Siderophore-mediated iron acquisition in the staphylococci
Abstract
Iron is frequently a growth-limiting nutrient due to its propensity to interact with oxygen to form insoluble precipitates and, therefore, biological systems have evolved specialized uptake mechanisms to obtain this essential nutrient. Many pathogenic bacteria are capable of obtaining stringently sequestered iron from animal hosts by one or both of the following mechanisms: extraction of heme from host erythrocyte and serum hemoproteins, or through the use of high affinity, iron-scavenging molecules termed siderophores. This review summarizes our current knowledge of siderophore-mediated iron acquisition systems in the genus Staphylococcus.
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Staphyloferrin B is structurally different from staphyloferrin A but is also a hydrophilic NIS siderophore.
“Staphyloferrin B is structurally distinct from staphyloferrin A but like staphyloferrin A is a hydrophilic NIS siderophore.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [61]
After binding iron, staphyloferrin A and staphyloferrin B are imported into the cytoplasm by HtsABC and SirABC, respectively.
“Upon binding iron, both staphyloferrin A and staphyloferrin B are transported into the cytoplasm through the ABC transporters HtsABC and the staphylococcal iron regulated transporter (SirABC), respectively [61].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [61]
Siderophore-iron complexes are taken back into the cytoplasm by dedicated ABC transporters.
“Siderophore-iron complexes are then transported back into the cytoplasm through dedicated ABC transporters [61].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [61]
The sbn locus contains the genes for staphyloferrin B synthesis and has a consensus Fur box in its operator region.
“The genes encoding the enzymatic machinery required for staphyloferrin B synthesis lie within the sbn locus which has a consensus fur box within the operator region for the operon [61].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [61]
S. aureus makes two siderophores, staphyloferrin A and staphyloferrin B, both through the NIS pathway, and secretes them.
“S. aureus encodes for two siderophores, staphyloferrin A and staphyloferrin B, and both are synthesized through the NIS pathway and then secreted into the extracellular milieu.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [61]
Staphyloferrin B has been found in supernatants of S. aureus and several coagulase-negative staphylococci and Gram-negative bacteria.
“Staphyloferrin B has been identified in the supernatants of S. aureus as well as several coagulase-negative staphylococci and Gram negative bacteria [61].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [61]
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“A more thorough discussion on both siderophore synthesis and the contribution of siderophores to staphylococcal pathogenesis can be found in [61].”
BackgroundMethodInfluentialStaphylococcus aureus heme and siderophore-iron acquisition pathways
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Self-citation
- Authors
- Beasley, F. C., & Heinrichs, D. E.
- Affiliations
- Western University (CA)
- Corresponding author
- Heinrichs, David E.
- ORCID
- Heinrichs, David E.
- Venue
- Journal of Inorganic Biochemistry
- Publisher
- Elsevier BV
- Published
- 2010-03
- Volume
- 104
- Issue
- 3
- Pages
- 282-288
- ISSN
- 0162-0134 (ISSN-L)
- OpenAlex
- W2000785657
- Cited by
- 90
- References
- 76
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 8 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 1 · 2019: 7 · 2018: 4 · 2017: 6 · 2016: 7 · 2015: 7 · 2014: 10 · 2013: 4 · 2012: 7
- FWCI
- 3.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Inorganic Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- siderophores, iron acquisition, Staphylococcus, heme acquisition, heme proteins, bacterial pathogenicity, host-pathogen interaction
- MeSH terms
- Animals, Bacterial Proteins, Citrates, Humans, Iron, Models, Molecular, Ornithine, Protein Conformation, Staphylococcus, Molecular Structure, Siderophores
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