ArticleBiochemistry2011
Unique heme-iron coordination by the hemoglobin receptor IsdB of Staphylococcus aureus.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 91 citations in OpenAlex.
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Hemoglobin receptor redundancy inJournal of structural biology: X · 2025Article
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Development of a bivalent protein subunit vaccine against infection by Pseudomonas aeruginosa and Staphylococcus aureus.NPJ vaccines · 2025Article
- Time-resolved X-ray solution scattering unveils the events leading to hemoglobin heme capture by staphylococcal IsdB.Nature communications · 2025Article
- Identification of small molecules affecting the interaction between human hemoglobin and Staphylococcus aureus IsdB hemophore.Scientific reports · 2024Article
- TLR4 sensing of IsdB ofmBio · 2024Article
- Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance.Heliyon · 2023Review
- Cryo-EM structures of staphylococcal IsdB bound to human hemoglobin reveal the process of heme extraction.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Axial Heme Coordination by the Tyr-His Motif in the Extracellular Hemophore HasAp Is Critical for the Release of Heme to the HasR Receptor ofBiochemistry · 2021Article
- Immunodominance of Epitopes and Protective Efficacy of HI Antigen Are Differentially Altered Using Different Adjuvants in a Mouse Model ofFrontiers in immunology · 2021Article
- Antibiotic Combined with Epitope-Specific Monoclonal Antibody Cocktail Protects Mice Against Bacteremia and Acute Pneumonia from Methicillin-ResistantJournal of inflammation research · 2021Article
- Article
- NEAr Transporter (NEAT) Domains: Unique Surface Displayed Heme Chaperones That Enable Gram-Positive Bacteria to Capture Heme-Iron From Hemoglobin.Frontiers in microbiology · 2020Review
- The Role of Gram-Positive Surface Proteins in Bacterial Niche- and Host-Specialization.Frontiers in microbiology · 2020Review
- Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight.Scientific reports · 2019Article
- HumanmBio · 2019Article
- NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.Protein science : a publication of the Protein Society · 2019Article
- Post-transcriptional regulation of theThe Journal of biological chemistry · 2019Article
- TheThe Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Iron is an essential requirement for life for nearly all organisms. The human pathogen Staphylococcus aureus is able to acquire iron from the heme cofactor of hemoglobin (Hb) released from lysed erythrocytes. IsdB, the predominant Hb receptor of S. aureus, is a cell wall-anchored protein that is composed of two NEAT domains. The N-terminal NEAT domain (IsdB-N1) binds Hb, and the C-terminal NEAT domain (IsdB-N2) relays heme to IsdA for transport into the cell. Here we present the 1.45 Å resolution X-ray crystal structure of the IsdB-N2-heme complex. While the structure largely conforms to the eight-strand β-sandwich fold seen in other NEAT domains such as IsdA-N and uses a conserved Tyr residue to coordinate heme-iron, a Met residue is also involved in iron coordination, resulting in a novel Tyr-Met hexacoordinate heme-iron state. The kinetics of the transfer of heme from IsdB-N2 to IsdA-N can be modeled as a two-step process. The rate of transfer of heme between the isolated NEAT domains (82 s(-1)) was found to be similar to that measured for the full-length proteins. Replacing the iron coordinating Met with Leu did not abrogate high-affinity heme binding but did reduce the heme transfer rate constant by more than half. This unusual Met-Tyr heme coordination may also bestow properties on IsdB that help it to bind heme in different oxidation states or extract heme from hemoglobin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.