ArticlePloS one2012
Purification and structural characterization of siderophore (corynebactin) from Corynebacterium diphtheriae.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
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- Third Generation Genome Sequencing of the Endobacterium Corynebacterium kroppenstedtii subsp. demodicis Reveals Details of Its Microbe-Host-Interaction With the Most Complex Human Commensal, Demodex folliculorum.Environmental microbiology reports · 2026Article
- DtxR is a global iron-dependent regulatory protein with multiple roles in the control of gene expression inJournal of bacteriology · 2026Article
- Microbial Siderophores: A New Insight on Healthcare Applications.BME frontiers · 2025Review
- A Practical Toolkit for the Detection, Isolation, Quantification, and Characterization of Siderophores and Metallophores in Microorganisms.ACS omega · 2024Review
- SIDERITE: Unveiling hidden siderophore diversity in the chemical space through digital exploration.iMeta · 2024Article
- Uropathogenic Escherichia coli wield enterobactin-derived catabolites as siderophores.The Journal of biological chemistry · 2024Article
- UropathogenicbioRxiv : the preprint server for biology · 2023Article
- Ribonuclease J-Mediated mRNA Turnover Modulates Cell Shape, Metabolism and Virulence inMicroorganisms · 2021Article
- Recent developments in siderotyping: procedure and application.World journal of microbiology & biotechnology · 2020Review
- Siderophore-Mediated Interactions Determine the Disease Suppressiveness of Microbial Consortia.mSystems · 2020Article
- NEAr Transporter (NEAT) Domains: Unique Surface Displayed Heme Chaperones That Enable Gram-Positive Bacteria to Capture Heme-Iron From Hemoglobin.Frontiers in microbiology · 2020Review
- Citryl Ornithine Is an Intermediate in a Three-Step Biosynthetic Pathway for Rhizoferrin inACS chemical biology · 2019Article
- Article
- Structural and functional delineation of aerobactin biosynthesis in hypervirulentThe Journal of biological chemistry · 2018Article
- The commensal lifestyle of Staphylococcus aureus and its interactions with the nasal microbiota.Nature reviews. Microbiology · 2017Review
- Iron and Virulence inFrontiers in cellular and infection microbiology · 2017Review
- Alternative pathways utilize or circumvent putrescine for biosynthesis of putrescine-containing rhizoferrin.The Journal of biological chemistryArticle
- Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
During infection, Corynebacterium diphtheriae must compete with host iron-sequestering mechanisms for iron. C. diphtheriae can acquire iron by a siderophore-dependent iron-uptake pathway, by uptake and degradation of heme, or both. Previous studies showed that production of siderophore (corynebactin) by C. diphtheriae is repressed under high-iron growth conditions by the iron-activated diphtheria toxin repressor (DtxR) and that partially purified corynebactin fails to react in chemical assays for catecholate or hydroxamate compounds. In this study, we purified corynebactin from supernatants of low-iron cultures of the siderophore-overproducing, DtxR-negative mutant strain C. diphtheriae C7(β) ΔdtxR by sequential anion-exchange chromatography on AG1-X2 and Source 15Q resins, followed by reverse-phase high-performance liquid chromatography (RP-HPLC) on Zorbax C8 resin. The Chrome Azurol S (CAS) chemical assay for siderophores was used to detect and measure corynebactin during purification, and the biological activity of purified corynebactin was shown by its ability to promote growth and iron uptake in siderophore-deficient mutant strains of C. diphtheriae under iron-limiting conditions. Mass spectrometry and NMR analysis demonstrated that corynebactin has a novel structure, consisting of a central lysine residue linked through its α- and ε- amino groups by amide bonds to the terminal carboxyl groups of two different citrate residues. Corynebactin from C. diphtheriae is structurally related to staphyloferrin A from Staphylococcus aureus and rhizoferrin from Rhizopus microsporus in which d-ornithine or 1,4-diaminobutane, respectively, replaces the central lysine residue that is present in corynebactin.
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