ArticleProtein science : a publication of the Protein Society2019
NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- 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
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- The Staphylococcus aureus IsdH Receptor Forms a Dynamic Complex with Human Hemoglobin that Triggers Heme Release via Two Distinct Hot Spots.Journal of molecular biology · 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
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Iron is a versatile metal cofactor that is used in a wide range of essential cellular processes. During infections, many bacterial pathogens acquire iron from human hemoglobin (Hb), which contains the majority of the body's total iron content in the form of heme (iron protoporphyrin IX). Clinically important Gram-positive bacterial pathogens scavenge heme using an array of secreted and cell-wall-associated receptors that contain NEAr-iron Transporter (NEAT) domains. Experimentally defining the Hb binding properties of NEAT domains has been challenging, limiting our understanding of their function in heme uptake. Here we show that solution-state NMR spectroscopy is a powerful tool to define the Hb binding properties of NEAT domains. The utility of this method is demonstrated using the NEAT domains from Bacillus anthracis and Listeria monocytogenes. Our results are compatible with the existence of at least two types of NEAT domains that are capable of interacting with either Hb or heme. These binding properties can be predicted from their primary sequences, with Hb- and heme-binding NEAT domains being distinguished by the presence of (F/Y)YH(Y/F) and S/YXXXY motifs, respectively. The results of this work should enable the functions of a wide range of NEAT domain containing proteins in pathogenic bacteria to be reliably predicted.
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