ArticleThe Journal of biological chemistry2010
Characterization of a hemophore-like protein from Porphyromonas gingivalis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Colouring dysbiosis: FetB-dependent Mn-PPIX produced by Porphyromonas gingivalis shapes the oral microbiota.NPJ biofilms and microbiomes · 2026Article
- Biochemical and functional characterization ofFrontiers in microbiology · 2026Article
- Porphyrin pathways as targets for combating antimicrobial resistance: virulence and therapeutic opportunities.Frontiers in cellular and infection microbiology · 2026Review
- The survival status ofJournal of oral microbiology · 2026Review
- Interbacterial warfare in the human gut: insights from Bacteroidales' perspective.Gut microbes · 2025Review
- Structural Basis and Mechanism of a Unique Haemophore in the Haem-Iron Acquisition by Riemerella anatipestifer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Study in the iron uptake mechanism of Pasteurella multocida.Veterinary research · 2025Review
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- HmuY proteins of theFrontiers in cellular and infection microbiology · 2025Article
- 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
- Hemophore-like proteins produced by periodontopathogens are recognized by the host immune system and react differentially with IgG antibodies.Journal of oral microbiology · 2023Article
- Glycation of Host Proteins Increases Pathogenic Potential ofInternational journal of molecular sciences · 2021Article
- A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii.Nature communications · 2021Article
- Tryptophan Fluorescence Quenching Assays for Measuring Protein-ligand Binding Affinities: Principles and a Practical Guide.Bio-protocol · 2019Article
- Iron Acquisition in Mycobacterium tuberculosis.Chemical reviews · 2019Review
- Structural properties of a haemophore facilitate targeted elimination of the pathogen Porphyromonas gingivalis.Nature communications · 2018Article
- Transcriptome analysis of Porphyromonas gingivalis and Acinetobacter baumannii in polymicrobial communities.Molecular oral microbiology · 2018Article
- In Vitro Efficacy of Free and Nanoparticle Formulations of Gallium(III) meso-Tetraphenylporphyrine against Mycobacterium avium and Mycobacterium abscessus and Gallium Biodistribution in Mice.Molecular pharmaceutics · 2018Article
- Genes Contributing toFrontiers in cellular and infection microbiology · 2017Article
- SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall inFrontiers in cellular and infection microbiology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The porphyrin auxotrophic pathogen Porphyromonas gingivalis obtains the majority of essential iron and porphyrin from host hemoproteins. To achieve this, the organism expresses outer membrane gingipains containing cysteine proteinase domains linked to hemagglutinin domains. Heme mobilized in this way is taken up by P. gingivalis through a variety of potential portals where HmuY/HmuR of the hmu locus are best described. These receptors have relatively low binding affinities for heme. In this report, we describe a novel P. gingivalis protein, HusA, the product of PG2227, which rapidly bound heme with a high binding constant at equilibrium of 7 × 10(-10) M. HusA is both expressed on the outer membrane and released from the organism. Spectral analysis indicated an unusual pattern of binding where heme was ligated preferentially as a dimer. Further, the presence of dimeric heme induced protein dimer formation. Deletional inactivation of husA showed that expression of this moiety was essential for growth of P. gingivalis under conditions of heme limitation. This finding was in accord with the pronounced increase in gene expression levels for husA with progressive reduction of heme supplementation. Antibodies reactive against HusA were detected in patients with chronic periodontitis, suggesting that the protein is expressed during the course of infection by P. gingivalis. It is predicted that HusA efficiently sequesters heme from gingipains and fulfills the function of a high affinity hemophore-like protein to meet the heme requirement for growth of P. gingivalis during establishment of infection.
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