f nucleatum  (ATCC)


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    Name:
    Fusobacterium nucleatum subsp nucleatum VPI 4351 1210
    Description:

    Catalog Number:
    23726
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    Structured Review

    ATCC f nucleatum
    Desulfobulbus sp. strain HOT041 ( D. oralis ) in coculture with Fusobacterium <t>nucleatum</t> and in pure culture. (A) FISH using fluorescent oligonucleotide probes specific for Deltaproteobacteria (green) and universal Bacteria (red). (B). Growth of Desulfobulbus sp. strain HOT041 and F. nucleatum in coculture monitored by species-specific qPCR (with error bars based on three replicates). (C and D) Scanning electron micrographs of the D. oralis isolate. The arrowheads point to membrane vesicles.

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    Images

    1) Product Images from "Insights into the Evolution of Host Association through the Isolation and Characterization of a Novel Human Periodontal Pathobiont, Desulfobulbus oralis"

    Article Title: Insights into the Evolution of Host Association through the Isolation and Characterization of a Novel Human Periodontal Pathobiont, Desulfobulbus oralis

    Journal: mBio

    doi: 10.1128/mBio.02061-17

    Desulfobulbus sp. strain HOT041 ( D. oralis ) in coculture with Fusobacterium nucleatum and in pure culture. (A) FISH using fluorescent oligonucleotide probes specific for Deltaproteobacteria (green) and universal Bacteria (red). (B). Growth of Desulfobulbus sp. strain HOT041 and F. nucleatum in coculture monitored by species-specific qPCR (with error bars based on three replicates). (C and D) Scanning electron micrographs of the D. oralis isolate. The arrowheads point to membrane vesicles.
    Figure Legend Snippet: Desulfobulbus sp. strain HOT041 ( D. oralis ) in coculture with Fusobacterium nucleatum and in pure culture. (A) FISH using fluorescent oligonucleotide probes specific for Deltaproteobacteria (green) and universal Bacteria (red). (B). Growth of Desulfobulbus sp. strain HOT041 and F. nucleatum in coculture monitored by species-specific qPCR (with error bars based on three replicates). (C and D) Scanning electron micrographs of the D. oralis isolate. The arrowheads point to membrane vesicles.

    Techniques Used: Fluorescence In Situ Hybridization, Real-time Polymerase Chain Reaction

    2) Product Images from "Identification and characterization of a novel Fusobacterium nucleatum adhesin involved in physical interaction and biofilm formation with Streptococcus gordonii. Identification and characterization of a novel Fusobacterium nucleatum adhesin involved in physical interaction and biofilm formation with Streptococcus gordonii"

    Article Title: Identification and characterization of a novel Fusobacterium nucleatum adhesin involved in physical interaction and biofilm formation with Streptococcus gordonii. Identification and characterization of a novel Fusobacterium nucleatum adhesin involved in physical interaction and biofilm formation with Streptococcus gordonii

    Journal: MicrobiologyOpen

    doi: 10.1002/mbo3.444

    radD and cmpA expression: WT Fusobacterium nucleatum was grown in Columbia broth for 25 hr. Cell samples were collected every 3 hr and (a) OD 600 was measured, as well as (b) radD and cmpA expression by qRT ‐ PCR . Gene expression was normalized to rpoB and compare to the first time point. The dashed line was added to aid in the comparison. (c) radD and cmpA expression were also measured in cells from Fn biofilm grown overnight in SHI ‐ FSMS . Gene expression was normalized to rpoB and compare to planktonic cells grown under the same conditions. Each value represents means and standard deviation of at least three independent experiments. To aid with visualization, the dashed line represents no change
    Figure Legend Snippet: radD and cmpA expression: WT Fusobacterium nucleatum was grown in Columbia broth for 25 hr. Cell samples were collected every 3 hr and (a) OD 600 was measured, as well as (b) radD and cmpA expression by qRT ‐ PCR . Gene expression was normalized to rpoB and compare to the first time point. The dashed line was added to aid in the comparison. (c) radD and cmpA expression were also measured in cells from Fn biofilm grown overnight in SHI ‐ FSMS . Gene expression was normalized to rpoB and compare to planktonic cells grown under the same conditions. Each value represents means and standard deviation of at least three independent experiments. To aid with visualization, the dashed line represents no change

    Techniques Used: Expressing, Quantitative RT-PCR, Standard Deviation

    Quantitative coaggregation of (a) wild‐type ( WT ) Streptococcus gordonii strain V288 and the WT Fusobacterium nucleatum strain ATCC 23726, or the radD mutant derivative, at different phases of growth. (b) Quantitative coaggregation of WT S. gordonii strains ( DL 1, V288, ATCC 10558, and ATCC 51656) with WT F. nucleatum strain ATCC 23726, or the radD mutant derivative at exponential growth. Data represent means and standard deviation of percent coaggregation of at least three independent experiments. * p
    Figure Legend Snippet: Quantitative coaggregation of (a) wild‐type ( WT ) Streptococcus gordonii strain V288 and the WT Fusobacterium nucleatum strain ATCC 23726, or the radD mutant derivative, at different phases of growth. (b) Quantitative coaggregation of WT S. gordonii strains ( DL 1, V288, ATCC 10558, and ATCC 51656) with WT F. nucleatum strain ATCC 23726, or the radD mutant derivative at exponential growth. Data represent means and standard deviation of percent coaggregation of at least three independent experiments. * p

    Techniques Used: Mutagenesis, Standard Deviation

    Quantitative coaggregation of wild‐type Streptococcus gordonii strain (a) V288, (b) ATCC 10558, (c) DL 1, and (d) ATCC 51656 with Fusobacterium nucleatum strains: Wild‐type ( WT ) and the mutant derivatives: radD , cmpA , and radD cmpA double mutant. Data represent means and standard deviation of percent coaggregation of at least three independent experiments. * p
    Figure Legend Snippet: Quantitative coaggregation of wild‐type Streptococcus gordonii strain (a) V288, (b) ATCC 10558, (c) DL 1, and (d) ATCC 51656 with Fusobacterium nucleatum strains: Wild‐type ( WT ) and the mutant derivatives: radD , cmpA , and radD cmpA double mutant. Data represent means and standard deviation of percent coaggregation of at least three independent experiments. * p

    Techniques Used: Mutagenesis, Standard Deviation

    (a) Fusobacterium nucleatum radD cmpA double mutant (strain BL 83) was constructed by insertion of the inactivation plasmid pBPL 9 into cmpA (Fn1554) in a radD::catP mutant background. Black arrows indicate the location of primers used for mutant construction and analysis. (b) Confirmation of plasmid insertion into cmpA by PCR analysis of the cmpA mutant (m) with wild‐type (WT) as the control
    Figure Legend Snippet: (a) Fusobacterium nucleatum radD cmpA double mutant (strain BL 83) was constructed by insertion of the inactivation plasmid pBPL 9 into cmpA (Fn1554) in a radD::catP mutant background. Black arrows indicate the location of primers used for mutant construction and analysis. (b) Confirmation of plasmid insertion into cmpA by PCR analysis of the cmpA mutant (m) with wild‐type (WT) as the control

    Techniques Used: Mutagenesis, Construct, Plasmid Preparation, Polymerase Chain Reaction

    Streptococcus gordonii and Fusobacterium nucleatum dual‐species biofilm: (a) Confocal laser scanning microscopy of syto9‐stained dual‐species biofilm after overnight incubation. S. gordonii (Sg) cells constitutively express mCherry from their chromosome and appear orange/yellow on the images. Wild‐type ( WT ) F. nucleatum (Fn) and its mutant derivatives ( radD , cmpA , and radD cmpA double mutant) are strained by syto9‐only and appear green on the images. (b) The presence of the Fn mutant strains in the Sg‐Fn dual‐species biofilm is displayed as the percentage of Fn cells normalized to the number of attached Sg cells/well, compared to that measured with WT Fn. Cellular ratios were determined by measuring DNA concentration by qPCR , targeting the F. nucleatum gene fomA and the S. gordonii gene srtA . At least three independent experiments were performed per strain combination. Each value represents means and standard deviation of at least three independent experiments. * p
    Figure Legend Snippet: Streptococcus gordonii and Fusobacterium nucleatum dual‐species biofilm: (a) Confocal laser scanning microscopy of syto9‐stained dual‐species biofilm after overnight incubation. S. gordonii (Sg) cells constitutively express mCherry from their chromosome and appear orange/yellow on the images. Wild‐type ( WT ) F. nucleatum (Fn) and its mutant derivatives ( radD , cmpA , and radD cmpA double mutant) are strained by syto9‐only and appear green on the images. (b) The presence of the Fn mutant strains in the Sg‐Fn dual‐species biofilm is displayed as the percentage of Fn cells normalized to the number of attached Sg cells/well, compared to that measured with WT Fn. Cellular ratios were determined by measuring DNA concentration by qPCR , targeting the F. nucleatum gene fomA and the S. gordonii gene srtA . At least three independent experiments were performed per strain combination. Each value represents means and standard deviation of at least three independent experiments. * p

