ArticleArchives of microbiology2008
Porphyromonas gingivalis HmuY and HmuR: further characterization of a novel mechanism of heme utilization.
Article in Archives of microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed, 103 citations in OpenAlex.
- Porphyromonas gingivalis produces a functional HemH ferrochelatase important for its survival in a heme-limited environment.Scientific reports · 2026Article
- The survival status ofJournal of oral microbiology · 2026Review
- Biochemical and functional characterization ofFrontiers in microbiology · 2026Article
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 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
- 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
- Comparative analysis ofMicrobiology spectrum · 2024Article
- The leprosy reaction is associated with salivary anti-Porphyromonas gingivalis IgA antibodies.AMB Express · 2023Article
- Protein interactome mapping of Porphyromonas gingivalis provides insights into the formation of the PorQ-Z complex of the type IX secretion system.Molecular oral microbiology · 2023Article
- Genomics ofPathogens (Basel, Switzerland) · 2023Article
- Hemophore-like proteins produced by periodontopathogens are recognized by the host immune system and react differentially with IgG antibodies.Journal of oral microbiology · 2023Article
- The secretome of the fish pathogenFrontiers in cellular and infection microbiology · 2023Article
- Two functionally distinct heme/iron transport systems are virulence determinants of the fish pathogenVirulence · 2022Article
- [Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2022Review
- Modulation of Iron Import and Metronidazole Resistance inFrontiers in microbiology · 2022Article
- Peptidomimetics as Potential Anti-Virulence Drugs Against Resistant Bacterial Pathogens.Frontiers in microbiology · 2022Review
- Glycation of Host Proteins Increases Pathogenic Potential ofInternational journal of molecular sciences · 2021Article
- Insertional Inactivation ofMicroorganisms · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Porphyromonas gingivalis HmuY is a putative heme-binding lipoprotein associated with the outer membrane. It is part of an operon together with a gene encoding an outer-membrane hemin utilization receptor (HmuR) and four uncharacterized genes. A similar operon organization was found in Bacteroides fragilis and B. thetaiotaomicron, with the former containing an additional HmuY homologue encoded upstream of the hmuR-like gene. In P. gingivalis cultured under heme-limited conditions, a approximately 1-kb hmuY transcript was produced at high levels along with some approximately 3.5 and approximately 9-kb transcripts. Compared with the parental strain, mutants deficient in hmuY or hmuR or hmuY-hmuR gene function grew more slowly and bound lower amounts of hemin and hemoglobin. Significantly, they grew more slowly or were unable to grow when human serum was used as the sole iron/heme source. Analysis of the hmu promoter showed that it is regulated by iron. The HmuY protein normally occurs as a homodimer, but in the presence of hemin it may form tetramers. These results show that HmuY may be the first reported member of a new class of proteins in Porphyromonas and Bacteroides species involved in heme utilization, a function being exerted in conjunction with HmuR, an outer-membrane heme transporter.
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What OpenQuestion holds
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.