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PloS One 2014Dipeptidyl peptidases (DPPs) that liberate dipeptides from the N-terminal end of oligopeptides are crucial for the growth of Porphyromonas species, anaerobic...
Dipeptidyl peptidases (DPPs) that liberate dipeptides from the N-terminal end of oligopeptides are crucial for the growth of Porphyromonas species, anaerobic asaccharolytic gram negative rods that utilize amino acids as energy sources. Porphyromonas endodontalis is a causative agent of periapical lesions with acute symptoms and Asp/Glu-specific DPP11 has been solely characterized in this organism. In this study, we identified and characterized two P. endodontalis DPPs, DPP5 and DPP7. Cell-associated DPP activity toward Lys-Ala-4-methylcoumaryl-7-amide (MCA) was prominent in P. endodontalis ATCC 35406 as compared with the Porphyromonas gingivalis strains ATCC 33277, 16-1, HW24D1, ATCC 49417, W83, W50, and HNA99. The level of hydrolysis of Leu-Asp-MCA by DPP11, Gly-Pro-MCA by DPP4, and Met-Leu-MCA was also higher than in the P. gingivalis strains. MER236725 and MER278904 are P. endodontalis proteins belong to the S9- and S46-family peptidases, respectively. Recombinant MER236725 exhibited enzymatic properties including substrate specificity, and salt- and pH-dependence similar to P. gingivalis DPP5 belonging to the S9 family. However, the kcat/Km figure (194 µM-1·sec-1) for the most potent substrate (Lys-Ala-MCA) was 18.4-fold higher as compared to the P. gingivalis entity (10.5 µM-1·sec-1). In addition, P. endodontalis DPP5 mRNA and protein contents were increased several fold as compared with those in P. gingivalis. Recombinant MER278904 preferentially hydrolyzed Met-Leu-MCA and exhibited a substrate specificity similar to P. gingivalis DPP7 belonging to the S46 family. In accord with the deduced molecular mass of 818 amino acids, a 105-kDa band was immunologically detected, indicating that P. endodontalis DPP7 is an exceptionally large molecule in the DPP7/DPP11/S46 peptidase family. The enhancement of four DPP activities was conclusively demonstrated in P. endodontalis, and remarkable Lys-Ala-MCA-hydrolysis was achieved by qualitative and quantitative potentiation of the DPP5 molecule.
Topics: Amino Acid Sequence; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; Enzyme-Linked Immunosorbent Assay; Isoenzymes; Porphyromonas; Sequence Homology, Amino Acid; Species Specificity
PubMed: 25494328
DOI: 10.1371/journal.pone.0114221 -
Advances in Experimental Medicine and... 2008The capacity of certain pathogens to exploit innate immune receptors enables them to undermine immune clearance and persist in their host, often causing disease. Here we... (Review)
Review
The capacity of certain pathogens to exploit innate immune receptors enables them to undermine immune clearance and persist in their host, often causing disease. Here we review subversive interactions of Porphyromonas gingivalis, a major periodontal pathogen, with the complement receptor-3 (CR3; CD11b/CD18) in monocytes/macrophages. Through its cell surface fimbriae, P. gingivalis stimulates Toll-like receptor-2 (TLR2) inside-out signaling which induces the high-affinity conformation of CR3. Although this activates CR3-dependent monocyte adhesion and transendothelial migration, P. gingivalis has co-opted this TLR2 proadhesive pathway for CR3 binding and intracellular entry. In CR3-deficient macrophages, the internalization of P. gingivalis is reduced twofold but its ability to survive intracellularly is reduced 1,000-fold, indicating that CR3 is exploited by the pathogen as a relatively safe portal of entry. The interaction of P. gingivalis fimbriae with CR3 additionally inhibits production of bioactive (p70) interleukin-12, which mediates immune clearance. In vivo blockade of CR3 leads to reduced persistence of P. gingivalis in the mouse host and diminished ability to cause periodontal bone loss, the hallmark of periodontal disease. Strikingly, the ability of P. gingivalis to interact with and exploit CR3 depends upon quantitatively minor components (FimCDE) of its fimbrial structure, which predominantly consists of polymerized fimbrillin (FimA). Indeed, isogenic mutants lacking FimCDE but expressing FimA are dramatically less persistent and virulent than the wildtype organism both in vitro and in vivo. This model of immune evasion through CR3 exploitation by P. gingivalis supports the concept that pathogens evolved to manipulate innate immune function for promoting their adaptive fitness.