    Techniques Used: Confocal Laser Scanning Microscopy, Staining, Incubation, Mutagenesis, Concentration Assay, Real-time Polymerase Chain Reaction, Standard Deviation

    Quantitative coaggregation of wild‐type ( WT ) Streptococcus gordonii strain V288 with Fusobacterium nucleatum ATCC 23726 WT strain and OMP mutant derivatives ( radD , Fn254, cmpA , Fn1893, Fn2047, and aim1 ). Data represent means and standard deviation of percent coaggregation of at least three independent experiments. * p
    Figure Legend Snippet: Quantitative coaggregation of wild‐type ( WT ) Streptococcus gordonii strain V288 with Fusobacterium nucleatum ATCC 23726 WT strain and OMP mutant derivatives ( radD , Fn254, cmpA , Fn1893, Fn2047, and aim1 ). Data represent means and standard deviation of percent coaggregation of at least three independent experiments. * p

    Techniques Used: Mutagenesis, Standard Deviation

    3) Product Images from "Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease"

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0111329

    Fu-S-P activity correlates with the number of F. nucleatum cells. Fu-S-P (0.03 mM) was incubated for 2 hrs with increasing numbers of washed F. nucleatum cells. Relative Fluorescent Units (RFU) were determined as described in Materials and Methods. No activity was observed with boiled cells.
    Figure Legend Snippet: Fu-S-P activity correlates with the number of F. nucleatum cells. Fu-S-P (0.03 mM) was incubated for 2 hrs with increasing numbers of washed F. nucleatum cells. Relative Fluorescent Units (RFU) were determined as described in Materials and Methods. No activity was observed with boiled cells.

    Techniques Used: Activity Assay, Incubation

    PMSF inhibits growth of F. nucleatum but not of E. coli . (A) Growth of F. nucleatum 12230 (black line) is inhibited by PMSF (solid green line), but this inhibition is relieved by P. gingivalis supernatant (SN Pg) containing PMSF-resistant cysteine proteases (broken green line). (B) Growth of E. coli is not affected by PMSF, ruling out PMSF toxicity. *P
    Figure Legend Snippet: PMSF inhibits growth of F. nucleatum but not of E. coli . (A) Growth of F. nucleatum 12230 (black line) is inhibited by PMSF (solid green line), but this inhibition is relieved by P. gingivalis supernatant (SN Pg) containing PMSF-resistant cysteine proteases (broken green line). (B) Growth of E. coli is not affected by PMSF, ruling out PMSF toxicity. *P

    Techniques Used: Inhibition

    Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).
    Figure Legend Snippet: Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).

    Techniques Used: Mass Spectrometry

    PMSF inhibits the proteolytic activity of F. nucleatum . A, F. nucleatum FDC 364. B, F. nucleatum ATCC 25586. C, F. nucleatum 12230. D, F. nucleatum ATCC 23726. M, Molecular weight markers. Presented data are of representative zymograms.
    Figure Legend Snippet: PMSF inhibits the proteolytic activity of F. nucleatum . A, F. nucleatum FDC 364. B, F. nucleatum ATCC 25586. C, F. nucleatum 12230. D, F. nucleatum ATCC 23726. M, Molecular weight markers. Presented data are of representative zymograms.

    Techniques Used: Activity Assay, Molecular Weight

    Self-restriction of Fsp25586 is not efficient. Zymogram analysis of cell culture supernatant prepared from F. nucleatum ATCC 23726 carrying the pHS30 vector (A), or the pHSPROT plasmid expressing Fsp25586 (B).
    Figure Legend Snippet: Self-restriction of Fsp25586 is not efficient. Zymogram analysis of cell culture supernatant prepared from F. nucleatum ATCC 23726 carrying the pHS30 vector (A), or the pHSPROT plasmid expressing Fsp25586 (B).

    Techniques Used: Cell Culture, Plasmid Preparation, Expressing

    Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.
    Figure Legend Snippet: Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.

    Techniques Used: Molecular Weight

    4) Product Images from "Mechanisms by which Porphyromonas gingivalis evades innate immunity"

    Article Title: Mechanisms by which Porphyromonas gingivalis evades innate immunity

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0182164

    Differential effect of P . gingivalis W50 substrains on extinguishing cytokine production from DCs. (A) DCs from B10.A-Rag2 -/- mice were either unstimulated (medium) or stimulated on the sixth day with 5x10 7 E. coli , F. nucleatum or P. gingivalis alone or a mixture of two bacteria together in a 24-well plate for 16 h at 37°C. CSN were analyzed for the presence of IL-12p75 using a specific ELISA. (B) Same as (A) except that IFNγ was added to the cultures to enhance IL-12 production. P. gingivalis were heat-killed at 60°C for 1 h in a water bath (HKP g) , or not, before being added at 5x10 7 /well to the culture containing F. nucleatum or E. coli . (C) DCs were stimulated with 100 ng/ml of LPS ( E . coli ) plus 100 ng/ml of IFNγ alone (No Pg ) or in combination with various strains of P. gingivalis at 5x10 7 /well for 24 h before testing for the presence of IL-12p75 in the CSN. (D) Same as (C) except various numbers of P. gingivalis W50-NIDCR or -ATCC were added to the DCs in a 24-well plate. (A-D) Data are the mean ± SD of compilation of two independent experiments. (D) The data are expressed as the mean ± SD of duplicates.
    Figure Legend Snippet: Differential effect of P . gingivalis W50 substrains on extinguishing cytokine production from DCs. (A) DCs from B10.A-Rag2 -/- mice were either unstimulated (medium) or stimulated on the sixth day with 5x10 7 E. coli , F. nucleatum or P. gingivalis alone or a mixture of two bacteria together in a 24-well plate for 16 h at 37°C. CSN were analyzed for the presence of IL-12p75 using a specific ELISA. (B) Same as (A) except that IFNγ was added to the cultures to enhance IL-12 production. P. gingivalis were heat-killed at 60°C for 1 h in a water bath (HKP g) , or not, before being added at 5x10 7 /well to the culture containing F. nucleatum or E. coli . (C) DCs were stimulated with 100 ng/ml of LPS ( E . coli ) plus 100 ng/ml of IFNγ alone (No Pg ) or in combination with various strains of P. gingivalis at 5x10 7 /well for 24 h before testing for the presence of IL-12p75 in the CSN. (D) Same as (C) except various numbers of P. gingivalis W50-NIDCR or -ATCC were added to the DCs in a 24-well plate. (A-D) Data are the mean ± SD of compilation of two independent experiments. (D) The data are expressed as the mean ± SD of duplicates.

    Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay

    5) Product Images from "Granulocyte-Macrophage Colony-Stimulating Factor Amplification of Interleukin-1? and Tumor Necrosis Factor Alpha Production in THP-1 Human Monocytic Cells Stimulated with Lipopolysaccharide of Oral Microorganisms"

    Article Title: Granulocyte-Macrophage Colony-Stimulating Factor Amplification of Interleukin-1? and Tumor Necrosis Factor Alpha Production in THP-1 Human Monocytic Cells Stimulated with Lipopolysaccharide of Oral Microorganisms

    Journal: Clinical and Diagnostic Laboratory Immunology

    doi:

    Agarose (1.2%) gel stained with ethidium bromide displaying the 250-bp TNF-α RT-PCR product from treated and untreated THP-1 cells. Lanes: 1, 100-bp DNA ladder; 2, untreated THP-1 cells; 3, GM-CSF (50 IU/ml)-treated THP-1 cells; 4, F. nucleatum LPS (1 μg/ml)-treated (2 h) THP-1 cells; 5, P. gingivalis LPS (1 μg/ml)-treated (2 h) THP-1 cells; 6, F. nucleatum -plus-GM-CSF-treated (2 h) THP-1 cells; 7, P. gingivalis LPS-plus-GM-CSF-treated (2 h) THP-1 cells; 8, PMA-treated (2 h) THP-1 cells.
    Figure Legend Snippet: Agarose (1.2%) gel stained with ethidium bromide displaying the 250-bp TNF-α RT-PCR product from treated and untreated THP-1 cells. Lanes: 1, 100-bp DNA ladder; 2, untreated THP-1 cells; 3, GM-CSF (50 IU/ml)-treated THP-1 cells; 4, F. nucleatum LPS (1 μg/ml)-treated (2 h) THP-1 cells; 5, P. gingivalis LPS (1 μg/ml)-treated (2 h) THP-1 cells; 6, F. nucleatum -plus-GM-CSF-treated (2 h) THP-1 cells; 7, P. gingivalis LPS-plus-GM-CSF-treated (2 h) THP-1 cells; 8, PMA-treated (2 h) THP-1 cells.

