ArticleInfection and immunity2006
Identification of amino acid residues involved in heme binding and hemoprotein utilization in the Porphyromonas gingivalis heme receptor HmuR.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Chaperone-assisted cryo-EM structure ofbioRxiv : the preprint server for biology · 2024Article
- Investigating the importance of selected surface-exposed loops in HpuB for hemoglobin binding and utilization byInfection and immunity · 2024Article
- Chaperone-assisted cryo-EM structure of P. aeruginosa PhuR reveals molecular basis for heme binding.Structure (London, England : 1993) · 2024Article
- Hemophore-like proteins of the HmuY family in the oral and gut microbiome: unraveling the mystery of their evolution.Microbiology and molecular biology reviews : MMBR · 2024Review
- Two functionally distinct heme/iron transport systems are virulence determinants of the fish pathogenVirulence · 2022Article
- TrkA serves as a virulence modulator inFrontiers in cellular and infection microbiology · 2022Article
- Glycation of Host Proteins Increases Pathogenic Potential ofInternational journal of molecular sciences · 2021Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- Article
- Dissecting binding of a β-barrel membrane protein by phage display.Molecular bioSystems · 2017Article
- Heme uptake in bacterial pathogens.Current opinion in chemical biology · 2014Review
- Differential roles of tryptophan residues in conformational stability of Porphyromonas gingivalis HmuY hemophore.BMC biochemistry · 2014Article
- Axial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporter.Biochemistry · 2013Article
- Insights on how the Mycobacterium tuberculosis heme uptake pathway can be used as a drug target.Future medicinal chemistry · 2013Article
- Mutational analysis of hemoglobin binding and heme utilization by a bacterial hemoglobin receptor.Journal of bacteriology · 2013Article
- Role and regulation of heme iron acquisition in gram-negative pathogens.Frontiers in cellular and infection microbiology · 2013Review
- Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans.Frontiers in cellular and infection microbiology · 2013Review
- The influence of iron availability on human salivary microbial community composition.Microbial ecology · 2012Article
- The Neisseria meningitidis ZnuD zinc receptor contributes to interactions with epithelial cells and supports heme utilization when expressed in Escherichia coli.Infection and immunity · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
We have previously identified and characterized a heme/hemoglobin receptor, HmuR, in Porphyromonas gingivalis. To analyze the conserved amino acid residues of HmuR that may be involved in hemin/hemoprotein binding and utilization, we constructed a series of P. gingivalis A7436 hmuR mutants with amino acid replacements and characterized the ability of these mutants to utilize hemin and hemoproteins. Site-directed mutagenesis was employed to introduce mutations H95A, H434A, H95A-H434A, YRAP420-423YAAA, and NPDL442-445NAAA into HmuR in both P. gingivalis and Escherichia coli. Point mutations at H95 and H434 and in the NPDL motif of HmuR resulted in decreased binding to hemin, hemoglobin, and human serum albumin-hemin complex. Notably, mutations of these conserved sites and motifs led to reduced growth of P. gingivalis when human serum was used as the heme source. Analysis using a three-dimensional homology model of HmuR indicated that H95, H434, and the NPDL motif are present on apical or extracellular loops of HmuR, while the YRAP motif is present on the barrel wall. Taken together, these results support a role for H95, H434, and the NPDL motif of the P. gingivalis HmuR protein in heme binding and utilization of serum hemoproteins and the HmuR YRAP motif in serum hemoprotein utilization.
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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.