Topics: Animals; Fimbriae, Bacterial; Immunity, Innate; Macrophage-1 Antigen; Mice; Models, Immunological; Porphyromonas gingivalis; Virulence
PubMed: 19025124
DOI: 10.1007/978-0-387-78952-1_15 -
The Keio Journal of Medicine Sep 2003Porphyromonas gingivalis (P. gingivalis), a gram-negative anaerobe, is involved in the pathogenesis of periodontal disease, and is found frequently in the subgingival... (Review)
Review
Porphyromonas gingivalis (P. gingivalis), a gram-negative anaerobe, is involved in the pathogenesis of periodontal disease, and is found frequently in the subgingival flora in patients with periodontitis. This organism possesses a variety of virulence factors including lipopolysaccharide, capsular material, fimbriae and proteases (enzymes). Among the P. gingivalis antigens, enzymes such as Arginine-specific gingipains (RgpA, RgpB) and lysine-specific gingipain (Kgp) have been studied for their ability to induce biologically significant antibodies. This review summarizes recent information on the gingipains and their possible application in the development of an anti-P. gingivalis vaccine.
Topics: Adhesins, Bacterial; Animals; Antigens; Bacteroidaceae Infections; Cysteine Endopeptidases; Gingipain Cysteine Endopeptidases; Hemagglutinins; Humans; Phagocytosis; Porphyromonas gingivalis; Protein Structure, Tertiary; Vaccines; Virulence Factors
PubMed: 14529148
DOI: 10.2302/kjm.52.158 -
Hua Xi Kou Qiang Yi Xue Za Zhi = Huaxi... Dec 2017Autophagy is an intracellular conservative degradation pathway. This event has been considered as a key step in host defense against bacterial infection. However,... (Review)
Review
Autophagy is an intracellular conservative degradation pathway. This event has been considered as a key step in host defense against bacterial infection. However, Porphyromonas gingivalis, as one of the evidence-sufficient periodontal pathogens, can utilize self-induced autophagy to achieve persistent intracellular survival and proliferation, which enable this organism to escape from host immune surveillance. This review focuses on molecular mechanism of P. gingivalis internalization and autophagy to illuminate its pathogenesis and to further explore the relationship between P. gingivalis and systemic diseases.
Topics: Autophagy; Gingiva; Porphyromonas gingivalis; Research
PubMed: 29333782
DOI: 10.7518/hxkq.2017.06.017 -
Biomedical Journal Aug 2016In this issue of the Biomedical Journal, we learn how bacteria and parasites alike counteract inflammatory signaling by manipulating purinergic signaling. We also focus...
In this issue of the Biomedical Journal, we learn how bacteria and parasites alike counteract inflammatory signaling by manipulating purinergic signaling. We also focus on an original article shedding light on the role of an Epstein-Barr virus encoded gene in metastasis in nasopharyngeal carcinoma. Finally, we learn about a possible link between Trichomonas vaginalis and recurrent urinary tract infection.
Topics: Humans; Leishmania; Porphyromonas; Purinergic Agents; Trichomonas
PubMed: 27793264
DOI: 10.1016/j.bj.2016.09.001 -
In vitro anti‑bacterial activity of diosgenin on Porphyromonas gingivalis and Prevotella intermedia.Molecular Medicine Reports Dec 2020Diosgenin (Dios), a natural steroidal sapogenin, is a bioactive compound extracted from dietary fenugreek seeds. It has a wide range of applications, exhibiting...
Diosgenin (Dios), a natural steroidal sapogenin, is a bioactive compound extracted from dietary fenugreek seeds. It has a wide range of applications, exhibiting anti‑oxidant, anti‑inflammatory and anti‑cancer activities. However, whether the extracts have beneficial effects on periodontal pathogens has so far remained elusive. The aim of the present study was to investigate the anti‑bacterial effects of Dios on Porphyromonas gingivalis (P. gingivalis) and Prevotella intermedia (P. intermedia) in vitro. The anti‑microbial effect of Dios on P. gingivalis and P. intermedia was assessed by a direct contact test (DCT) and the Cell Counting Kit (CCK)‑8 assay at 60, 90 and 120 min. In addition, counting of colony‑forming units (CFU) and live/dead cell staining were used to evaluate the anti‑bacterial effects. The results of the DCT and CCK‑8 assays indicated that Dios had beneficial dose‑dependent inhibitory effects on P. gingivalis and P. intermedia. The CFU counting results also indicated that Dios had dose‑dependent anti‑bacterial effects on P. gingivalis and P. intermedia. Of note, Dios had significant anti‑bacterial effects on the biofilms of P. gingivalis and P. intermedia in vitro as visualized by the live/dead cell staining method. In conclusion, the present results demonstrated that Dios had a marked anti‑bacterial activity against P. gingivalis and P. intermedia in vitro, both in suspension and on biofilms. The present study highlighted the potential applications of Dios as a novel natural agent to prevent and treat periodontitis through its anti‑bacterial effects.
Topics: Anti-Bacterial Agents; Biofilms; China; Diosgenin; Microbial Sensitivity Tests; Periodontitis; Porphyromonas gingivalis; Prevotella intermedia
PubMed: 33174005
DOI: 10.3892/mmr.2020.11620 -
Indian Journal of Dental Research :... 2009
Topics: Diabetes Mellitus; Gram-Negative Bacterial Infections; Heart Diseases; Humans; Periodontal Diseases; Porphyromonas endodontalis; Porphyromonas gingivalis; Stroke
PubMed: 19553735
DOI: 10.4103/0970-9290.52880 -
Virulence May 2014There is evidence that advanced infectious chronic periodontal inflammatory disease may have an impact on general health including cardiovascular diseases. The aim of...