    Techniques Used: Staining, Reverse Transcription Polymerase Chain Reaction

    Different dose-response experiments for IL-1β assay. THP-1 cells (10 6 /ml) were treated with different doses of GM-CSF for 24 h, PMA for 12 h, F. nucleatum LPS for 8 h, and P. gingivalis LPS for 8 h, and supernatant fluids were tested for IL-1β. A GM-CSF concentration (concn) of 50 IU/ml was chosen for future experimentation. A PMA concentration of 10 −8 mol/ml was chosen as optimal. One microgram of F. nucleatum or P. gingivalis LPS was used for IL-1β stimulation.
    Figure Legend Snippet: Different dose-response experiments for IL-1β assay. THP-1 cells (10 6 /ml) were treated with different doses of GM-CSF for 24 h, PMA for 12 h, F. nucleatum LPS for 8 h, and P. gingivalis LPS for 8 h, and supernatant fluids were tested for IL-1β. A GM-CSF concentration (concn) of 50 IU/ml was chosen for future experimentation. A PMA concentration of 10 −8 mol/ml was chosen as optimal. One microgram of F. nucleatum or P. gingivalis LPS was used for IL-1β stimulation.

    Techniques Used: Concentration Assay

    (A) IL-1β production after F. nucleatum LPS and GM-CSF treatment. Significantly ( P
    Figure Legend Snippet: (A) IL-1β production after F. nucleatum LPS and GM-CSF treatment. Significantly ( P

    Techniques Used:

    Different dose-response experiments for TNF-α assay. THP-1 cells (10 6 /ml) were treated with different doses of GM-CSF for 24 h, PMA for 12 h, and F. nucleatum or P. gingivalis LPS for 8 h, and supernatant fluids were tested for TNF-α. A 50-IU/ml GM-CSF concentration (concn) was chosen for future experimentation. A 10 −8 mol/ml PMA concentration was chosen as optimal. One microgram of F. nucleatum or P. gingivalis LPS was used for TNF-α stimulation.
    Figure Legend Snippet: Different dose-response experiments for TNF-α assay. THP-1 cells (10 6 /ml) were treated with different doses of GM-CSF for 24 h, PMA for 12 h, and F. nucleatum or P. gingivalis LPS for 8 h, and supernatant fluids were tested for TNF-α. A 50-IU/ml GM-CSF concentration (concn) was chosen for future experimentation. A 10 −8 mol/ml PMA concentration was chosen as optimal. One microgram of F. nucleatum or P. gingivalis LPS was used for TNF-α stimulation.

    Techniques Used: Concentration Assay

    (A) TNF-α production after treatment with F. nucleatum LPS and/or GM-CSF. There was a sharp rise in TNF-α production at 4 h of F. nucleatum LPS (1 μg/ml) stimulation, and the level gradually returned to the baseline by 48 h. Significantly ( P
    Figure Legend Snippet: (A) TNF-α production after treatment with F. nucleatum LPS and/or GM-CSF. There was a sharp rise in TNF-α production at 4 h of F. nucleatum LPS (1 μg/ml) stimulation, and the level gradually returned to the baseline by 48 h. Significantly ( P

    Techniques Used:

    6) Product Images from "Improved antimicrobial effect of ginseng extract by heat transformation"

    Article Title: Improved antimicrobial effect of ginseng extract by heat transformation

    Journal: Journal of Ginseng Research

    doi: 10.1016/j.jgr.2016.03.002

    Membrane potential of Porphyromonas gingivalis , Clostridium perfringens , and Fusobacterium nucleatum treated with HTS-4 and AGS. AGS, Panax quinquefolius leaf-stem; AU, absorbance units; HTS, heat-transformed saponins; MBC, minimum bactericidal concentration; MIC, minimum inhibitory concentration; NC, negative control.
    Figure Legend Snippet: Membrane potential of Porphyromonas gingivalis , Clostridium perfringens , and Fusobacterium nucleatum treated with HTS-4 and AGS. AGS, Panax quinquefolius leaf-stem; AU, absorbance units; HTS, heat-transformed saponins; MBC, minimum bactericidal concentration; MIC, minimum inhibitory concentration; NC, negative control.

    Techniques Used: Transformation Assay, Concentration Assay, Negative Control

    Protein release. Release of protein from (A) Porphyromonas gingivalis , (B) Clostridium perfringens , and (C) Fusobacterium nucleatum treated with HTS-4 and AGS. AGS, Panax quinquefolius leaf-stem; HTS, heat-transformed saponins; MBC, minimum bactericidal concentration; MIC, minimum inhibitory concentration; NC, negative control.
    Figure Legend Snippet: Protein release. Release of protein from (A) Porphyromonas gingivalis , (B) Clostridium perfringens , and (C) Fusobacterium nucleatum treated with HTS-4 and AGS. AGS, Panax quinquefolius leaf-stem; HTS, heat-transformed saponins; MBC, minimum bactericidal concentration; MIC, minimum inhibitory concentration; NC, negative control.

    Techniques Used: Transformation Assay, Concentration Assay, Negative Control

    Nucleic acid absorbance. Release of 260-nm absorbing material from (A) Porphyromonas gingivalis , (B) Clostridium perfringens , and (C) Fusobacterium nucleatum treated with HTS-4 and AGS. AGS, Panax quinquefolius leaf-stem; HTS, heat-transformed saponins; MBC, minimum bactericidal concentration; MIC, minimum inhibitory concentration; NC, negative control.
    Figure Legend Snippet: Nucleic acid absorbance. Release of 260-nm absorbing material from (A) Porphyromonas gingivalis , (B) Clostridium perfringens , and (C) Fusobacterium nucleatum treated with HTS-4 and AGS. AGS, Panax quinquefolius leaf-stem; HTS, heat-transformed saponins; MBC, minimum bactericidal concentration; MIC, minimum inhibitory concentration; NC, negative control.

    Techniques Used: Transformation Assay, Concentration Assay, Negative Control

    7) Product Images from "Regulation of the Peptidoglycan Amidase PGLYRP2 in Epithelial Cells by Interleukin-36γ"

    Article Title: Regulation of the Peptidoglycan Amidase PGLYRP2 in Epithelial Cells by Interleukin-36γ

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00384-18

    Stimulation of PGLYRP2 and hBD2 expression in oral epithelial cells by bacteria. (A and B) TIGK cells were cultured with wild-type P. gingivalis or P. gingivalis KDP136 (Kgp/Rgp-null mutant) at an MOI of 100:1 for the times indicated. PGLYRP2 (A) and hBD2 (B) mRNA levels were then measured ( n = 3). (C to H) TIGK cells were cultured with F. nucleatum (C and F), S. gordonii (D and G), and S. sanguinis (E and H) at an MOI of 100:1 for the times indicated. PGLYRP2 (C to E) and hBD2 (F to H) mRNA levels were then measured ( n = 3). ***, P
    Figure Legend Snippet: Stimulation of PGLYRP2 and hBD2 expression in oral epithelial cells by bacteria. (A and B) TIGK cells were cultured with wild-type P. gingivalis or P. gingivalis KDP136 (Kgp/Rgp-null mutant) at an MOI of 100:1 for the times indicated. PGLYRP2 (A) and hBD2 (B) mRNA levels were then measured ( n = 3). (C to H) TIGK cells were cultured with F. nucleatum (C and F), S. gordonii (D and G), and S. sanguinis (E and H) at an MOI of 100:1 for the times indicated. PGLYRP2 (C to E) and hBD2 (F to H) mRNA levels were then measured ( n = 3). ***, P

    Techniques Used: Expressing, Cell Culture, Mutagenesis

    8) Product Images from "Vaccination targeting surface FomA of Fusobacterium nucleatum against bacterial co-aggregation: implication for treatment of periodontal infection and halitosis"

    Article Title: Vaccination targeting surface FomA of Fusobacterium nucleatum against bacterial co-aggregation: implication for treatment of periodontal infection and halitosis

    Journal: Vaccine

    doi: 10.1016/j.vaccine.2010.02.047

    Blockage of VSC production using neutralizing antibodies to FomA. Detection of VSC production of F. nucleatum ( F.n ), P. gingivalis ( P.g ) and F. nucleatum plus P. gingivalis ( F.n + P.g ) in the absence (A) or presence of (B) anti-FomA or anti-GFP serum.
    Figure Legend Snippet: Blockage of VSC production using neutralizing antibodies to FomA. Detection of VSC production of F. nucleatum ( F.n ), P. gingivalis ( P.g ) and F. nucleatum plus P. gingivalis ( F.n + P.g ) in the absence (A) or presence of (B) anti-FomA or anti-GFP serum.

