Immune Interference in Mycobacterium tuberculosis Intracellular Iron Acquisition through Siderocalin Recognition of Carboxymycobactins
Open accessAbstract
The innate immune system antibacterial protein Siderocalin (Scn) binds ferric carboxymycobactin (CMB) and also several catecholate siderophores. Although the recognition of catecholates by Scn has been thoroughly investigated, the binding interactions of Scn with the full spectrum of CMB isoforms have not been studied. Here we show that Scn uses different binding modes for the limited subset of bound CMB isoforms, resulting in a range of binding affinities that are much weaker than other siderophore targets of Scn. Understanding the binding interaction between Scn and CMBs provides clues for the influence of Scn on mycobacterial iron acquisition.
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NGAL binds enterobactin and, to a lesser extent, M. tuberculosis carboxymycobactins.
“NGAL binds enterobactin, the prototypical catecholate siderophore of E. coli, and to a lesser extent M. tuberculosis' carboxymycobactins (Flo et al., 2004;Hoette et al., 2011).”
From Iron in infection and immunity (2020) · cites this paper as Hoette et al., 2011
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- Authors
- Hoette, T. M., Clifton, M. C., Zawadzka, A. M., Holmes, M. A., Strong, R. K., & Raymond, K. N.
- Affiliations
- University of California, Berkeley (US)
- Fred Hutch Cancer Center (US)
- Corresponding author
- Strong, Roland K.
- Raymond, Kenneth N.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-10-21
- Volume
- 6
- Issue
- 12
- Pages
- 1327-1331
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- PMC
- PMC3241878
- OpenAlex
- W2047735270
- Cited by
- 31
- References
- 30
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2021: 1 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 6 · 2014: 3 · 2013: 4 · 2012: 2
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- ACS Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- U.S. Department of Energy (-AC02-05CH11231, 05CH11231, DE-AC02-)
- National Institutes of Health
- Office of Science (DEAC02–05CH11231, AC02-05CH11231, DE-AC02)
- National Institute of Allergy and Infectious Diseases (R01AI11744, R01AI011744, R01AI59432, R01AI059432)
- Basic Energy Sciences (DE-AC02, DE-AC02-05CH11231., AC02–05CH11231)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Keywords
- siderocalin, Mycobacterium tuberculosis, iron acquisition, siderophore binding, innate immunity, catecholate siderophores, binding affinity, host-pathogen interaction, iron sequestration
- MeSH terms
- Lipocalin-2, Acute-Phase Proteins, Carrier Proteins, Humans, Immunity, Innate, Iron, Iron Chelating Agents, Models, Molecular, Molecular Conformation, Mycobacterium tuberculosis, Oxazoles, Proto-Oncogene Proteins, Lipocalins, Static Electricity
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