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  • 1
    Electronic Resource
    Electronic Resource
    Molecular cloning and characterization of the genes encoding the immunoreactive major cell-surface proteins of Porphyromonas gingivalis (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 120 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A 72-kDa major cell-surface protein (72K-CSP) was purified from the wash fluid of Porphyromonas gingivalis OMZ409. Using the synthetic oligonucleotide probes corresponding to the determined amino-terminal amino acid sequence of 72K-CSP, recombinant plasmid clones carrying approx. 3.4-kb KpnI-XhoI fragments in XL1-Blue libraries of P. gingivalis OMZ409 and 381 were obtained. The premature form proteins of 558 and 563 amino acids led by putative signal sequences were thought to be processed to form the mature proteins of a predicted size of 55 655 Da for strain OMZ409 and of 55 654 for strain 381. Both proteins had unusual proline-rich regions in their carboxyl-terminal regions. No homologous sequences could be found in protein databases. Examination of antigen-specific antibody responses in the serum of patients with adult periodontitis by ELISA revealed that 72K-CSP had a different immunoreactivity from that of P. gingivalis 381 fimbriae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07002.x
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  • 2
    Electronic Resource
    Electronic Resource
    Porphyromonas gingivalis fimbriae and their synthetic peptides induce proinflammatory cytokines in human peripheral blood monocyte cultures (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 116 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Porphyromonas gingivalis fimbriae as well as synthetic peptides that mimic the fimbrial subunit protein, which includes the amino acid sequence XLTXXLTXXNXX, induced high production of proinflammatory cytokines such as interleukin-1β, interleukin-6, interleukin-8, tumor necrosis factor-α in human peripheral blood monocyte/macrophage cultures. Responses induced by some peptide segments were comparable to those induced by Escherichia coli lipopolysaccharides. A chemically modified peptide analogous to an active peptide segment was found to be antagonistic with regard to interleukin-6 production induced by the native fimbriae. It may be suggested that P. gingivalis fimbriae and their degraded peptides function as proinflammatory agents in vivo, while certain analog peptides inhibited the process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06707.x
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  • 3
    Electronic Resource
    Electronic Resource
    Binding of Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 226 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Treponema denticola has been reported to coaggregate with Porphyromonas gingivalis and localize closely together in matured subgingival plaque. In this study of the interaction of T. denticola with P. gingivalis, the P. gingivalis fimbria-binding protein of T. denticola was identified by two-dimensional electrophoresis followed by a ligand overlay assay with P. gingivalis fimbriae, and was determined to be dentilisin, a chymotrypsin-like proteinase of T. denticola. The binding was further demonstrated with a ligand overlay assay using an isolated GST fusion dentilisin construct. Our results suggest that P. gingivalis fimbriae and T. denticola dentilisin are implicated in the coaggregation of these bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00615-3
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  • 4
    Electronic Resource
    Electronic Resource
    Differential induction of IL-1β and IL-6 production by the nontoxic lipid A from Porphyromonas gingivalis in comparison with synthetic Escherichia coli lipid A in human peripheral blood mononuclear cells (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 14 (1996), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Porphyromonas gingivalis 381 lipid A possesses 1-phospho β(1–6)-linked glucosamine disaccharide with 3-hydroxy-15-methylhexadecanoyl and 3-hexadecanoyloxy-15-methylhexadecanoyl groups at the 2- and 2′-positions, respectively. P. gingivalis lipid A indicated lower activities in inducing interleukin-1β (IL-1β) mRNA expression, pro-IL-1β protein synthesis and IL-1β production than those of synthetic Escherichia coli lipid A (compound 506) in human peripheral blood mononuclear cells (PBMC). The induction of IL-6 mRNA and IL-6 synthesis by P. gingivalis lipid A were comparable to those of compound 506. Herbimycin A, H-7 and H-8, inhibitors of tyrosine kinase, protein kinase C and cyclic nucleotide-dependent protein kinase, inhibited P. gingivalis lipid A- and compound 506-induced IL-1β and IL-6 synthesis. W-7, an inhibitor of calmodulin (CaM) kinase, inhibited only P. gingivalis lipid A-induced IL-1β production. The result suggests that the CaM kinase-dependent cascade is involved in the down-regulation of IL-1β production by P. gingivalis lipid A. P. gingivalis lipid A and compound 506 also functioned in the induction of tyrosine and serine/threonine phosphorylation of several proteins in PBMC. P. gingivalis lipid A inhibited specific binding of fluorescein-labelled E. coli LPS to the PBMC. The nontoxic lipid A of P. gingivalis, having a chemical structure different from toxic compound 506, appears to induce the up- and down-regulation of the differential cytokine-producing activities following the activation of various intracellular enzymes including the CaM kinase through the common receptor sites of LPS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1996.tb00261.x
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  • 5
    Electronic Resource
    Electronic Resource
    Endotoxic and immunobiological activities of a chemically synthesized lipid A of Helicobacter pylori strain 206–1 (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 36 (2003), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A synthetic lipid A of Helicobacter pylori strain 206-1 (compound HP206–1), which is similar to its natural lipid A, exhibited no or very low endotoxic activities as compared to Escherichia coli-type synthetic lipid A (compound 506). Furthermore, compound HP206-1 as well as its natural lipid A demonstrated no or very low mitogenic responses in murine spleen cell. On the other hand, compound HP206-1 showed a weaker but significant production of interleukin-8 in a gastric cancer cell line, MKN-1, in comparison with compound 506. Furthermore, compound HP206-1 exhibited induction of tumor necrosis factor-α production in human peripheral blood mononuclear cells and the cytokine production was clearly inhibited by mouse anti-human Toll-like receptor (TLR) 4 monoclonal antibody HTA125. Our findings indicate that the chemically synthesized lipid A, mimicking the natural lipid A portion of lipopolysaccharide from H. pylori strain 206-1, has a low endotoxic potency and immunobiological activities, and is recognized by TLR4.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0928-8244(03)00093-2
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  • 6
    Electronic Resource
    Electronic Resource
    Osteoclast differentiation by human osteoblastic cell line SaOS-2 primed with bacterial lipid A (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 38 (2003), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We examined the responses of human osteoblastic cell line SaOS-2 to bacterial lipid A, a bioactive center of lipopolysaccharide, during osteoclast differentiation of human peripheral blood mononuclear cells (PBMC). SaOS-2 cells expressed mRNA for Toll-like receptor (TLR) 4, MD-2, CD14, and myeloid differentiation factor 88, whereas they failed to express mRNA for TLR2. Escherichia coli-type synthetic lipid A (compound 506) induced cytokine mRNA expression and nuclear factor (NF)-κB activation in SaOS-2 cells. Compound 506 also increased the expression of receptor activator of NF-κB ligand. Further, cells primed with compound 506 augmented the differentiation of PBMC into osteoclastic cells, and the effect was inhibited by anti-TLR4 monoclonal antibody. These findings suggest that the TLR signaling cascade in osteoblastic cells is involved in regulating the function of osteoclastogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0928-8244(03)00111-1
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  • 7
    Electronic Resource
    Electronic Resource
    Hyporesponsiveness of inflamed human gingival fibroblasts from patients with chronic periodontal diseases against cell surface components of Porphyromonas gingivalis (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 18 (1997), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Inflamed human gingival fibroblasts (HGF) of patients with chronic periodontal diseases have less active interleukin-8 (IL-8) production compared with normal HGF of volunteers with healthy gingival tissues, after stimulation with Porphyromonas gingivalis surface components such as fimbriae, lipopolysaccharide (LPS) and its lipid A, but not LPS or lipid A from other bacterial species. A decrease in number of specific binding sites for P. gingivalis fimbrial molecules in inflamed HGF is also observed by Scatchard plot analysis. A short exposure (6 h) to P. gingivalis LPS resulted in significant potentiation of the LPS-dependent IL-8 production in normal HGF, whereas a long exposure (48 h) to the LPS significantly reduced IL-8 production. Tyrosine phosphorylation of proteins of 127 kDa and 186 kDa in inflamed HGF stimulated with P. gingivalis fimbriae or its LPS was observed by immunoblotting, and these two phosphoproteins were termed tolerance-induced protein, TIP. Protein bands of 45 kDa which bound to radioiodinated P. gingivalis fimbriae in the presence and absence of fetal bovine serum (FBS), and major 73-kDa and minor 30-kDa and 45-kDa bands which bound to radioiodinated P. gingivalis LPS in the presence of FBS in normal and inflamed HGF were observed by using photocrosslinking. These findings suggest that the hyporesponsiveness of HGF induced by a prolonged exposure to P. gingivalis may emerge because of HGF damage or result from host defense in chronic periodontal lesions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1997.tb01023.x
