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Review
. 2013 Dec 4:3:92.
doi: 10.3389/fcimb.2013.00092. eCollection 2013.

The roles of transition metals in the physiology and pathogenesis of Streptococcus pneumoniae

Erin S Honsa  1 , Michael D L Johnson  1 , Jason W Rosch  1
Affiliations
Review

The roles of transition metals in the physiology and pathogenesis of Streptococcus pneumoniae

Erin S Honsa et al. Front Cell Infect Microbiol. .

Abstract

For bacterial pathogens whose sole environmental reservoir is the human host, the acquisition of essential nutrients, particularly transition metals, is a critical aspect of survival due to tight sequestration and limitation strategies deployed to curtail pathogen outgrowth. As such, these bacteria have developed diverse, specialized acquisition mechanisms to obtain these metals from the niches of the body in which they reside. To oppose the spread of infection, the human host has evolved multiple mechanisms to counter bacterial invasion, including sequestering essential metals away from bacteria and exposing bacteria to lethal concentrations of metals. Hence, to maintain homeostasis within the host, pathogens must be able to acquire necessary metals from host proteins and to export such metals when concentrations become detrimental. Furthermore, this acquisition and efflux equilibrium must occur in a tissue-specific manner because the concentration of metals varies greatly within the various microenvironments of the human body. In this review, we examine the functional roles of the metal import and export systems of the Gram-positive pathogen Streptococcus pneumoniae in both signaling and pathogenesis.

Keywords: Streptococcus pneumoniae; infection; metal transport; pathogenesis; virulence factors.

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Figures

Figure 1
Figure 1
Summary of the metal uptake and efflux systems of pneumococcus. Transporters and their respective substrates are indicated in blue. The regulators that respond to the respective metals are indicated in red. As a point of reference, the levels of the discussed metals at various host sites in both naïve and infected animals are provided in the corners of the diagram (McDevitt et al., 2011).
See this image and copyright information in PMC

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References

    1. Andreini C., Bertini I., Cavallaro G., Holliday G. L., Thornton J. M. (2008). Metal ions in biological catalysis: from enzyme databases to general principles. J. Biol. Inorg. Chem. 13, 1205–1218 10.1007/s00775-008-0404-5 - DOI - PubMed
    1. Azzouzi A., Steunou A. S., Durand A., Khalfaoui-Hassani B., Bourbon M. L., Astier C., et al. (2013). Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu-ATPase mutant copA of Rubrivivax gelatinosus. Mol. Microbiol. 88, 339–351 10.1111/mmi.12188 - DOI - PubMed
    1. Balogun R. A., Ogunniyi A., Sanford K., Okafor C., Lobo P. I., Siami G., et al. (2010). Therapeutic apheresis in special populations. J. Clin. Apher. 25, 265–274 10.1002/jca.20250 - DOI - PubMed
    1. Barre O., Mourlane F., Solioz M. (2007). Copper induction of lactate oxidase of Lactococcus lactis: a novel metal stress response. J. Bacteriol. 189, 5947–5954 10.1128/JB.00576-07 - DOI - PMC - PubMed
    1. Batinic-Haberle I., Liochev S. I., Spasojevic I., Fridovich I. (1997). A potent superoxide dismutase mimic: manganese beta-octabromo-meso-tetrakis-(N-methylpyridinium-4-yl) porphyrin. Arch. Biochem. Biophys. 343, 225–233 10.1006/abbi.1997.0157 - DOI - PubMed

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