    Techniques Used:

    The co-aggregation of F. nucleatum with P. gingivalis and biofilm enhancement. The detection of bacterial co-aggregation and biofilm formation is described in “Materials and methods”. (A) F. nucleatum ( F.n ), P. gingivalis ( P.g ), and F.
    Figure Legend Snippet: The co-aggregation of F. nucleatum with P. gingivalis and biofilm enhancement. The detection of bacterial co-aggregation and biofilm formation is described in “Materials and methods”. (A) F. nucleatum ( F.n ), P. gingivalis ( P.g ), and F.

    Techniques Used:

    Abrogation of bacteria-induced gum swelling via passive neutralization of FomA. After pre-treatment of F. nucleatum (4 × 10 8 CFU) with anti-FomA or anti-GFP serum, bacteria were incubated with P. gingivalis (10 3 CFU) in PBS for 3 h. Both bacteria
    Figure Legend Snippet: Abrogation of bacteria-induced gum swelling via passive neutralization of FomA. After pre-treatment of F. nucleatum (4 × 10 8 CFU) with anti-FomA or anti-GFP serum, bacteria were incubated with P. gingivalis (10 3 CFU) in PBS for 3 h. Both bacteria

    Techniques Used: Neutralization, Incubation

    ] with abscesses and swollen tissues was used for evaluation of the in vivo efficacy of vaccination. (A) After inoculation with live bacteria F. nucleatum (4 ×
    Figure Legend Snippet: ] with abscesses and swollen tissues was used for evaluation of the in vivo efficacy of vaccination. (A) After inoculation with live bacteria F. nucleatum (4 ×

    Techniques Used: In Vivo

    9) Product Images from "Differential and coordinated expression of defensins and cytokines by gingival epithelial cells and dendritic cells in response to oral bacteria"

    Article Title: Differential and coordinated expression of defensins and cytokines by gingival epithelial cells and dendritic cells in response to oral bacteria

    Journal: BMC Immunology

    doi: 10.1186/1471-2172-11-37

    Differential defensins expression in response to oral bacteria by DCs and GECs . DCs ( A, B, C ) and GECs ( D, E, F ) were stimulated with graded doses of oral bacteria cell wall extracts ( A. naeslundii , AnCW; F. nucleatum , FnCW; and P. gingivalis , PgCW) for 24 h. The gene expression of hBD1, 2, and 3 was quantified by quantitative real-time PCR. LPS was used as a positive control. A, D . hBD1 expression; B, E . hBD2 expression; C. F . hBD3 expression. Results are shown as mean fold change ± SEM over unstimulated controls. The data are average of three independent experiments performed in duplicate. GECs were stimulated with bacterial preparation for 24 and 48 h. Proteins were harvested, and hBD2 and hBD3 proteins in GECs were measured by ELISA ( G, H ). The concentration of defensins range was pg/ml. Inductions of hBD2 and hBD3 proteins are as fold induction relative to unstimulated controls. The data are average of two independent experiments performed in duplicate. Error bars represent the mean ± SEM. Asterisks indicate statistically significant difference compared to unstimulated control (Ctl) (*p
    Figure Legend Snippet: Differential defensins expression in response to oral bacteria by DCs and GECs . DCs ( A, B, C ) and GECs ( D, E, F ) were stimulated with graded doses of oral bacteria cell wall extracts ( A. naeslundii , AnCW; F. nucleatum , FnCW; and P. gingivalis , PgCW) for 24 h. The gene expression of hBD1, 2, and 3 was quantified by quantitative real-time PCR. LPS was used as a positive control. A, D . hBD1 expression; B, E . hBD2 expression; C. F . hBD3 expression. Results are shown as mean fold change ± SEM over unstimulated controls. The data are average of three independent experiments performed in duplicate. GECs were stimulated with bacterial preparation for 24 and 48 h. Proteins were harvested, and hBD2 and hBD3 proteins in GECs were measured by ELISA ( G, H ). The concentration of defensins range was pg/ml. Inductions of hBD2 and hBD3 proteins are as fold induction relative to unstimulated controls. The data are average of two independent experiments performed in duplicate. Error bars represent the mean ± SEM. Asterisks indicate statistically significant difference compared to unstimulated control (Ctl) (*p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Positive Control, Enzyme-linked Immunosorbent Assay, Concentration Assay, CTL Assay

    Array analysis of the released cytokines and chemokines in response to F. nucleatum and P. gingivalis in DCs and GECs . Each cytokine or chemokine is represented by duplicate spots. Supernatants (1 ml) of unstimulated cells or cells stimulated for 24 h with FnCW or PgCW were applied to RayBio human cytokine protein array III as described in Materials and Methods. The rectangles in the upper left and lower right portions of the arrays indicate positive controls. The upregulated cytokines and chemokines are indicated by solid rectangles; down-regulated or absent products are indicated by dashed rectangles. The cytokine array image represents one of two independent experiments ( A, B ). ENA-78, epithelial neutrophil-activating protein 78; GRO, growth regulated oncogene; MCP, macrophage colony stimulating factor; MDC, macrophage-derived chemoattractant; SDF-1, stromal cell-derived factor; TARC, thymus and activation-regulated chemokine. Note the upregulation of IL-1β in DCs with both bacterial preparations (bold rectangle). C . IL-1β in the cultured media from DCs after FnCW or PgCW stimulation. The cells were stimulated with FnCW or PgCW at the indicated dose and time points. The culture media were collected and IL-1β was quantified by ELISA. Results are represented as mean ± SD for two determinations in a representative experiment. Similar results were obtained with conditioned media from three different donors. (**: p
    Figure Legend Snippet: Array analysis of the released cytokines and chemokines in response to F. nucleatum and P. gingivalis in DCs and GECs . Each cytokine or chemokine is represented by duplicate spots. Supernatants (1 ml) of unstimulated cells or cells stimulated for 24 h with FnCW or PgCW were applied to RayBio human cytokine protein array III as described in Materials and Methods. The rectangles in the upper left and lower right portions of the arrays indicate positive controls. The upregulated cytokines and chemokines are indicated by solid rectangles; down-regulated or absent products are indicated by dashed rectangles. The cytokine array image represents one of two independent experiments ( A, B ). ENA-78, epithelial neutrophil-activating protein 78; GRO, growth regulated oncogene; MCP, macrophage colony stimulating factor; MDC, macrophage-derived chemoattractant; SDF-1, stromal cell-derived factor; TARC, thymus and activation-regulated chemokine. Note the upregulation of IL-1β in DCs with both bacterial preparations (bold rectangle). C . IL-1β in the cultured media from DCs after FnCW or PgCW stimulation. The cells were stimulated with FnCW or PgCW at the indicated dose and time points. The culture media were collected and IL-1β was quantified by ELISA. Results are represented as mean ± SD for two determinations in a representative experiment. Similar results were obtained with conditioned media from three different donors. (**: p

    Techniques Used: Protein Array, Derivative Assay, Activation Assay, Cell Culture, Enzyme-linked Immunosorbent Assay

    10) Product Images from "The peptidylarginine deiminase gene is a conserved feature of Porphyromonas gingivalis"

    Article Title: The peptidylarginine deiminase gene is a conserved feature of Porphyromonas gingivalis

    Journal: Scientific Reports

    doi: 10.1038/srep13936

    Patterns of citrullinated proteins of P. gingivalis isolates from patients with or without RA. ( A,C,E ) Western blots and Coomassie staining of bacterial cell lysates of 12 representative P. gingivalis isolates of patients with or without RA (both n = 6). ( A ) Citrullinated protein patterns as detected with the AMC detection method (AMC). ( C ) Citrullinated protein patterns as detected with the F95 anti-citrulline antibody (F95). ( E ) Coomassie staining. ( B,D ) Graphical representation of the Western blots shown in panels ( A,C ). ( B ) Citrullinated protein patterns as detected with the AMC detection method (AMC). ( D ) Citrullinated protein patterns as detected with the F95 anti-citrulline antibody (F95). ( F ) Graphical representation of citrullinated protein patterns as detected by Western blots using the F95 anti-citrulline antibody (F95) against bacterial cell lysates of 24 representative P. gingivalis isolates of patients with or without RA (both n = 12). The Western blots were analyzed with the same image display settings. 1 = Molecular weight marker in kilo Dalton (kDa), 2 = P. asaccharolytica, 3 = P. endodontalis, 4 = F. nucleatum, Pg non-RA = P. gingivalis isolates from subjects without RA, Pg RA = P. gingivalis isolates of patients with RA. The strong positive staining at circa 120 kDa in P. endodontalis (3) both with the AMC and the F95 detection method (panels A,C) is due to non-specific binding of the secondary antibody.
    Figure Legend Snippet: Patterns of citrullinated proteins of P. gingivalis isolates from patients with or without RA. ( A,C,E ) Western blots and Coomassie staining of bacterial cell lysates of 12 representative P. gingivalis isolates of patients with or without RA (both n = 6). ( A ) Citrullinated protein patterns as detected with the AMC detection method (AMC). ( C ) Citrullinated protein patterns as detected with the F95 anti-citrulline antibody (F95). ( E ) Coomassie staining. ( B,D ) Graphical representation of the Western blots shown in panels ( A,C ). ( B ) Citrullinated protein patterns as detected with the AMC detection method (AMC). ( D ) Citrullinated protein patterns as detected with the F95 anti-citrulline antibody (F95). ( F ) Graphical representation of citrullinated protein patterns as detected by Western blots using the F95 anti-citrulline antibody (F95) against bacterial cell lysates of 24 representative P. gingivalis isolates of patients with or without RA (both n = 12). The Western blots were analyzed with the same image display settings. 1 = Molecular weight marker in kilo Dalton (kDa), 2 = P. asaccharolytica, 3 = P. endodontalis, 4 = F. nucleatum, Pg non-RA = P. gingivalis isolates from subjects without RA, Pg RA = P. gingivalis isolates of patients with RA. The strong positive staining at circa 120 kDa in P. endodontalis (3) both with the AMC and the F95 detection method (panels A,C) is due to non-specific binding of the secondary antibody.