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  • 8
    Electronic Resource
    Electronic Resource
    Immunobiological activities of a chemically synthesized lipid A of Porphyromonas gingivalis (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 28 (2000), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A synthetic lipid A of Porphyromonas gingivalis strain 381 (compound PG-381), which is similar to its natural lipid A, demonstrated no or very low endotoxic activities as compared to Escherichia coli-type synthetic lipid A (compound 506). On the other hand, compound PG-381 had stronger hemagglutinating activities on rabbit erythrocytes than compound 506. Compound PG-381 also induced mitogenic responses in spleen cells from lipopolysaccharide (LPS)-hyporesponsive C3H/HeJ mice, as well as LPS-responsive C3H/HeN mice. The addition of polymyxin B resulted in the inhibition of mitogenic activities, however, compound 506 did not show these capacities. Additionally, compound PG-381 showed a lower level of activity in inducing cytokine production in peritoneal macrophages and gingival fibroblasts from C3H/HeN mice, but not C3H/HeJ mice, in comparison to compound 506. Thus, this study demonstrates that the chemical synthesis of lipid A, mimicking the natural lipid A portion of LPS from P. gingivalis, confirms its low endotoxic potency and immunobiological activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01487.x
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  • 9
    Electronic Resource
    Electronic Resource
    Prevention of endotoxin-induced lethality in mice by calmodulin kinase activator (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 27 (2000), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Porphyromonas gingivalis strain 381 lipid A showed lower activity in inducing interleukin (IL)-1α and IL-1β production and cytokine mRNA expression than synthetic Escherichia coli lipid A (compound 506) in alveolar macrophages of C57BL/6 mice. Both the lipid As induced tumor necrosis factor α in alveolar macrophages and IL-6 in peritoneal macrophages. A calmodulin (CaM) antagonist, W-7, inhibited IL-1β production and its mRNA expression induced by P. gingivalis lipid A but not compound 506 in alveolar macrophages. A CaM kinase activator reduced the induction of IL-1β in the serum of mice when administered with compound 506, and protected the mice against the lethal toxicity. The modulation of a variety of intracellular enzymes including the CaM kinase may result in clinical control of endotoxic sepsis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01431.x
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  • 10
    Electronic Resource
    Electronic Resource
    A peptide, ALTTE, within the fimbrial subunit protein from Porphyromonas gingivalis, induces production of interleukin 6, gene expression and protein phosphorylation in human peripheral blood mononuclear cells (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 11 (1995), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Porphyromonas gingivalis 381 fimbriae and a synthetic peptide composed of residues 69–73 (ALTTE) of the fimbrial subunit protein, FP381(69–73), function in the induction of interleukin 6 (IL-6) production, IL-6 mRNA expression, and tyrosine and serine/threonine phosphorylation of several proteins in human peripheral blood mononuclear cells (PBMC). Herbimycin A and H-7, inhibitors of tyrosine kinases and protein kinase C (PKC), markedly inhibited IL-6 production, gene expression, and tyrosine and serine/threonine phosphorylation of proteins. An inactive analog of synthetic peptide replaced alanine to glycine at position 69 in FP381(69–73), GLTTE, exhibited an antagonistic effect on the IL-6 production induced by the fimbriae. These results suggest that the peptide ALTTE functions as an agent in inflammatory reactions and immune responses in the inflamed gingival and periodontal tissues, in which the participation of protein phosphorylation by tyrosine kinases and PKC in signal transduction may be considered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1995.tb00117.x
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