Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/75447
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dc.contributor.authorPotter, A.en
dc.contributor.authorTrappetti, C.en
dc.contributor.authorPaton, J.en
dc.date.issued2012en
dc.identifier.citationJournal of Bacteriology, 2012; 194(22):6248-6254en
dc.identifier.issn0021-9193en
dc.identifier.issn1098-5530en
dc.identifier.urihttp://hdl.handle.net/2440/75447-
dc.description.abstractThe 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.en
dc.description.statementofresponsibilityAdam J. Potter, Claudia Trappetti, and James C. Patonen
dc.language.isoenen
dc.publisherAmer Soc Microbiologyen
dc.rightsCopyright © 2012, American Society for Microbiology. All Rights Reserveden
dc.subjectAnimals; Mice; Streptococcus pneumoniae; Metals; Glutathione Reductase; Bacterial Proteins; Membrane Transport Proteins; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Oxidative Stress; Mutation; Time Factorsen
dc.titleStreptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicityen
dc.typeJournal articleen
dc.identifier.rmid0020123015en
dc.identifier.doi10.1128/JB.01393-12en
dc.identifier.pubid22571-
pubs.library.collectionMolecular and Biomedical Science publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidTrappetti, C. [0000-0001-8272-0068]en
dc.identifier.orcidPaton, J. [0000-0001-9807-5278]en
Appears in Collections:Molecular and Biomedical Science publications

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