    Techniques Used: Western Blot, Staining, Molecular Weight, Marker, Binding Assay

    PPAD gene composition analyzed by PCR and restriction enzyme analysis of the PCR products. ( A ) PCR products of PPAD obtained with whole-gene primers (1668 base pairs) using 10 representative P. gingivalis isolates of patients without RA. No PPAD genes are detectable in other Porphyromonas species or other selected periodontal pathogens. ( B ) PCR products of PPAD obtained with active site region primers (328 base pairs) of 14 representative P. gingivalis isolates from patients without RA. No PPAD genes are detectable in other Porphyromonas species or other selected periodontal pathogens. ( C ) Restriction enzyme analysis with Sau 3AI of PPAD PCR products obtained with whole-gene primers of 13 representative P. gingivalis isolates from patients without RA. ( D ) PPAD PCR products obtained with whole-gene primers of 14 representative P. gingivalis isolates from patients with or without RA. M = marker displayed as number of base pairs (GeneRuler™ 1 kb Plus DNA ladder). C 1 = positive control (PPAD of P. gingivalis W83). C 2 = positive control (PPAD of P. gingivalis ATCC 33277). 1 = P. intermedia , 2 = P. asaccharolytica , 3 = P. endodontalis and 4 = F. nucleatum. Digested = PPAD PCR products digested with Sau 3AI. Undigested = PPAD PCR products of the same 13 P. gingivalis clinical isolates not incubated with Sau 3AI. non-RA = without rheumatoid arthritis. RA = with rheumatoid arthritis.
    Figure Legend Snippet: PPAD gene composition analyzed by PCR and restriction enzyme analysis of the PCR products. ( A ) PCR products of PPAD obtained with whole-gene primers (1668 base pairs) using 10 representative P. gingivalis isolates of patients without RA. No PPAD genes are detectable in other Porphyromonas species or other selected periodontal pathogens. ( B ) PCR products of PPAD obtained with active site region primers (328 base pairs) of 14 representative P. gingivalis isolates from patients without RA. No PPAD genes are detectable in other Porphyromonas species or other selected periodontal pathogens. ( C ) Restriction enzyme analysis with Sau 3AI of PPAD PCR products obtained with whole-gene primers of 13 representative P. gingivalis isolates from patients without RA. ( D ) PPAD PCR products obtained with whole-gene primers of 14 representative P. gingivalis isolates from patients with or without RA. M = marker displayed as number of base pairs (GeneRuler™ 1 kb Plus DNA ladder). C 1 = positive control (PPAD of P. gingivalis W83). C 2 = positive control (PPAD of P. gingivalis ATCC 33277). 1 = P. intermedia , 2 = P. asaccharolytica , 3 = P. endodontalis and 4 = F. nucleatum. Digested = PPAD PCR products digested with Sau 3AI. Undigested = PPAD PCR products of the same 13 P. gingivalis clinical isolates not incubated with Sau 3AI. non-RA = without rheumatoid arthritis. RA = with rheumatoid arthritis.

    Techniques Used: Polymerase Chain Reaction, Marker, Positive Control, Incubation

    11) Product Images from "Antibacterial activity and cytocompatibility of an implant coating consisting of TiO2 nanotubes combined with a GL13K antimicrobial peptide"

    Article Title: Antibacterial activity and cytocompatibility of an implant coating consisting of TiO2 nanotubes combined with a GL13K antimicrobial peptide

    Journal: International Journal of Nanomedicine

    doi: 10.2147/IJN.S128775

    Evaluation of antimicrobial activity of the MNA-TNTs, GL13K-TNTs, and TNTs against ( A ) Porphyromonas gingivalis ATCC 33277 and ( B ) Fusobacterium nucleatum ATCC 25586, assessed using disk-diffusion assay. Abbreviations: MNA, metronidazole; MNA-TNTs, MNA-immobilized TNTs; TNTs, TiO 2 nanotubes; ATCC, American Type Culture Collection.
    Figure Legend Snippet: Evaluation of antimicrobial activity of the MNA-TNTs, GL13K-TNTs, and TNTs against ( A ) Porphyromonas gingivalis ATCC 33277 and ( B ) Fusobacterium nucleatum ATCC 25586, assessed using disk-diffusion assay. Abbreviations: MNA, metronidazole; MNA-TNTs, MNA-immobilized TNTs; TNTs, TiO 2 nanotubes; ATCC, American Type Culture Collection.

    Techniques Used: Activity Assay, Diffusion-based Assay

    12) Product Images from "Fusobacterium nucleatum-associated ?-Defensin Inducer (FAD-I)"

    Article Title: Fusobacterium nucleatum-associated ?-Defensin Inducer (FAD-I)

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.133140

    RT-PCR analysis of hBD2 mRNA induction in HOECs at different steps of purification. A , RT-PCR analysis was performed with RNA from HOEC monolayers treated with phorbol 12-myristate 13-acetate ( PMA ) as positive control ( lane 2 ) or 10 μg of F. nucleatum
    Figure Legend Snippet: RT-PCR analysis of hBD2 mRNA induction in HOECs at different steps of purification. A , RT-PCR analysis was performed with RNA from HOEC monolayers treated with phorbol 12-myristate 13-acetate ( PMA ) as positive control ( lane 2 ) or 10 μg of F. nucleatum

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Purification, Positive Control

    Induction of hBD2 mRNA and protein by Pg1527 . A , Western blot analysis of cell wall preparations from P. gingivalis transformed with FN1527 ( Pg + 1527 ), P. gingivalis transformed with vector only ( Pg + vector ), F. nucleatum 25586 cell wall ( Fn ), or P.
    Figure Legend Snippet: Induction of hBD2 mRNA and protein by Pg1527 . A , Western blot analysis of cell wall preparations from P. gingivalis transformed with FN1527 ( Pg + 1527 ), P. gingivalis transformed with vector only ( Pg + vector ), F. nucleatum 25586 cell wall ( Fn ), or P.

    Techniques Used: Western Blot, Transformation Assay, Plasmid Preparation

    HOEC expression of hBD2 following challenge by cell extracts from E. coli expressing different F. nucleatum recombinant proteins and induction of hBD2 by affinity-purified FN1527 c-Myc. A , HOECs were treated with extracts (100 μg/ml total protein)
    Figure Legend Snippet: HOEC expression of hBD2 following challenge by cell extracts from E. coli expressing different F. nucleatum recombinant proteins and induction of hBD2 by affinity-purified FN1527 c-Myc. A , HOECs were treated with extracts (100 μg/ml total protein)

    Techniques Used: Expressing, Recombinant, Affinity Purification

    F. nucleatum cell wall and FAD-I induce hBD2 via TLR2. HOECs were treated with 5 μg/ml anti-TLR2 antibody or isotype control for 30 min and then stimulated with either 10 μg/ml F. nucleatum cell wall ( Fn-CW ) ( A ) or 10 μg/ml 1527
    Figure Legend Snippet: F. nucleatum cell wall and FAD-I induce hBD2 via TLR2. HOECs were treated with 5 μg/ml anti-TLR2 antibody or isotype control for 30 min and then stimulated with either 10 μg/ml F. nucleatum cell wall ( Fn-CW ) ( A ) or 10 μg/ml 1527

    Techniques Used:

    13) Product Images from "Assessment of the involvement of the macrophage migration inhibitory factor (MIF)-glucocorticoid regulatory dyad in MMP2 expression during periodontitis"

    Article Title: Assessment of the involvement of the macrophage migration inhibitory factor (MIF)-glucocorticoid regulatory dyad in MMP2 expression during periodontitis

    Journal: European journal of oral sciences

    doi: 10.1111/eos.12363

    Levels of proinflammatory IL6 in vivo and in vitro . A and B: Local tissue Il6 mRNA levels in healthy and inflamed gingivae nine days after ligature placement are shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). * P =0.05, ** P =0.006 for healthy vs . inflamed tissues in WT and MIF KO mice and ** P =0.01 for inflamed sites in WT vs . MIF KO animals. Grey bars: WT mice (n=6), white bars: MIF KO mice (n=6). Results are shown as mean values ±SD, each sample was run in duplicate. C: Levels of IL6 released from HGFs after stimulation with HC, MIF or F. nucleatum (* P ) was employed. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.
    Figure Legend Snippet: Levels of proinflammatory IL6 in vivo and in vitro . A and B: Local tissue Il6 mRNA levels in healthy and inflamed gingivae nine days after ligature placement are shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). * P =0.05, ** P =0.006 for healthy vs . inflamed tissues in WT and MIF KO mice and ** P =0.01 for inflamed sites in WT vs . MIF KO animals. Grey bars: WT mice (n=6), white bars: MIF KO mice (n=6). Results are shown as mean values ±SD, each sample was run in duplicate. C: Levels of IL6 released from HGFs after stimulation with HC, MIF or F. nucleatum (* P ) was employed. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.

