Metal Binding Specificity of the MntABC Permease of Neisseria gonorrhoeae and Its Influence on Bacterial Growth and Interaction with Cervical Epithelial Cells
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mntABC from Neisseria gonorrhoeae encodes an ABC permease which includes a periplasmic divalent cation binding receptor protein of the cluster IX family, encoded by mntC. Analysis of an mntC mutant showed that growth of N. gonorrhoeae could be stimulated by addition of either manganese(II) or zinc(II) ions, suggesting that the MntABC system could transport both ions. In contrast, growth of the mntAB mutant in liquid culture was possible only when the medium was supplemented with an antioxidant such as mannitol, consistent with the view that ion transport via MntABC is essential for protection of N. gonorrhoeae against oxidative stress. Using recombinant MntC, we determined that MntC binds Zn 2+and Mn 2+with almost equal affinity (dissociation constant of ∼0.1 μM). Competition assays with the metallochromic zinc indicator 4-(2-pyridylazo)resorcinol showed that MntC binds Mn 2+and Zn 2+at the same binding site. Analysis of the N. gonorrhoeae genome showed that MntC is the only Mn/Zn metal binding receptor protein cluster IX in this bacterium, in contrast to the situation in many other bacteria which have systems with dedicated Mn and Zn binding proteins as part of distinctive ABC cassette permeases. Both the mntC and mntAB mutants had reduced intracellular survival in a human cervical epithelial cell model and showed reduced ability to form a biofilm. These data suggest that the MntABC transporter is of importance for survival of Neisseria gonorrhoeae in the human host.
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Disruption of MntABC in Neisseria gonorrhoeae reduces intracellular survival and biofilm formation.
“Disruption of MntABC in Neisseria gonorrhoeae reduces intracellular survival and biofilm formation [153].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [153]
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- Authors
- Lim, K. H. L., Jones, C. E., vanden Hoven, R. N., Edwards, J. L., Falsetta, M. L., Apicella, M. A., Jennings, M. P., & McEwan, A. G.
- Affiliations
- The University of Queensland (AU)
- Australian Bacterial Pathogenesis Program and Centre for Metals in Biology, School of Molecular and Microbial Sciences, The University of Queensland, St. Lucia 4072, Australia
- Abigail Wexner Research Institute (US)
- University of Iowa (US)
- Corresponding author
- McEwan, Alastair G.
- ORCID
- Venue
- Infection and Immunity
- Publisher
- American Society for Microbiology
- Published
- 2008-08
- Volume
- 76
- Issue
- 8
- Pages
- 3569-3576
- ISSN
- 0019-9567 (ISSN-L)
- 1098-5522
- PMC
- PMC2493241
- OpenAlex
- W2115780465
- Cited by
- 72
- References
- 39
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 2 · 2023: 4 · 2022: 6 · 2021: 2 · 2020: 2 · 2019: 5 · 2018: 1 · 2017: 4 · 2016: 2 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 4
- FWCI
- 3.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Infection and Immunity (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Nationwide Children's Hospital
- National Institutes of Health
- Research Institute, Nationwide Children's Hospital
- Medical Research Council
- National Health and Medical Research Council
- National Institute of Allergy and Infectious Diseases (R01AI045728, AI045728)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Keywords
- Neisseria gonorrhoeae, ABC transporters, manganese transport, zinc transport, oxidative stress, antioxidant defense, biofilm formation, cervical epithelial cells, metallochromic indicators
- MeSH terms
- Bacterial Proteins, Binding Sites, Cations, Divalent, Cell Line, Cervix Uteri, Epithelial Cells, Female, Humans, Kinetics, Metals, Neisseria gonorrhoeae, Biofilms, Membrane Transport Proteins, Periplasmic Binding Proteins
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