ArticleJournal of bacteriology1999
Hemoglobinase activity of the lysine gingipain protease (Kgp) of Porphyromonas gingivalis W83.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 119 citations in OpenAlex.
- The survival status ofJournal of oral microbiology · 2026Review
- PorA of the Type IX Secretion Is a Ligand of the PorXY Two-Component Regulatory System in Porphyromonas gingivalis.Molecular microbiology · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- TheFrontiers in cellular and infection microbiology · 2025Article
- The oral pathogen Porphyromonas gingivalis gains tolerance to the antimicrobial peptide DGL13K by synonymous mutations in hagA.PloS one · 2024Article
- Hemin availability induces coordinated DNA methylation and gene expression changes inmSystems · 2023Article
- Local and Systemic Effects ofMicroorganisms · 2023Review
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular basis for avirulence of spontaneous variants of Porphyromonas gingivalis: Genomic analysis of strains W50, BE1 and BR1.Molecular oral microbiology · 2022Article
- Porphyromonas gingivalis Gingipains-Mediated Degradation of Plasminogen Activator Inhibitor-1 Leads to Delayed Wound Healing Responses in Human Endothelial Cells.Journal of innate immunity · 2022Article
- S-PRG Filler Eluate Induces Oxidative Stress in Oral Microorganism: Suppression of Growth and Pathogenicity, and Possible Clinical Application.Antibiotics (Basel, Switzerland) · 2021Article
- Article
- Insertional Inactivation ofMicroorganisms · 2021Article
- PorA, a conserved C-terminal domain-containing protein, impacts the PorXY-SigP signaling of the type IX secretion system.Scientific reports · 2020Article
- Quercetin inhibits virulence properties of Porphyromas gingivalis in periodontal disease.Scientific reports · 2020Article
- Role of extracytoplasmic function sigma factor PG1660 (RpoE) in the oxidative stress resistance regulatory network of Porphyromonas gingivalis.Molecular oral microbiology · 2018Article
- Article
- Hemin binding by Porphyromonas gingivalis strains is dependent on the presence of A-LPS.Molecular oral microbiology · 2017Article
- Using Tn-seq To Identify Pigmentation-Related Genes of Porphyromonas gingivalis: Characterization of the Role of a Putative Glycosyltransferase.Journal of bacteriology · 2017Article
- Effect of deletion of theJournal of dental sciences · 2016Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Porphyromonas gingivalis, an important periodontal disease pathogen, forms black-pigmented colonies on blood agar. Pigmentation is believed to result from accumulation of iron protoporphyrin IX (FePPIX) derived from erythrocytic hemoglobin. The Lys-X (Lys-gingipain) and Arg-X (Arg-gingipain) cysteine proteases of P. gingivalis bind and degrade erythrocytes. We have observed that mutations abolishing activity of the Lys-X-specific cysteine protease, Kgp, resulted in loss of black pigmentation of P. gingivalis W83. Because the hemagglutinating and hemolytic potentials of mutant strains were reduced but not eliminated, we hypothesized that this protease played a role in acquisition of FePPIX from hemoglobin. In contrast to Arg-gingipain, Lys-gingipain was not inhibited by hemin, suggesting that this protease played a role near the cell surface where high concentrations of hemin confer the black pigmentation. Human hemoglobin contains 11 Lys residues in the alpha chain and 10 Lys residues in the beta chain. In contrast, there are only three Arg residues in each of the alpha and beta chains. These observations are consistent with human hemoglobin being a preferred substrate for Lys-gingipain but not Arg-gingipain. The ability of the Lys-gingipain to cleave human hemoglobin at Lys residues was confirmed by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry of hemoglobin fragments resulting from digestion with the purified protease. We were able to detect several of the predicted hemoglobin fragments rendered by digestion with purified Lys-gingipain. Thus, we postulate that the Lys-gingipain of P. gingivalis is a hemoglobinase which plays a role in heme and iron uptake by effecting the accumulation of FePPIX on the bacterial cell surface.
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