    Techniques Used: In Vivo, In Vitro, Mouse Assay

    MIF protein release from HGFs. MIF release was inducible by hydrocortisol (HC), but not by TNF-α or F. nucleatum (* P ), were used as a positive control. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.
    Figure Legend Snippet: MIF protein release from HGFs. MIF release was inducible by hydrocortisol (HC), but not by TNF-α or F. nucleatum (* P ), were used as a positive control. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.

    Techniques Used: Positive Control

    MMP2 levels in murine gingival tissues and HGF supernatants. A : Mmp2 mRNA levels in WT and MIF KO mice in healthy and inflamed gingival sites shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). B: MMP2 release by HGFs from five different donors in cell culture experiments in response to hydrocortisol (HC), MIF and F. nucleatum (*** P =0.0003 compared to negative controls), each sample was run in triplicate wells.
    Figure Legend Snippet: MMP2 levels in murine gingival tissues and HGF supernatants. A : Mmp2 mRNA levels in WT and MIF KO mice in healthy and inflamed gingival sites shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). B: MMP2 release by HGFs from five different donors in cell culture experiments in response to hydrocortisol (HC), MIF and F. nucleatum (*** P =0.0003 compared to negative controls), each sample was run in triplicate wells.

    Techniques Used: Mouse Assay, Cell Culture

    14) Product Images from "Er:YAG Laser Irradiation Reduces Microbial Viability When Used in Combination with Irrigation with Sodium Hypochlorite, Chlorhexidine, and Hydrogen Peroxide"

    Article Title: Er:YAG Laser Irradiation Reduces Microbial Viability When Used in Combination with Irrigation with Sodium Hypochlorite, Chlorhexidine, and Hydrogen Peroxide

    Journal: Microorganisms

    doi: 10.3390/microorganisms7120612

    Effectiveness of Er:YAG laser treatment with or without irrigation on viability of F. nucleatum. Bacterial strains were grown anaerobically in BHI broth. For treatment, cultures were aliquoted onto a 96-well plate and treated with laser irradiation, anti-microbial at listed concentration, or combination therapy. Then, all samples were plated on TSA blood agar plates post-treatment. After incubation, colonies were counted to judge the efficiency of treatment. Laser-treated samples were treated with an Er:YAG laser at the following settings: 40 mJ; 40 Hz; 1.6 W, 20 seconds, 300 µs short pulse duration, contact mode. Untreated cultures served as controls. Data is representative of four biological replicates. ( p
    Figure Legend Snippet: Effectiveness of Er:YAG laser treatment with or without irrigation on viability of F. nucleatum. Bacterial strains were grown anaerobically in BHI broth. For treatment, cultures were aliquoted onto a 96-well plate and treated with laser irradiation, anti-microbial at listed concentration, or combination therapy. Then, all samples were plated on TSA blood agar plates post-treatment. After incubation, colonies were counted to judge the efficiency of treatment. Laser-treated samples were treated with an Er:YAG laser at the following settings: 40 mJ; 40 Hz; 1.6 W, 20 seconds, 300 µs short pulse duration, contact mode. Untreated cultures served as controls. Data is representative of four biological replicates. ( p

    Techniques Used: Irradiation, Concentration Assay, Incubation

    15) Product Images from "Fusobacterium nucleatum-associated ?-Defensin Inducer (FAD-I)"

    Article Title: Fusobacterium nucleatum-associated ?-Defensin Inducer (FAD-I)

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.133140

    RT-PCR analysis of hBD2 mRNA induction in HOECs at different steps of purification. A , RT-PCR analysis was performed with RNA from HOEC monolayers treated with phorbol 12-myristate 13-acetate ( PMA ) as positive control ( lane 2 ) or 10 μg of F. nucleatum
    Figure Legend Snippet: RT-PCR analysis of hBD2 mRNA induction in HOECs at different steps of purification. A , RT-PCR analysis was performed with RNA from HOEC monolayers treated with phorbol 12-myristate 13-acetate ( PMA ) as positive control ( lane 2 ) or 10 μg of F. nucleatum

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Purification, Positive Control

    Induction of hBD2 mRNA and protein by Pg1527 . A , Western blot analysis of cell wall preparations from P. gingivalis transformed with FN1527 ( Pg + 1527 ), P. gingivalis transformed with vector only ( Pg + vector ), F. nucleatum 25586 cell wall ( Fn ), or P.
    Figure Legend Snippet: Induction of hBD2 mRNA and protein by Pg1527 . A , Western blot analysis of cell wall preparations from P. gingivalis transformed with FN1527 ( Pg + 1527 ), P. gingivalis transformed with vector only ( Pg + vector ), F. nucleatum 25586 cell wall ( Fn ), or P.

    Techniques Used: Western Blot, Transformation Assay, Plasmid Preparation

    HOEC expression of hBD2 following challenge by cell extracts from E. coli expressing different F. nucleatum recombinant proteins and induction of hBD2 by affinity-purified FN1527 c-Myc. A , HOECs were treated with extracts (100 μg/ml total protein)
    Figure Legend Snippet: HOEC expression of hBD2 following challenge by cell extracts from E. coli expressing different F. nucleatum recombinant proteins and induction of hBD2 by affinity-purified FN1527 c-Myc. A , HOECs were treated with extracts (100 μg/ml total protein)

    Techniques Used: Expressing, Recombinant, Affinity Purification

    F. nucleatum cell wall and FAD-I induce hBD2 via TLR2. HOECs were treated with 5 μg/ml anti-TLR2 antibody or isotype control for 30 min and then stimulated with either 10 μg/ml F. nucleatum cell wall ( Fn-CW ) ( A ) or 10 μg/ml 1527
    Figure Legend Snippet: F. nucleatum cell wall and FAD-I induce hBD2 via TLR2. HOECs were treated with 5 μg/ml anti-TLR2 antibody or isotype control for 30 min and then stimulated with either 10 μg/ml F. nucleatum cell wall ( Fn-CW ) ( A ) or 10 μg/ml 1527

    Techniques Used:

    16) Product Images from "P. gingivalis Modulates Keratinocytes through FOXO Transcription Factors"

    Article Title: P. gingivalis Modulates Keratinocytes through FOXO Transcription Factors

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0078541

    P. gingivalis but not F. nucleatum or S. gordonii induces expression of differentiation markers. Primary human gingival epithelial cell cultures were incubated with or without exposure to an air-liquid-interface to induce differentiation and then challenged with P. gingivalis (Pg), S. gordonii (Sg), or F. nucleatum (Fn) at 2×10 8 /cm 2 for 24 hrs. mRNA levels of keratin-1 or keratin-10 were measured by real-time PCR. +Significant difference between undifferentiated and differentiated cells (P
    Figure Legend Snippet: P. gingivalis but not F. nucleatum or S. gordonii induces expression of differentiation markers. Primary human gingival epithelial cell cultures were incubated with or without exposure to an air-liquid-interface to induce differentiation and then challenged with P. gingivalis (Pg), S. gordonii (Sg), or F. nucleatum (Fn) at 2×10 8 /cm 2 for 24 hrs. mRNA levels of keratin-1 or keratin-10 were measured by real-time PCR. +Significant difference between undifferentiated and differentiated cells (P

    Techniques Used: Expressing, Incubation, Real-time Polymerase Chain Reaction

    P. gingivalis but not F. nucleatum or S. gordonii induces apoptosis of differentiated multi-layer culture of gingival keratinocytes. P. gingivalis , F. nucleatum and S. gordonii were incubated with multi-layer, differentiated primary human gingival epithelial cells induced by air-liquid interface. Apoptosis was assessed by ELISA measuring cytoplasmic histone-associated DNA. A: Bacterial dose response. B: Incubation with the protease inhibitor leupeptin (100 µM). * Significantly different from matched control (P
    Figure Legend Snippet: P. gingivalis but not F. nucleatum or S. gordonii induces apoptosis of differentiated multi-layer culture of gingival keratinocytes. P. gingivalis , F. nucleatum and S. gordonii were incubated with multi-layer, differentiated primary human gingival epithelial cells induced by air-liquid interface. Apoptosis was assessed by ELISA measuring cytoplasmic histone-associated DNA. A: Bacterial dose response. B: Incubation with the protease inhibitor leupeptin (100 µM). * Significantly different from matched control (P

