ArticleProceedings of the National Academy of Sciences of the United States of America2022
Cryo-EM structures of staphylococcal IsdB bound to human hemoglobin reveal the process of heme extraction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Two birds with one stone: An antibiotic hit blockingiScience · 2026Article
- Native Mass Spectrometry-Based Proteomics Reveals the Mechanism of Hemophore Release by PathogenicbioRxiv : the preprint server for biology · 2026Article
- Hemoglobin receptor redundancy inJournal of structural biology: X · 2025Article
- Molecular Dynamics Reveals Unique Distal Histidine Positions and Interfacial Transitions of Fish and Mammalian Deoxyhemoglobin at Post-mortem pH.Journal of agricultural and food chemistry · 2025Article
- 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
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of small molecules affecting the interaction between human hemoglobin and Staphylococcus aureus IsdB hemophore.Scientific reports · 2024Article
- Iron Overload in Brain: Transport Mismatches, Microbleeding Events, and How Nanochelating Therapies May Counteract Their Effects.International journal of molecular sciences · 2024Review
- Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance.Heliyon · 2023Review
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Iron surface determinant B (IsdB) is a hemoglobin (Hb) receptor essential for hemic iron acquisition by Staphylococcus aureus. Heme transfer to IsdB is possible from oxidized Hb (metHb), but inefficient from Hb either bound to oxygen (oxyHb) or bound to carbon monoxide (HbCO), and encompasses a sequence of structural events that are currently poorly understood. By single-particle cryo-electron microscopy, we determined the structure of two IsdB:Hb complexes, representing key species along the heme extraction pathway. The IsdB:HbCO structure, at 2.9-Å resolution, provides a snapshot of the preextraction complex. In this early stage of IsdB:Hb interaction, the hemophore binds to the β-subunits of the Hb tetramer, exploiting a folding-upon-binding mechanism that is likely triggered by a cis/trans isomerization of Pro173. Binding of IsdB to α-subunits occurs upon dissociation of the Hb tetramer into α/β dimers. The structure of the IsdB:metHb complex reveals the final step of the extraction process, where heme transfer to IsdB is completed. The stability of the complex, both before and after heme transfer from Hb to IsdB, is influenced by isomerization of Pro173. These results greatly enhance current understanding of structural and dynamic aspects of the heme extraction mechanism by IsdB and provide insight into the interactions that stabilize the complex before the heme transfer event. This information will support future efforts to identify inhibitors of heme acquisition by S. aureus by interfering with IsdB:Hb complex formation.
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