ArticlePLoS pathogens2009
Unique structure and stability of HmuY, a novel heme-binding protein of Porphyromonas gingivalis.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
54 citing papers in PubMed, 105 citations in OpenAlex.
- The Role of the Oral Microbiome in the Development and Treatment of Periodontal Disease: Functional Meta-Omics Evidence.Current microbiology · 2026Review
- Socio-evolutionary role of bacterial membrane vesicles in cooperation and competition within microbial communities.The ISME journal · 2026Review
- 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
- Commensal gut bacteria employ de-chelatase HmuS to harvest iron from heme.The EMBO journal · 2025Article
- Structural Basis and Mechanism of a Unique Haemophore in the Haem-Iron Acquisition by Riemerella anatipestifer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- In Silico Docking of Medicinal Herbs Against P. gingivalis for Chronic Periodontitis Intervention.International dental journal · 2025Article
- 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
- Defining the role of Hmu and Hus systems in Porphyromonas gingivalis heme and iron homeostasis and virulence.Scientific reports · 2024Article
- Review
- Prevalence of Slam-dependent hemophilins in Gram-negative bacteria.Journal of bacteriology · 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
- Article
- Hemophore-like proteins produced by periodontopathogens are recognized by the host immune system and react differentially with IgG antibodies.Journal of oral microbiology · 2023Article
- Two functionally distinct heme/iron transport systems are virulence determinants of the fish pathogenVirulence · 2022Article
- Proteomic Network of Antibiotic-Induced Outer Membrane Vesicles Released by Extensively Drug-Resistant Elizabethkingia anophelis.Microbiology spectrum · 2022Article
- Article
- Unique Properties of Heme Binding of theMolecules (Basel, Switzerland) · 2022Article
- Glycation of Host Proteins Increases Pathogenic Potential ofInternational journal of molecular sciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Infection, survival, and proliferation of pathogenic bacteria in humans depend on their capacity to impair host responses and acquire nutrients in a hostile environment. Among such nutrients is heme, a co-factor for oxygen storage, electron transport, photosynthesis, and redox biochemistry, which is indispensable for life. Porphyromonas gingivalis is the major human bacterial pathogen responsible for severe periodontitis. It recruits heme through HmuY, which sequesters heme from host carriers and delivers it to its cognate outer-membrane transporter, the TonB-dependent receptor HmuR. Here we report that heme binding does not significantly affect the secondary structure of HmuY. The crystal structure of heme-bound HmuY reveals a new all-beta fold mimicking a right hand. The thumb and fingers pinch heme iron through two apical histidine residues, giving rise to highly symmetric octahedral iron co-ordination. The tetrameric quaternary arrangement of the protein found in the crystal structure is consistent with experiments in solution. It shows that thumbs and fingertips, and, by extension, the bound heme groups, are shielded from competing heme-binding proteins from the host. This may also facilitate heme transport to HmuR for internalization. HmuY, both in its apo- and in its heme-bound forms, is resistant to proteolytic digestion by trypsin and the major secreted proteases of P. gingivalis, gingipains K and R. It is also stable against thermal and chemical denaturation. In conclusion, these studies reveal novel molecular properties of HmuY that are consistent with its role as a putative virulence factor during bacterial infection.
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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.