Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/75447
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Type: Journal article
Title: Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
Author: Potter, A.
Trappetti, C.
Paton, J.
Citation: Journal of Bacteriology, 2012; 194(22):6248-6254
Publisher: Amer Soc Microbiology
Issue Date: 2012
ISSN: 0021-9193
1098-5530
Statement of
Responsibility: 
Adam J. Potter, Claudia Trappetti, and James C. Paton
Abstract: The thiol-containing tripeptide glutathione is an important cellular constituent of many eukaryotic and prokaryotic cells. In addition to its disulfide reductase activity, glutathione is known to protect cells from many forms of physiological stress. This report represents the first investigation into the role of glutathione in the Gram-positive pathogen Streptococcus pneumoniae. We demonstrate that pneumococci import extracellular glutathione using the ABC transporter substrate binding protein GshT. Mutation of gshT and the gene encoding glutathione reductase (gor) increases pneumococcal sensitivity to the superoxide generating compound paraquat, illustrating the importance of glutathione utilization in pneumococcal oxidative stress resistance. In addition, the gshT and gor mutant strains are hypersensitive to challenge with the divalent metal ions copper, cadmium, and zinc. The importance of glutathione utilization in pneumococcal colonization and invasion of the host is demonstrated by the attenuated phenotype of the gshT mutant strain in a mouse model of infection.
Keywords: Animals; Mice; Streptococcus pneumoniae; Metals; Glutathione Reductase; Bacterial Proteins; Membrane Transport Proteins; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Oxidative Stress; Mutation; Time Factors
Rights: Copyright © 2012, American Society for Microbiology. All Rights Reserved
RMID: 0020123015
DOI: 10.1128/JB.01393-12
Appears in Collections:Molecular and Biomedical Science publications

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