Cited by 263Bacterial Infections and VaccinesBacterial Genetics and BiotechnologyIron Metabolism and Disorders

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Structural basis for iron piracy by pathogenic Neisseria

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Noinaj, Nicholas, Easley, Nicole C., Oke, Muse, Mizuno, Naoko, Gumbart, James, Boura, Evzen, Steere, Ashley N., Zak, Olga, Aisen, Philip, Tajkhorshid, Emad, Evans, Robert W., Gorringe, Andrew R., Mason, Anne B., Steven, Alasdair C., Buchanan, Susan K.·2012·Nature

DOI 10.1038/nature10823PMC PMC3292680

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Abstract

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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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: Noinaj, Nicholas
Oke, Muse
Mizuno, Naoko
Gumbart, James
Tajkhorshid, Emad
Evans, Robert W.
Gorringe, Andrew R.
Mason, Anne B.
Steven, Alasdair C.
Buchanan, Susan K.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2012-02-12
Volume: 483
Issue: 7387
Pages: 53-58
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature10823
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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Structural basis for iron piracy by pathogenic Neisseria

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