    Techniques Used: Incubation, Enzyme-linked Immunosorbent Assay, Protease Inhibitor

    P. gingivalis but not F. nucleatum or S. gordonii down-regulates TLR2 and TLR4 mRNA levels. Primary human gingival epithelial cell cultures were incubated with or without exposure to an air-liquid-interface to induce differentiation and then challenged with P. gingivalis (Pg), S. gordonii (Sg), or F. nucleatum (Fn) at 2×10 8 /cm 2 for 20 hrs. mRNA levels of TLR-2 or TLR-4 were measured by real-time PCR. +Significant difference between undifferentiated and differentiated cells (P
    Figure Legend Snippet: P. gingivalis but not F. nucleatum or S. gordonii down-regulates TLR2 and TLR4 mRNA levels. Primary human gingival epithelial cell cultures were incubated with or without exposure to an air-liquid-interface to induce differentiation and then challenged with P. gingivalis (Pg), S. gordonii (Sg), or F. nucleatum (Fn) at 2×10 8 /cm 2 for 20 hrs. mRNA levels of TLR-2 or TLR-4 were measured by real-time PCR. +Significant difference between undifferentiated and differentiated cells (P

    Techniques Used: Incubation, Real-time Polymerase Chain Reaction

    P. gingivalis but not F. nucleatum or S. gordonii induces loss of barrier function. P. gingivalis , F. nucleatum and S. gordonii were tested for loss of barrier function with fluorescein isothiocyanate–dextran (FITC-Dextran) with multi-layer, differentiated primary human gingival epithelial cells induced by air-liquid interface. A: Bacterial dose response. B: Incubation with the protease inhibitor leupeptin (100 µM). * Significantly different from matched control (P
    Figure Legend Snippet: P. gingivalis but not F. nucleatum or S. gordonii induces loss of barrier function. P. gingivalis , F. nucleatum and S. gordonii were tested for loss of barrier function with fluorescein isothiocyanate–dextran (FITC-Dextran) with multi-layer, differentiated primary human gingival epithelial cells induced by air-liquid interface. A: Bacterial dose response. B: Incubation with the protease inhibitor leupeptin (100 µM). * Significantly different from matched control (P

    Techniques Used: Incubation, Protease Inhibitor

    17) Product Images from "Differential effects of periopathogens on host protease inhibitors SLPI, elafin, SCCA1, and SCCA2"

    Article Title: Differential effects of periopathogens on host protease inhibitors SLPI, elafin, SCCA1, and SCCA2

    Journal: Journal of Oral Microbiology

    doi: 10.3402/jom.v2i0.5070

    Recombinant SLPI, elafin, SCCA1, and SCCA2 are degraded by P. gingivalis supernatants in vitro in a dose-dependent manner. Western Blot analysis for each protease inhibitor using a constant concentration of recombinant protease inhibitor incubated with cell-free supernatants of oral bacteria for 15 min at RT. The undiluted supernatant (1×) corresponds to MOI 100; increasing dilution factor is indicated below each protease inhibitor. Protein mixtures were denatured at 70°C for 10 min, separated by electrophoresis, and analyzed by Western Blot. Control: control, recombinant protein only. The controls shown with P. gingivalis also apply to the recombinant proteins treated with T. forsythia and F. nucleatum .
    Figure Legend Snippet: Recombinant SLPI, elafin, SCCA1, and SCCA2 are degraded by P. gingivalis supernatants in vitro in a dose-dependent manner. Western Blot analysis for each protease inhibitor using a constant concentration of recombinant protease inhibitor incubated with cell-free supernatants of oral bacteria for 15 min at RT. The undiluted supernatant (1×) corresponds to MOI 100; increasing dilution factor is indicated below each protease inhibitor. Protein mixtures were denatured at 70°C for 10 min, separated by electrophoresis, and analyzed by Western Blot. Control: control, recombinant protein only. The controls shown with P. gingivalis also apply to the recombinant proteins treated with T. forsythia and F. nucleatum .

    Techniques Used: Recombinant, In Vitro, Western Blot, Protease Inhibitor, Concentration Assay, Incubation, Electrophoresis

    P. gingivalis supernatant significantly induced mRNA gene expression of epithelial protease inhibitors (SLPI, elafin, SCCA1, and SCCA2). GECs were stimulated with cell-free supernatants of P. gingivalis (Pg), P. gingivalis mutant KDP112 (Pg−/−), T. forsythia (Tf) A. actinomycetemcomitans (Aa), and whole bacterial F. nucleatum (Fn) at MOIs of 100 or equivalent for 24 h. Change of mRNA expression was evaluated by QRT-PCR and results are expressed as fold change in gene expression compared with the unstimulated control after normalization with the housekeeping gene ribosomal phosphoprotein (RPO). The change of gene expression of SLPI, elafin, SCCA1, and SCCA2 was minimal in GEC stimulated by Fn, Aa, Tf, Pg−/− compared to the unstimulated control (inset of Fig. 1 ). TLCK pre-incubated with P. gingivalis supernatant blocked upregulation. The data are derived from three different cell donors tested in duplicate. Error bars indicate SEM (standard error of the mean).
    Figure Legend Snippet: P. gingivalis supernatant significantly induced mRNA gene expression of epithelial protease inhibitors (SLPI, elafin, SCCA1, and SCCA2). GECs were stimulated with cell-free supernatants of P. gingivalis (Pg), P. gingivalis mutant KDP112 (Pg−/−), T. forsythia (Tf) A. actinomycetemcomitans (Aa), and whole bacterial F. nucleatum (Fn) at MOIs of 100 or equivalent for 24 h. Change of mRNA expression was evaluated by QRT-PCR and results are expressed as fold change in gene expression compared with the unstimulated control after normalization with the housekeeping gene ribosomal phosphoprotein (RPO). The change of gene expression of SLPI, elafin, SCCA1, and SCCA2 was minimal in GEC stimulated by Fn, Aa, Tf, Pg−/− compared to the unstimulated control (inset of Fig. 1 ). TLCK pre-incubated with P. gingivalis supernatant blocked upregulation. The data are derived from three different cell donors tested in duplicate. Error bars indicate SEM (standard error of the mean).

    Techniques Used: Expressing, Mutagenesis, Quantitative RT-PCR, Incubation, Derivative Assay

    Secreted SLPI and elafin are degraded by P. gingivalis supernatants. GECs were treated for 24 h (A and B) or for the time indicated (C) with various bacterial supernatants and the media analyzed by ELISA. (A) Secreted level of SLPI and elafin compared for various bacteria. GECs were stimulated with P. gingivalis (Pg), P. gingivalis mutant KDP112 (Pg−/−), T. forsythia (Tf) A. actinomycetemcomitans (Aa), and F. nucleatum (Fn) at MOIs of 100 or equivalent. (B) Secreted SLPI and elafin in media from GECs treated with graded doses of P. gingivalis supernatants and whole P. gingivalis . (C and D) Time course for the secreted levels of SLPI (C) and elafin (D) in GEC media in response to P. gingivalis supernatant stimulation (dark bar) and the unstimulated control (grey bar). The secreted level in response to P. gingivalis supernatant is shown with an expanded scale (insets). The results were expressed as means±SD (standard deviation) of values from three independent experiments. (*) indicates significant difference ( p
    Figure Legend Snippet: Secreted SLPI and elafin are degraded by P. gingivalis supernatants. GECs were treated for 24 h (A and B) or for the time indicated (C) with various bacterial supernatants and the media analyzed by ELISA. (A) Secreted level of SLPI and elafin compared for various bacteria. GECs were stimulated with P. gingivalis (Pg), P. gingivalis mutant KDP112 (Pg−/−), T. forsythia (Tf) A. actinomycetemcomitans (Aa), and F. nucleatum (Fn) at MOIs of 100 or equivalent. (B) Secreted SLPI and elafin in media from GECs treated with graded doses of P. gingivalis supernatants and whole P. gingivalis . (C and D) Time course for the secreted levels of SLPI (C) and elafin (D) in GEC media in response to P. gingivalis supernatant stimulation (dark bar) and the unstimulated control (grey bar). The secreted level in response to P. gingivalis supernatant is shown with an expanded scale (insets). The results were expressed as means±SD (standard deviation) of values from three independent experiments. (*) indicates significant difference ( p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Mutagenesis, Standard Deviation

