Cited by 90Bacterial Genetics and BiotechnologyAntimicrobial Resistance in StaphylococcusIron Metabolism and Disorders

Siderophore-mediated iron acquisition in the staphylococci

Beasley, Federico C., Heinrichs, David E.·2010·Journal of Inorganic Biochemistry

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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Crossref · 10.1016/j.jinorgbio.2009.09.011

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76 of 76 references verified0 citation errors · 0 not checkable

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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.”
  • 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].”
  • 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].”
  • 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].”
  • 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.”

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Authors
Beasley, F. C., & Heinrichs, D. E.
Affiliations
Western University (CA)
Corresponding author
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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