Bacterial iron homeostasis
Open accessAbstract
Iron is essential to virtually all organisms, but poses problems of toxicity and poor solubility. Bacteria have evolved various mechanisms to counter the problems imposed by their iron dependence, allowing them to achieve effective iron homeostasis under a range of iron regimes. Highly efficient iron acquisition systems are used to scavenge iron from the environment under iron-restricted conditions. In many cases, this involves the secretion and internalisation of extracellular ferric chelators called siderophores. Ferrous iron can also be directly imported by the G protein-like transporter, FeoB. For pathogens, host-iron complexes (transferrin, lactoferrin, haem, haemoglobin) are directly used as iron sources. Bacterial iron storage proteins (ferritin, bacterioferritin) provide intracellular iron reserves for use when external supplies are restricted, and iron detoxification proteins (Dps) are employed to protect the chromosome from iron-induced free radical damage. There is evidence that bacteria control their iron requirements in response to iron availability by down-regulating the expression of iron proteins during iron-restricted growth. And finally, the expression of the iron homeostatic machinery is subject to iron-dependent global control ensuring that iron acquisition, storage and consumption are geared to iron availability and that intracellular levels of free iron do not reach toxic levels.
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E. coli has an iron content of 10^5-10^6 molecules per cell.
“For comparison, E. coli has an iron content of 10 5 -10 6 molecules per cell (Andrews et al., 2003).”
From Iron in infection and immunity (2020) · cites this paper as Andrews et al., 2003
Section 2.1 (Introduction) gives the same numerical range for E. coli iron content, depending on growth conditions. It counts iron atoms per cell, however, not molecules per cell. (LLM, conf=0.88)
Experimental — accuracy not yet measuredBacterial pathogens store iron in one of three types of proteins: ferritin, bacterioferritins, and Dps proteins.
“Bacterial pathogens store iron in one of three types of proteins: ferritin, bacterioferritins, and Dps proteins.”
From Iron in infection and immunity (2013) · cites this paper as Andrews et al., 2003
Binding of Fur-Fe2+ and DtxR-Fe2+ upstream of iron uptake and storage operons/genes inhibits their transcription under iron-replete conditions.
“Binding of Fur–Fe2+ and DtxR–Fe2+ upstream of iron uptake and storage operons/genes inhibits their transcription under iron‐replete conditions. 56 , 61”
From The battle for iron in enteric infections (2020) · cites this paper as [61]
Central to iron homeostasis in Salmonella is Fur, which controls essential mechanisms of iron uptake and storage.
“Central to iron homeostasis in Salmonella is Fur, which controls essential mechanisms of iron uptake and storage. 61 , 62”
From The battle for iron in enteric infections (2020) · cites this paper as [61]
Free iron is scarce in the host, an innate immune defense known as nutritional immunity.
“In the host, however, free iron is scarce, an innate immune defense strategy of the host known as “nutritional immunity” (Andrews et al., 2003; Schaible and Kaufmann, 2004; Weinberg, 1975).”
From Staphylococcus aureus Targets the Duffy Antigen Receptor for Chemokines (DARC) to Lyse Erythrocytes (2015) · cites this paper as Andrews et al., 2003
Several pathogens are able to acquire transferrin-bound iron.
“In addition, several pathogens are able to acquire TF-bound iron [51–54].”
From Iron deficiency or anemia of inflammation?: Differential diagnosis and mechanisms of anemia of inflammation (2016) · cites this paper as [51]
Four regulatory modes of Fur have been identified: apo-Fur activation, apo-Fur repression, holo-Fur activation, and holo-Fur repression.
“The four regulatory modes of Fur have been identified: apo-Fur activation, apo-Fur repression, holo-Fur activation, and holo-Fur repression ( 28 , 60 , 62 ).”
From YdiV regulates Escherichia coli ferric uptake by manipulating the DNA-binding ability of Fur in a SlyD-dependent manner (2020) · cites this paper as [60]
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- Authors
- Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F.
- Affiliations
- University of Reading (GB)
- Corresponding author
- Andrews, Simon C.
- ORCID
- Andrews, Simon C.
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-06
- Volume
- 27
- Issue
- 2-3
- Pages
- 215-237
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2014723793
- Cited by
- 2,702
- References
- 185
- Citations by year
- 2026: 116 · 2025: 142 · 2024: 139 · 2023: 147 · 2022: 153 · 2021: 179 · 2020: 151 · 2019: 138 · 2018: 122 · 2017: 118 · 2016: 126 · 2015: 117 · 2014: 141 · 2013: 96 · 2012: 111
- FWCI
- 7.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEMS Microbiology Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- siderophores, iron acquisition, transferrin, lactoferrin, heme, ferritin, bacterioferritin, Dps protein, iron limitation, iron toxicity, iron storage
- MeSH terms
- Bacteria, Bacterial Proteins, DNA-Binding Proteins, Escherichia coli, Heme, Homeostasis, Iron, Models, Genetic, Gene Expression Regulation, Bacterial, Siderophores, Protein Structure, Tertiary
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