ArticleJournal of bacteriology2015
Utilization of host iron sources by Corynebacterium diphtheriae: multiple hemoglobin-binding proteins are essential for the use of iron from the hemoglobin-haptoglobin complex.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- DtxR is a global iron-dependent regulatory protein with multiple roles in the control of gene expression inJournal of bacteriology · 2026Article
- Native Mass Spectrometry-Based Proteomics Reveals the Mechanism of Hemophore Release by PathogenicbioRxiv : the preprint server for biology · 2026Article
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Exoproteome and Surfaceome of ToxigenicJournal of proteome research · 2025Article
- Virulence and mutations analysis based on the whole genome of a BrazilianFrontiers in microbiology · 2025Article
- Review
- Phylogenomic analyses of multidrug resistant Corynebacterium striatum strains isolated from patients in a tertiary care hospital in the UK.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024Article
- Heme sequestration by hemophilin frommSphere · 2024Article
- Development and atomic structure of a new fluorescence-based sensor to probe heme transfer in bacterial pathogens.Journal of inorganic biochemistry · 2023Article
- Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance.Heliyon · 2023Review
- Analysis of the HbpA Protein from Corynebacterium diphtheriae Clinical Isolates and Identification of a Putative Hemoglobin-Binding Site on HbpA.Journal of bacteriology · 2022Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- The Corynebacterium diphtheriae HbpA Hemoglobin-Binding Protein Contains a Domain That Is Critical for Hemoprotein Binding, Cellular Localization, and Function.Journal of bacteriology · 2021Article
- Analysis of the Manganese and MntR Regulon in Corynebacterium diphtheriae.Journal of bacteriology · 2021Article
- Corynebacterium diphtheriae Iron-Regulated Surface Protein HbpA Is Involved in the Utilization of the Hemoglobin-Haptoglobin Complex as an Iron Source.Journal of bacteriology · 2018Article
- Article
- Genomic analysis of endemic clones of toxigenic and non-toxigenic Corynebacterium diphtheriae in Belarus during and after the major epidemic in 1990s.BMC genomics · 2017Article
- Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Journal of inorganic biochemistry · 2017Article
- Quantitative Proteomic Analysis Reveals Changes in the BenchmarkFrontiers in cellular and infection microbiology · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The use of hemin iron by Corynebacterium diphtheriae requires the DtxR- and iron-regulated ABC hemin transporter HmuTUV and the secreted Hb-binding protein HtaA. We recently described two surface anchored proteins, ChtA and ChtC, which also bind hemin and Hb. ChtA and ChtC share structural similarities to HtaA; however, a function for ChtA and ChtC was not determined. In this study, we identified additional host iron sources that are utilized by C. diphtheriae. We show that several C. diphtheriae strains use the hemoglobin-haptoglobin (Hb-Hp) complex as an iron source. We report that an htaA deletion mutant of C. diphtheriae strain 1737 is unable to use the Hb-Hp complex as an iron source, and we further demonstrate that a chtA-chtC double mutant is also unable to use Hb-Hp iron. Single-deletion mutants of chtA or chtC use Hb-Hp iron in a manner similar to that of the wild type. These findings suggest that both HtaA and either ChtA or ChtC are essential for the use of Hb-Hp iron. Enzyme-linked immunosorbent assay (ELISA) studies show that HtaA binds the Hb-Hp complex, and the substitution of a conserved tyrosine (Y361) for alanine in HtaA results in significantly reduced binding. C. diphtheriae was also able to use human serum albumin (HSA) and myoglobin (Mb) but not hemopexin as iron sources. These studies identify a biological function for the ChtA and ChtC proteins and demonstrate that the use of the Hb-Hp complex as an iron source by C. diphtheriae requires multiple iron-regulated surface components.
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