Role of the manganese efflux system mntE for signalling and pathogenesis in Streptococcus pneumoniae
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Summary: The ability of bacteria to sense and respond to both environmental and intracellular metal concentrations plays an important role in pathogenesis. The acquisition of manganese is vital for the virulence of several bacterial species. Although manganese uptake systems have been well studied in bacteria, no manganese efflux system has yet been identified. In this study we have identified a cation diffusion facilitator (CDF) protein (Sp1552) of unknown substrate specificity that functions as a manganese export system in Streptococcus pneumoniae. We designated the gene for this manganese efflux system mntE and found that the mutant strain was highly sensitive to manganese stress. Although the mutant was more resistant to oxidative stress and produced more H 2 O 2 and pili, it had reduced virulence in a murine model of infection, indicating that manganese export plays a role in host pathogenesis. There was a distinct differential transcriptional response to extracellular and intracellular manganese accumulation. Our study indicates that manganese efflux is required for invasive disease and may provide a useful antimicrobial target to devise future therapeutics.
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Inactivation of MntE in S. pneumoniae reduces nasal colonization and bloodstream invasion in mice, despite increased resistance to reactive oxygen species.
“Inactivation of the manganese efflux protein MntE in S. pneumoniae reduces nasal colonization and bloodstream invasion in mice, despite an increased resistance to reactive oxygen species [142].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [142]
The manganese efflux protein MntE is required for S. pneumoniae pathogenesis in murine nasal passages and dissemination to blood.
“Similarly, the manganese efflux protein MntE is required for S. pneumoniae pathogenesis in murine nasal passages and dissemination to blood (116).”
From Transition Metals and Virulence in Bacteria (2016) · cites this paper as [116]
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- Authors
- Rosch, J. W., Gao, G., Ridout, G., Wang, Y., & Tuomanen, E. I.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Rosch, Jason W.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2009-03-19
- Volume
- 72
- Issue
- 1
- Pages
- 12-25
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- PMC
- PMC2706702
- OpenAlex
- W1496998265
- Cited by
- 134
- References
- 62
- Citations by year
- 2026: 2 · 2024: 7 · 2023: 7 · 2022: 6 · 2021: 6 · 2020: 12 · 2019: 10 · 2018: 4 · 2017: 11 · 2016: 7 · 2015: 11 · 2014: 7 · 2013: 11 · 2012: 10
- FWCI
- 6.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- American Lebanese Syrian Associated Charities
- National Institutes of Health
- National Heart, Lung, and Blood Institute (U54HL070590)
- National Institute of Allergy and Infectious Diseases (R01AI27913, R01AI027913)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Epidemiology › Pneumonia and Respiratory Infections
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Keywords
- Streptococcus pneumoniae, manganese efflux, MnTe, cation diffusion facilitator, manganese stress, oxidative stress resistance, hydrogen peroxide, fimbriae, virulence, invasive disease, transcriptional response, antimicrobial drug targets
- MeSH terms
- Animals, Bacterial Proteins, Homeostasis, Humans, Hydrogen Peroxide, Manganese, Mice, Inbred BALB C, Fimbriae, Bacterial, RNA, Bacterial, Streptococcus pneumoniae, Virulence, Gene Expression Regulation, Bacterial, Oxidative Stress, Oligonucleotide Array Sequence Analysis, Gene Expression Profiling, Mice, Facilitated Diffusion
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