Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/89991
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Type: Journal article
Title: Overlapping functionality of the Pht proteins in zinc homeostasis of Streptococcus pneumoniae
Author: Plumptre, C.
Hughes, C.
Harvey, R.
Eijkelkamp, B.
McDevitt, C.
Paton, J.
Citation: Infection and Immunity, 2014; 82(10):4315-4324
Publisher: American Society for Microbiology
Issue Date: 2014
ISSN: 0019-9567
1098-5522
Statement of
Responsibility: 
Charles D. Plumptre, Catherine E. Hughes, Richard M. Harvey, Bart A. Eijkelkamp, Christopher A. McDevitt, James C. Paton
Abstract: Streptococcus 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.
Keywords: Animals; Mice; Streptococcus pneumoniae; Zinc; Bacterial Proteins; Homeostasis; Virulence; Microbial Viability; Gene Deletion; Female
Rights: Copyright © 2014, American Society for Microbiology. All Rights Reserved.
RMID: 0030008795
DOI: 10.1128/IAI.02155-14
Grant ID: http://purl.org/au-research/grants/nhmrc/565526
http://purl.org/au-research/grants/nhmrc/1022240
http://purl.org/au-research/grants/arc/DP120101432
http://purl.org/au-research/grants/arc/DP120103957
Appears in Collections:Molecular and Biomedical Science publications

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