ArticleInfection and immunity2005
A functional virulence complex composed of gingipains, adhesins, and lipopolysaccharide shows high affinity to host cells and matrix proteins and escapes recognition by host immune systems.
Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 78 citations in OpenAlex.
- Review
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- Polymorphic Variants of Peptidylarginine Deiminase Gene fromInternational journal of molecular sciences · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- hTERT Peptide Fragment GV1001 Prevents the Development ofInternational journal of molecular sciences · 2024Article
- Local and Systemic Effects ofMicroorganisms · 2023Review
- Topical application ofInternational journal of molecular medicine · 2022Article
- Periodontitis and cardiometabolic disorders: The role of lipopolysaccharide and endotoxemia.Periodontology 2000 · 2022Review
- Article
- Exacerbation of AMD Phenotype in Lasered CNV Murine Model by Dysbiotic Oral Pathogens.Antioxidants (Basel, Switzerland) · 2021Article
- PorA, a conserved C-terminal domain-containing protein, impacts the PorXY-SigP signaling of the type IX secretion system.Scientific reports · 2020Article
- Drug TargetingSmall structures · 2020Article
- Proteolysis of Gingival Keratinocyte Cell Surface Proteins by Gingipains Secreted FromFrontiers in microbiology · 2020Article
- Parkinson's Disease: A Systemic Inflammatory Disease Accompanied by Bacterial Inflammagens.Frontiers in aging neuroscience · 2019Article
- Molecular mechanisms ofThe Japanese dental science review · 2017Review
- Effect of deletion of theJournal of dental sciences · 2016Article
- Involvement of an Skp-Like Protein, PGN_0300, in the Type IX Secretion System of Porphyromonas gingivalis.Infection and immunity · 2016Article
- Attenuation of the phosphatidylinositol 3-kinase/Akt signaling pathway by Porphyromonas gingivalis gingipains RgpA, RgpB, and Kgp.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arg-gingipain (Rgp) and Lys-gingipain (Kgp) are Porphyromonas gingivalis cysteine proteinases implicated as major virulence factors in pathologies of periodontitis. We purified a 660-kDa cell-associated gingipain complex existing as a homodimer of two catalytically active monomers which comprises their catalytic and adhesin domains. Electron microscopy revealed that the complex was composed of a globular particle with a 10-nm external diameter possessing one or two electron-dense hole-like structures. Two-dimensional gel electrophoresis and immunoblot analyses revealed the association of lipopolysaccharide (LPS) with the catalytic domains and a hemagglutinin domain, Hgp44, of Rgp and Kgp in the complex. The complex significantly degraded human type I collagen and elastin and strongly disrupted viability of human gingival fibroblasts and umbilical vein endotherial cells with an efficiency which was higher than that of the monomeric gingipains. The native complex produced only a small amount of nitrogen dioxide, tumor necrosis factor alpha, and interleukin-6 by macrophages, whereas the heat-denatured complex resulted in increased production. Inhibition of the proteolytic activities of the gingipain complex did not up-regulate the cytokine production, indicating that the functional domains in LPS are structurally masked by the complex proteins. These results indicate the importance of the complex in evasion of host defense mechanisms as well as in host tissue breakdown.
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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.