Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/89991
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dc.contributor.authorPlumptre, C.en
dc.contributor.authorHughes, C.en
dc.contributor.authorHarvey, R.en
dc.contributor.authorEijkelkamp, B.en
dc.contributor.authorMcDevitt, C.en
dc.contributor.authorPaton, J.en
dc.date.issued2014en
dc.identifier.citationInfection and Immunity, 2014; 82(10):4315-4324en
dc.identifier.issn0019-9567en
dc.identifier.issn1098-5522en
dc.identifier.urihttp://hdl.handle.net/2440/89991-
dc.description.abstractStreptococcus pneumoniae is a globally significant pathogen that causes a range of diseases, including pneumonia, sepsis, meningitis, and otitis media. Its ability to cause disease depends upon the acquisition of nutrients from its environment, including transition metal ions such as zinc. The pneumococcus employs a number of surface proteins to achieve this, among which are four highly similar polyhistidine triad (Pht) proteins. It has previously been established that these proteins collectively aid in the delivery of zinc to the ABC transporter substrate-binding protein AdcAII. Here we have investigated the contribution of each individual Pht protein to pneumococcal zinc homeostasis by analyzing mutant strains expressing only one of the four pht genes. Under conditions of low zinc availability, each of these mutants showed superior growth and zinc accumulation profiles relative to a mutant strain lacking all four genes, indicating that any of the four Pht proteins are able to facilitate delivery of zinc to AdcAII. However, optimal growth and zinc accumulation in vitro and pneumococcal survival and proliferation in vivo required production of all four Pht proteins, indicating that, despite their overlapping functionality, the proteins are not dispensable without incurring a fitness cost. We also show that surface-attached forms of the Pht proteins are required for zinc recruitment and that they do not contribute to defense against extracellular zinc stress.en
dc.description.statementofresponsibilityCharles D. Plumptre, Catherine E. Hughes, Richard M. Harvey, Bart A. Eijkelkamp, Christopher A. McDevitt, James C. Patonen
dc.language.isoenen
dc.publisherAmerican Society for Microbiologyen
dc.rightsCopyright © 2014, American Society for Microbiology. All Rights Reserved.en
dc.subjectAnimals; Mice; Streptococcus pneumoniae; Zinc; Bacterial Proteins; Homeostasis; Virulence; Microbial Viability; Gene Deletion; Femaleen
dc.titleOverlapping functionality of the Pht proteins in zinc homeostasis of Streptococcus pneumoniaeen
dc.typeJournal articleen
dc.identifier.rmid0030008795en
dc.identifier.doi10.1128/IAI.02155-14en
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/565526en
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1022240en
dc.relation.granthttp://purl.org/au-research/grants/arc/DP120101432en
dc.relation.granthttp://purl.org/au-research/grants/arc/DP120103957en
dc.identifier.pubid85648-
pubs.library.collectionMolecular and Biomedical Science publicationsen
pubs.library.teamDS04en
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidEijkelkamp, B. [0000-0003-0179-8977]en
dc.identifier.orcidMcDevitt, C. [0000-0003-1596-4841]en
dc.identifier.orcidPaton, J. [0000-0001-9807-5278]en
Appears in Collections:Molecular and Biomedical Science publications

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