S., Nerz, C., Birkenstock, T. A., Altenberend, F., Gotz, F. (2007). Inhibition of Staphylococcal Biofilm Formation by Nitrite. J. Bacteriol. 189: 7911-7919 [Abstract] [Full Text]  
  • Stapleton, M. R., Horsburgh, M. J., Hayhurst, E. J., Wright, L., Jonsson, I.-M., Tarkowski, A., Kokai-Kun, J. F., Mond, J. J., Foster, S. J. (2007). Characterization of IsaA and SceD, Two Putative Lytic Transglycosylases of Staphylococcus aureus. J. Bacteriol. 189: 7316-7325 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»