ArticleThe Journal of biological chemistry2014
Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Native Mass Spectrometry-Based Proteomics Reveals the Mechanism of Hemophore Release by PathogenicbioRxiv : the preprint server for biology · 2026Article
- Rli51 Attenuates Transcription of theInternational journal of molecular sciences · 2024Article
- Identification of small molecules affecting the interaction between human hemoglobin and Staphylococcus aureus IsdB hemophore.Scientific reports · 2024Article
- Effect of anti-biofilm peptideFrontiers in cellular and infection microbiology · 2024Article
- Heme acquisition and tolerance in Gram-positive model bacteria: An orchestrated balance.Heliyon · 2023Review
- Comparative Genomics Reveal the Utilization Ability of Variable Carbohydrates as Key Genetic Features ofPathogens (Basel, Switzerland) · 2022Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- NEAr Transporter (NEAT) Domains: Unique Surface Displayed Heme Chaperones That Enable Gram-Positive Bacteria to Capture Heme-Iron From Hemoglobin.Frontiers in microbiology · 2020Review
- NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.Protein science : a publication of the Protein Society · 2019Article
- Universal fluorescent sensors of high-affinity iron transport, applied to ESKAPE pathogens.The Journal of biological chemistry · 2019Article
- TheThe Journal of biological chemistry · 2018Article
- The Small Regulatory RNAs LhrC1-5 Contribute to the Response ofFrontiers in microbiology · 2018Article
- The heme-regulatory motif of nuclear receptor Rev-erbβ is a key mediator of heme and redox signaling in circadian rhythm maintenance and metabolism.The Journal of biological chemistry · 2017Article
- Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Journal of inorganic biochemistry · 2017Article
- Progress toward the Development of a NEAT Protein Vaccine for Anthrax Disease.Infection and immunity · 2016Article
- Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016Review
- Iron and zinc exploitation during bacterial pathogenesis.Metallomics : integrated biometal science · 2015Review
- Article
- An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- 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
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Iron is an essential nutrient that is required for the growth of the bacterial pathogen Listeria monocytogenes. In cell cultures, this microbe secretes hemin/hemoglobin-binding protein 2 (Hbp2; Lmo2185) protein, which has been proposed to function as a hemophore that scavenges heme from the environment. Based on its primary sequence, Hbp2 contains three NEAr transporter (NEAT) domains of unknown function. Here we show that each of these domains mediates high affinity binding to ferric heme (hemin) and that its N- and C-terminal domains interact with hemoglobin (Hb). The results of hemin transfer experiments are consistent with Hbp2 functioning as an Hb-binding hemophore that delivers hemin to other Hbp2 proteins that are attached to the cell wall. Surprisingly, our work reveals that the central NEAT domain in Hbp2 binds hemin even though its primary sequence lacks a highly conserved YXXXY motif that is used by all other previously characterized NEAT domains to coordinate iron in the hemin molecule. To elucidate the mechanism of hemin binding by Hbp2, we determined crystal structures of its central NEAT domain (Hbp2(N2); residues 183-303) in its free and hemin-bound states. The structures reveal an unprecedented mechanism of hemin binding in which Hbp2(N2) undergoes a major conformational rearrangement that facilitates metal coordination by a non-canonical tyrosine residue. These studies highlight previously unrecognized plasticity in the hemin binding mechanism of NEAT domains and provide insight into how L. monocytogenes captures heme iron.
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