ArticleScientific reports2019
Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Two birds with one stone: An antibiotic hit blockingiScience · 2026Article
- The Pathogenicity Mechanisms ofInternational journal of molecular sciences · 2025Review
- Hemoglobin receptor redundancy inJournal of structural biology: X · 2025Article
- The endothelium at the interface between tissues andClinical microbiology reviews · 2025Review
- Time-resolved X-ray solution scattering unveils the events leading to hemoglobin heme capture by staphylococcal IsdB.Nature communications · 2025Article
- Proline isomerization modulates the bacterial IsdB/hemoglobin interaction: an atomic force spectroscopy study.Discover nano · 2025Article
- Article
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bacterial hemophilin homologs and their specific type eleven secretor proteins have conserved roles in heme capture and are diversifying as a family.Journal of bacteriology · 2024Article
- Collaborative Cross mice have diverse phenotypic responses to infection with Methicillin-resistant Staphylococcus aureus USA300.PLoS genetics · 2024Article
- Identification of small molecules affecting the interaction between human hemoglobin and Staphylococcus aureus IsdB hemophore.Scientific reports · 2024Article
- TLR4 sensing of IsdB ofmBio · 2024Article
- Draft genome sequence of Staphylococcus aureus sequence type 5 SA01 isolated from bloodstream infection and comparative analysis with reference strains.Functional & integrative genomics · 2023Article
- Dietary Heme-Containing Proteins: Structures, Applications, and Challenges.Foods (Basel, Switzerland) · 2022Review
- 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
- Staphylococcus aureus iron-regulated surface determinant B (IsdB) protein interacts with von Willebrand factor and promotes adherence to endothelial cells.Scientific reports · 2021Article
- Ferric iron reductases and their contribution to unicellular ferrous iron uptake.Journal of inorganic biochemistry · 2021Review
- Atomistic Simulations of Heme Dissociation Pathways in Human Methemoglobins Reveal Hidden Intermediates.Biochemistry · 2020Article
- The iron-regulated surface determinant B (IsdB) protein fromThe Journal of biological chemistry · 2020Article
- Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among multidrug-resistant bacteria, methicillin-resistant Staphylococcus aureus is emerging as one of the most threatening pathogens. S. aureus exploits different mechanisms for its iron supply, but the preferred one is acquisition of organic iron through the expression of hemoglobin (Hb) receptors. One of these, IsdB, belonging to the Isd (Iron-Regulated Surface Determinant) system, was shown to be essential for bacterial growth and virulence. Therefore, interaction of IsdB with Hb represents a promising target for the rational design of a new class of antibacterial molecules. However, despite recent investigations, many structural and mechanistic details of complex formation and heme extraction process are still elusive. By combining site-directed mutagenesis, absorption spectroscopy, surface plasmon resonance and molecular dynamics simulations, we tackled most of the so far unanswered questions: (i) the exact complex stoichiometry, (ii) the microscopic kinetic rates of complex formation, (iii) the IsdB selectivity for binding to, and extracting heme from, α and β subunits of Hb, iv) the role of specific amino acid residues and structural regions in driving complex formation and heme transfer, and (v) the structural/dynamic effect played by the hemophore on Hb.
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