ArticlePloS one2013
Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Regulation of iron ion homeostasis inmBio · 2026Review
- Ferruginous hemeprotein HhuH facilitates the cadmium adsorption and chromium reduction inApplied and environmental microbiology · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Engineered skin bacteria induce antitumor T cell responses against melanoma.Science (New York, N.Y.) · 2023Article
- Air pollution induces Staphylococcus aureus USA300 respiratory tract colonization mediated by specific bacterial genetic responses involving the global virulence gene regulators Agr and Sae.Environmental microbiology · 2022Article
- Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- The Role of Iron inFrontiers in cell and developmental biology · 2022Review
- Identification of the iron-limitation stimulon in Staphylococcus lugdunensis.Archives of microbiology · 2021Article
- DyP-Type Peroxidases: Recent Advances and Perspectives.International journal of molecular sciences · 2021Review
- Interaction analyses based on growth parameters of GWAS between Escherichia coli and Staphylococcus aureus.AMB Express · 2021Article
- Transcriptome Analysis of Gene Expression inMicroorganisms · 2020Article
- Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.International journal of molecular sciences · 2020Review
- Article
- Quantitative proteomic analysis of cell envelope preparations under iron starvation stress in Aeromonas hydrophila.BMC microbiology · 2016Article
- The Iron age of host-microbe interactions.EMBO reports · 2015Review
- An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.Archives of biochemistry and biophysics · 2015Review
- Protoporphyrin (PPIX) efflux by the MacAB-TolC pump in Escherichia coli.MicrobiologyOpen · 2014Article
- Identification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHA.PLoS neglected tropical diseases · 2014Article
- Characterization of a Mycobacterium tuberculosis nanocompartment and its potential cargo proteins.The Journal of biological chemistry · 2014Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EfeUOB-like tripartite systems are widespread in bacteria and in many cases they are encoded by genes organized into iron-regulated operons. They consist of: EfeU, a protein similar to the yeast iron permease Ftrp1; EfeO, an extracytoplasmic protein of unknown function and EfeB, also an extracytoplasmic protein with heme peroxidase activity, belonging to the DyP family. Many bacterial EfeUOB systems have been implicated in iron uptake, but a prefential iron source remains undetermined. Nevertheless, in the case of Escherichia coli, the EfeUOB system has been shown to recognize heme and to allow extracytoplasmic heme iron extraction via a deferrochelation reaction. Given the high level of sequence conservations between EfeUOB orthologs, we hypothesized that heme might be the physiological iron substrate for the other orthologous systems. To test this hypothesis, we undertook characterization of the Staphylococcus aureus FepABC system. Results presented here indicate: i) that the S. aureus FepB protein binds both heme and PPIX with high affinity, like EfeB, the E. coli ortholog; ii) that it has low peroxidase activity, comparable to that of EfeB; iii) that both FepA and FepB drive heme iron utilization, and both are required for this activity and iv) that the E. coli FepA ortholog (EfeO) cannot replace FepA in FepB-driven iron release from heme indicating protein specificity in these activities. Our results show that the function in heme iron extraction is conserved in the two orthologous systems.
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