ArticleThe Journal of biological chemistry2011
Structural basis for hemoglobin capture by Staphylococcus aureus cell-surface protein, IsdH.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 57 citations in OpenAlex.
- In Silico Prioritisation of Similarity-Selected Small Molecules Targeting the IsdB NEAT Domain ofInternational journal of molecular sciences · 2026Article
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Hemoglobin receptor redundancy inJournal of structural biology: X · 2025Article
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and role of the linker domain of the iron surface-determinant protein IsdH in heme transportation in Staphylococcus aureus.The Journal of biological chemistry · 2022Article
- 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
- The human protein haptoglobin inhibits IsdH-mediated heme-sequestering byThe Journal of biological chemistry · 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
- Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight.Scientific reports · 2019Article
- NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.Protein science : a publication of the Protein Society · 2019Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- TheThe Journal of biological chemistry · 2018Article
- Energetics underlying hemin extraction from human hemoglobin byThe Journal of biological chemistry · 2018Article
- Structure-function analyses reveal key features inThe Journal of biological chemistry · 2018Article
- Molecular mechanisms of bio-catalysis of heme extraction from hemoglobin.Redox biology · 2017Article
- The Staphylococcus aureus Protein IsdH Inhibits Host Hemoglobin Scavenging to Promote Heme Acquisition by the Pathogen.The Journal of biological chemistry · 2016Article
- The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Journal of molecular biology · 2016Article
- The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes.The Journal of biological chemistry · 2014Article
- The structure of α-haemoglobin in complex with a haemoglobin-binding domain from Staphylococcus aureus reveals the elusive α-haemoglobin dimerization interface.Acta crystallographica. Section F, Structural biology communications · 2014Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
Abstract
Pathogens must steal iron from their hosts to establish infection. In mammals, hemoglobin (Hb) represents the largest reservoir of iron, and pathogens express Hb-binding proteins to access this source. Here, we show how one of the commonest and most significant human pathogens, Staphylococcus aureus, captures Hb as the first step of an iron-scavenging pathway. The x-ray crystal structure of Hb bound to a domain from the Isd (iron-regulated surface determinant) protein, IsdH, is the first structure of a Hb capture complex to be determined. Surface mutations in Hb that reduce binding to the Hb-receptor limit the capacity of S. aureus to utilize Hb as an iron source, suggesting that Hb sequence is a factor in host susceptibility to infection. The demonstration that pathogens make highly specific recognition complexes with Hb raises the possibility of developing inhibitors of Hb binding as antibacterial agents.
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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.