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Structural basis for iron piracy by pathogenic Neisseria
Open accessAbstract
Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system consists of TbpA, an integral outer membrane protein, and TbpB, a co-receptor attached to the cell surface; both proteins are potentially important vaccine and therapeutic targets. Two key questions driving Neisseria research are how human transferrin is specifically targeted, and how the bacteria liberate iron from transferrin at neutral pH. To address these questions, we solved crystal structures of the TbpA-transferrin complex and of the corresponding co-receptor TbpB. We characterized the TbpB-transferrin complex by small-angle X-ray scattering and the TbpA-TbpB-transferrin complex by electron microscopy. Our studies provide a rational basis for the specificity of TbpA for human transferrin, show how TbpA promotes iron release from transferrin, and elucidate how TbpB facilitates this process.
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“The uptake of transferrin by Neisseria species is specific to hominid transferrin, indicating that this specialized uptake mechanism facilitates their residence in the human host and several other hominids83.”
From Iron homeostasis in host defence and inflammation (2015) · cites this paper as [83]
In the citing paper
“TbpA and TbpB are induced along with several other proteins in the outer membranes of N. meningitidis under Fe-restricted conditions [30].”
From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [30]
In the citing paper
“In the case of Neisseria iron is extracted from the C-lobe of transferrin even at neutral pH”
From Iron in immune cell function and host defense (2021) · cites this paper as [15]
In the citing paper
“transferrin-binding protein A (TbpA), an important virulence factor in several human pathogens including Neisseria meningitidis, Neisseria gonorrhoeae, Haemophilus influenzae, and Moraxella catarrhalis, as well as a number of agricultural pathogens (Figure 2A) 21, 37, 38, 39, 40, 41.”
From Buried Treasure: Evolutionary Perspectives on Microbial Iron Piracy (2015) · cites this paper as [41]
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Metadata
- Authors
- Noinaj, N., Easley, N. C., Oke, M., Mizuno, N., Gumbart, J., Boura, E., Steere, A. N., Zak, O., Aisen, P., Tajkhorshid, E., Evans, R. W., Gorringe, A. R., Mason, A. B., Steven, A. C., & Buchanan, S. K.
- Affiliations
- National Institutes of Health (US)
- Argonne National Laboratory (US)
- University of Vermont (US)
- Albert Einstein College of Medicine (US)
- University of Illinois Urbana-Champaign (US)
- Brunel University of London (GB)
- Health Protection Agency (GB)
- Corresponding author
- Buchanan, Susan K.
- ORCID
- Venue
- Nature
- Published
- 2012-02-12
- Volume
- 483
- Issue
- 7387
- Pages
- 53-58
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3292680
- OpenAlex
- W2170163556
- Cited by
- 262
- References
- 54
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 12 · 2023: 13 · 2022: 17 · 2021: 11 · 2020: 22 · 2019: 19 · 2018: 14 · 2017: 28 · 2016: 23 · 2015: 26 · 2014: 19 · 2013: 21 · 2012: 17
- FWCI
- 23.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (P41GM104601, R01GM086749, U54GM087519)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK21739, ZIADK036143, R01DK021739)
- National Center for Research Resources (P41 RR-05969, P41RR005969)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- Neisseria, iron acquisition, transferrin, TbpA, TbpB, outer membrane proteins, co-receptors, crystal structure, small-angle X-ray scattering, electron microscopy, vaccine targets, therapeutic target
- MeSH terms
- Animals, Apoproteins, Bacterial Proteins, Binding Sites, Biological Transport, Cattle, Humans, Iron, Models, Molecular, Neisseria, Protein Conformation, Species Specificity, Structure-Activity Relationship, Transferrin, X-Ray Diffraction, Crystallography, X-Ray, Transferrin-Binding Protein A, Transferrin-Binding Protein B, Mice, Scattering, Small Angle, Molecular Dynamics Simulation
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