BACKGROUND
There is evidence that advanced infectious chronic periodontal inflammatory disease may have an impact on general health including cardiovascular diseases. The aim of this clinical study was to evaluate the ability of Porphyromonas gingivalis to colonize heart valves and, subsequently, to assess whether there is an association between the presence of the DNA of Porphyromonas gingivalis in periodontal pockets and in degenerated heart valves.
MATERIALS AND METHODS
Thirty patients were enrolled in the study and 31 valve specimens harvested during cardiac surgery operations were examined. All patients underwent a periodontal examination. To evaluate the periodontal status of the patients the following clinical parameters were recorded: the pocket depth, bleeding on probing (BOP) and aproximal plaque index (API). The presence of P. gingivalis in heart valve specimens and samples from periodontal pockets was analyzed using a single-step PCR method.
RESULTS
P. gingivalis DNA was detected in periodontal pockets of 15 patients (50%). However, the DNA of this periopathogen was found neither in the aortic nor in the mitral valve specimens.
CONCLUSIONS
This study suggests that P. gingivalis may not have an influence on the development of the degeneration of aortic and mitral valves.
Topics: Aged; Female; Heart Valves; Humans; Male; Middle Aged; Periodontal Pocket; Porphyromonas gingivalis
PubMed: 24705065
DOI: 10.4161/viru.28657 -
Hua Xi Kou Qiang Yi Xue Za Zhi = Huaxi... Aug 2016Chronic periodontitis is one of the most common oral diseases in humans, the main recognized pathogenic bac-terium of which is the Porphyromonas gingivalis. Various... (Review)
Review
Chronic periodontitis is one of the most common oral diseases in humans, the main recognized pathogenic bac-terium of which is the Porphyromonas gingivalis. Various types of viruses have been detected in periodontal disease in situ, and the joint action of viral and bacterial pathogens infection mechanism are complicated. Porphyromonas gingivalis has the characteristics resulting from the interaction with a variety of bacterium viruses, which may be the reason for chronic perio-dontitis being a protracted disease associated with a variety of systemic diseases. In this paper, we reviewed the relationship between Porphyromonas gingivalis and viral diseases to provide a new idea for the treatment of patients with periodontal disease and viral infections.
Topics: Bacteroidaceae Infections; Humans; Porphyromonas gingivalis; Virus Diseases
PubMed: 28317365
DOI: 10.7518/hxkq.2016.04.021 -
Beijing Da Xue Xue Bao. Yi Xue Ban =... Feb 2022To study the binding target of photosensitizer and bacteria in antimicrobial photodynamic therapy with computer-simulated target prediction and molecular docking...
OBJECTIVE
To study the binding target of photosensitizer and bacteria in antimicrobial photodynamic therapy with computer-simulated target prediction and molecular docking research methods and to calculate the binding energy.
METHODS
The protein names of () were obtained and summarized in Uniprot database and RCSB PDB database; the structure diagrams of methy-lene blue were screened in SciFinder database, PubChem database, ChemSpider database, and Chemical Book, and ChemBioDraw software was used to draw and confirm the three-dimensional structure for target prediction and Cytoscape software was used to build a visual network diagram; a protein interaction network was searched and built between the methylene blue target and the common target of in the String database; then we selected FimA, Mfa4, RgpB, and Kgp K1 proteins, used AutoDock software to calculate the docking energy of methylene blue and the above-mentioned proteins and performed molecular docking.
RESULTS
The target prediction results showed that there were 19 common targets between the 268 potential targets of methylene blue and 1 865 proteins. The 19 targets were: groS, radA, rplA, dps, fabH, pyrG, thyA, panC, RHO, frdA, ileS, bioA, def, ddl, TPR, murA, lepB, cobT, and gyrB. The results of the molecular docking showed that methylene blue could bind to 9 sites of FimA protein, with a binding energy of -6.26 kcal/mol; with 4 sites of Mfa4 protein and hydrogen bond formation site GLU47, and the binding energy of -5.91 kcal/mol, the binding energy of LYS80, the hydrogen bond forming site of RgpB protein, was -5.14 kcal/mol, and the binding energy of 6 sites of Kgp K1 protein and the hydrogen bond forming site GLY1114 of -5.07 kcal/mol.
CONCLUSION
Computer simulation of target prediction and molecular docking technology can initially reveal the binding, degree of binding and binding sites of methylene blue and proteins. This method provides a reference for future research on the screening of binding sites of photosensitizers to cells and bacteria.
Topics: Computer Simulation; Methylene Blue; Molecular Docking Simulation; Photosensitizing Agents; Porphyromonas gingivalis
PubMed: 35165464
DOI: 10.19723/j.issn.1671-167X.2022.01.005