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dc.contributor.authorA. Gould, Katherineen_US
dc.contributor.authorA. McDevitt, Christopheren_US
dc.contributor.authorB. Van der Hoek, Marken_US
dc.contributor.authorG. McEwan, Alastairen_US
dc.contributor.authorHoffmann, Peteren_US
dc.contributor.authorJ. Bagley, Christopheren_US
dc.contributor.authorJennings, Michaelen_US
dc.contributor.authorK. Mahdi, Laylaen_US
dc.contributor.authorOgunniyi, Abiodun D.en_US
dc.contributor.authorPaton, James C.en_US
dc.date.accessioned2017-04-04T16:29:36Z
dc.date.available2017-04-04T16:29:36Z
dc.date.issued2010en_US
dc.date.modified2011-01-27T06:45:27Z
dc.identifier.issn00219193en_US
dc.identifier.doi10.1128/JB.00064-10en_AU
dc.identifier.urihttp://hdl.handle.net/10072/35816
dc.description.abstractThe importance of Mn2+ for pneumococcal physiology and virulence has been studied extensively. However, the specific cellular role(s) for which Mn2+ is required are yet to be fully elucidated. Here, we analyzed the effect of Mn2+ limitation on the transcriptome and proteome of Streptococcus pneumoniae D39. This was carried out by comparing a deletion mutant lacking the solute binding protein of the high-affinity Mn2+ transporter, pneumococcal surface antigen A (PsaA), with its isogenic wild-type counterpart. We provide clear evidence for the Mn2+-dependent regulation of the expression of oxidative-stress-response enzymes SpxB and Mn2+-SodA and virulence-associated genes pcpA and prtA. We also demonstrate the upregulation of at least one oxidative- and nitrosative-stress-response gene cluster, comprising adhC, nmlR, and czcD, in response to Mn2+ stress. A significant increase in 6-phosphogluconate dehydrogenase activity in the psaA mutant grown under Mn2+-replete conditions and upregulation of an oligopeptide ABC permease (AppDCBA) were also observed. Together, the results of transcriptomic and proteomic analyses provided evidence for Mn2+ having a central role in activating or stimulating enzymes involved in central carbon and general metabolism. Our results also highlight the importance of high-affinity Mn2+ transport by PsaA in pneumococcal competence, physiology, and metabolism and elucidate mechanisms underlying the response to Mn2+ stress.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherAmerican Society for Microbiologyen_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom4489en_US
dc.relation.ispartofpageto4497en_US
dc.relation.ispartofissue17en_AU
dc.relation.ispartofjournalJournal of Bacteriologyen_US
dc.relation.ispartofvolume192en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchMedical Microbiology not elsewhere classifieden_US
dc.subject.fieldofresearchcode110899en_US
dc.titleCentral Role of Manganese in Regulation of Stress Responses, Physiology, and Metabolism in Streptococcus pneumoniaeen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2010
gro.hasfulltextNo Full Text


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