ArticleJournal of bacteriology2000
Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.
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Who cites it
46 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.
- Microbial signatures in human periodontal disease: a metatranscriptome meta-analysis.Frontiers in microbiology · 2024Pooled it
- Colouring dysbiosis: FetB-dependent Mn-PPIX produced by Porphyromonas gingivalis shapes the oral microbiota.NPJ biofilms and microbiomes · 2026Article
- The survival status ofJournal of oral microbiology · 2026Review
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Defining the role of Hmu and Hus systems in Porphyromonas gingivalis heme and iron homeostasis and virulence.Scientific reports · 2024Article
- Comparative analysis ofMicrobiology spectrum · 2024Article
- Heme utilization by the enterococci.FEMS microbes · 2024Review
- Novel devices for isolation and detection of bacterial and mammalian extracellular vesicles.Mikrochimica acta · 2021Review
- Article
- Bacterial bug-out bags: outer membrane vesicles and their proteins and functions.Journal of microbiology (Seoul, Korea) · 2020Review
- Bacteroides fragilis requires the ferrous-iron transporter FeoAB and the CobN-like proteins BtuS1 and BtuS2 for assimilation of iron released from heme.MicrobiologyOpen · 2019Article
- Structural properties of a haemophore facilitate targeted elimination of the pathogen Porphyromonas gingivalis.Nature communications · 2018Article
- Hemin binding by Porphyromonas gingivalis strains is dependent on the presence of A-LPS.Molecular oral microbiology · 2017Article
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- Two-component signal transduction systems in oral bacteria.Journal of oral microbiology · 2017Review
- Surface-Exposed Lipoproteins: An Emerging Secretion Phenomenon in Gram-Negative Bacteria.Trends in microbiology · 2016Review
- Outer membrane lipoprotein biogenesis: Lol is not the end.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Outer-membrane vesicles from Gram-negative bacteria: biogenesis and functions.Nature reviews. Microbiology · 2015Review
- Contact- and Protein Transfer-Dependent Stimulation of Assembly of the Gliding Motility Machinery in Myxococcus xanthus.PLoS genetics · 2015Article
- Comparative genome analysis of Prevotella intermedia strain isolated from infected root canal reveals features related to pathogenicity and adaptation.BMC genomics · 2015Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Porphyromonas gingivalis is a gram-negative, anaerobic coccobacillus that has been implicated as a major etiological agent in the development of chronic periodontitis. In this paper, we report the characterization of a protein, IhtB (iron heme transport; formerly designated Pga30), that is an outer membrane hemin-binding protein potentially involved in iron assimilation by P. gingivalis. IhtB was localized to the cell surface of P. gingivalis by Western blot analysis of a Sarkosyl-insoluble outer membrane preparation and by immunocytochemical staining of whole cells using IhtB peptide-specific antisera. The protein, released from the cell surface, was shown to bind to hemin using hemin-agarose. The growth of heme-limited, but not heme-replete, P. gingivalis cells was inhibited by preincubation with IhtB peptide-specific antisera. The ihtB gene was located between an open reading frame encoding a putative TonB-linked outer membrane receptor and three open reading frames that have sequence similarity to ATP binding cassette transport system operons in other bacteria. Analysis of the deduced amino acid sequence of IhtB showed significant similarity to the Salmonella typhimurium protein CbiK, a cobalt chelatase that is structurally related to the ATP-independent family of ferrochelatases. Molecular modeling indicated that the IhtB amino acid sequence could be threaded onto the CbiK fold with the IhtB structural model containing the active-site residues critical for chelatase activity. These results suggest that IhtB is a peripheral outer membrane chelatase that may remove iron from heme prior to uptake by P. gingivalis.
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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.