    18) Product Images from "Binding of Pro-Matrix Metalloproteinase 9 by Fusobacterium nucleatum subsp. nucleatum as a Mechanism To Promote the Invasion of a Reconstituted Basement Membrane "

    Article Title: Binding of Pro-Matrix Metalloproteinase 9 by Fusobacterium nucleatum subsp. nucleatum as a Mechanism To Promote the Invasion of a Reconstituted Basement Membrane

    Journal: Infection and Immunity

    doi: 10.1128/IAI.72.10.6160-6163.2004

    Penetration of a reconstituted basement membrane (Matrigel) by F. nucleatum subsp. nucleatum ATCC 25586 under various conditions. Columns: 1, bacteria coated with APMA-activated pro-MMP-9; 2, bacteria (1/10 the amount applied in column 1) coated with APMA-activated pro-MMP-9; 3, control uncoated bacteria; 4, bacteria coated with APMA-activated pro-MMP-9 plus 1 mM EDTA; 5, bacteria coated with APMA-activated pro-MMP-9 and treated at 60°C for 30 min. After an incubation of 2 (left panel), and 4 h (right panel), radioactivity in the buffer present in the lower well was determined and used to estimate the number of cells that migrated through Matrigel. The values are the means ± standard deviations of three independent assays. The asterisk indicates differences between cells coated with APMA-activated pro-MMP-9 and control uncoated cells at P
    Figure Legend Snippet: Penetration of a reconstituted basement membrane (Matrigel) by F. nucleatum subsp. nucleatum ATCC 25586 under various conditions. Columns: 1, bacteria coated with APMA-activated pro-MMP-9; 2, bacteria (1/10 the amount applied in column 1) coated with APMA-activated pro-MMP-9; 3, control uncoated bacteria; 4, bacteria coated with APMA-activated pro-MMP-9 plus 1 mM EDTA; 5, bacteria coated with APMA-activated pro-MMP-9 and treated at 60°C for 30 min. After an incubation of 2 (left panel), and 4 h (right panel), radioactivity in the buffer present in the lower well was determined and used to estimate the number of cells that migrated through Matrigel. The values are the means ± standard deviations of three independent assays. The asterisk indicates differences between cells coated with APMA-activated pro-MMP-9 and control uncoated cells at P

    Techniques Used: Incubation, Radioactivity

    Gelatinase activity of F. nucleatum subsp. nucleatum ATCC 25586 following various treatments. (A) Analysis by zymography on gelatin-containing polyacrylamide gel. (B) Analysis by a colorimetric assay using biotin-labeled gelatin and for which a high gelatinase activity yields a low signal determined by measuring the absorbance at 405 nm. Lanes and columns: 1, APMA-activated pro-MMP-9 control; 2, bacteria coated with pro-MMP-9 subsequently activated with APMA; 3, bacteria coated with pro-MMP-9 without activation; 4, control uncoated bacteria. The asterisk indicates a significant difference between cells coated with APMA-activated pro-MMP-9 and control uncoated cells at a P value of
    Figure Legend Snippet: Gelatinase activity of F. nucleatum subsp. nucleatum ATCC 25586 following various treatments. (A) Analysis by zymography on gelatin-containing polyacrylamide gel. (B) Analysis by a colorimetric assay using biotin-labeled gelatin and for which a high gelatinase activity yields a low signal determined by measuring the absorbance at 405 nm. Lanes and columns: 1, APMA-activated pro-MMP-9 control; 2, bacteria coated with pro-MMP-9 subsequently activated with APMA; 3, bacteria coated with pro-MMP-9 without activation; 4, control uncoated bacteria. The asterisk indicates a significant difference between cells coated with APMA-activated pro-MMP-9 and control uncoated cells at a P value of

    Techniques Used: Activity Assay, Zymography, Colorimetric Assay, Labeling, Activation Assay

    19) Product Images from "Insights into the Evolution of Host Association through the Isolation and Characterization of a Novel Human Periodontal Pathobiont, Desulfobulbus oralis"

    Article Title: Insights into the Evolution of Host Association through the Isolation and Characterization of a Novel Human Periodontal Pathobiont, Desulfobulbus oralis

    Journal: mBio

    doi: 10.1128/mBio.02061-17

    Desulfobulbus sp. strain HOT041 ( D. oralis ) in coculture with Fusobacterium nucleatum and in pure culture. (A) FISH using fluorescent oligonucleotide probes specific for Deltaproteobacteria (green) and universal Bacteria (red). (B). Growth of Desulfobulbus sp. strain HOT041 and F. nucleatum in coculture monitored by species-specific qPCR (with error bars based on three replicates). (C and D) Scanning electron micrographs of the D. oralis isolate. The arrowheads point to membrane vesicles.
    Figure Legend Snippet: Desulfobulbus sp. strain HOT041 ( D. oralis ) in coculture with Fusobacterium nucleatum and in pure culture. (A) FISH using fluorescent oligonucleotide probes specific for Deltaproteobacteria (green) and universal Bacteria (red). (B). Growth of Desulfobulbus sp. strain HOT041 and F. nucleatum in coculture monitored by species-specific qPCR (with error bars based on three replicates). (C and D) Scanning electron micrographs of the D. oralis isolate. The arrowheads point to membrane vesicles.

    Techniques Used: Fluorescence In Situ Hybridization, Real-time Polymerase Chain Reaction

    20) Product Images from "Conceptual Perspectives: Bacterial Antimicrobial Peptide Induction as a Novel Strategy for Symbiosis with the Human Host"

    Article Title: Conceptual Perspectives: Bacterial Antimicrobial Peptide Induction as a Novel Strategy for Symbiosis with the Human Host

    Journal: Frontiers in Microbiology

    doi: 10.3389/fmicb.2018.00302

    (A) F. nucleatum stimulation of normal human oral epithelial cells (HOECs) confers protection against P. gingivalis invasion. Semi-confluent (80%) monolayers of HOECs were either unchallenged or challenged with F. nucleatum cell wall fraction (FnCW) (10 μg/ml) for approximately 18 hrs. P. gingivalis was then added at a multiplicity of infection (MOI) of 10:1 or 100:1, 90 min, 37°C, 5% CO 2 . After 1 h incubation with gentamycin and metronidazole, cells were harvested and subjected to flow cytometric analysis. Results revealed a 54.3 and 67.2% reduction in P. gingivalis invasion for the 100:1 and 10:1 MOI's respectively, when compared to non F. nucleatum challenged HOECs. (B–D) Immunogold transmission electron microscopy (TEM) of F. nucleatum and P. gingivalis incubated with rhBD-2. Overnight cultures of F. nucleatum (ATCC strain 25586) and P. gingivalis (ATCC strain 33277) (1.6 × 10 9 cells/ml) were incubated with recombinant hBD-2 (rhBD-2) (10 μg/ml), 3 h, 37°C anaerobically, and embedded in 1.5% low gel temperature agarose (Bio-Rad), respectively. Samples were fixed, 10 min at room temperature with 1% formaldehyde and 0.1% glutaraldehyde in 1x HEPES-buffered saline (pH 7.4), followed by washing 3X with 1X phosphate buffered saline (PBS) containing 0.05M glycine to block glutaraldehyde groups remaining on the cell surface. Samples were blocked in PBS with 1% BSA (bovine serum albumin; PBS-BSA), followed by incubation with goat anti-hBD-2 antibody (Cell Sciences, Canton, MA) (1:100) in PBS-BSA, 2 h, room temperature. After washing, samples were incubated, 2 h, in 5 nm gold-conjugated rabbit anti-goat IgG (BB International) (1:30) in PBS-BSA. To stabilize the gold particles, the samples were fixed with glutaraldehyde and post-fixed in 1% osmium tetroxide for 1 h. Samples were then block-stained in 0.5% of aqueous uranyl acetate, dehydrated in ascending concentrations of ethanol and embedded in Epon 812. Ultrathin sections were then stained with 2% uranyl acetate in 50% methanol and lead citrate, and examined in an electron microscope (Model Zeiss CEM902, Oberkochen, Germany). Black arrow points to F. nucleatum amorphous-like structures emanating from the organism's outer membrane to which immunogold labeled rhBD-2 (green circles) is sequestered, keeping it from interacting with the bacterium's outer membrane (red arrows) (C) . Yellow arrow points to intact F. nucleatum cytoplasmic membrane. Extensive P. gingivalis cellular debris of outer (red arrow) and cytoplasmic membrane (yellow arrow) with rhBD-2 sequestered to these structures (green circles) are also shown (D) . (E) Semi-confluent HOECs were treated with 10 μg/ml of either FnCW or recombinant FAD-I (rFAD-I) for 18 h. Levels of IL-8 and TNF-α in the supernatants were measured by ELISA (R D systems, MN, US). Fold change in IL-8 and TNF- α released by each of the treatment compared to untreated cells were calculated.
    Figure Legend Snippet: (A) F. nucleatum stimulation of normal human oral epithelial cells (HOECs) confers protection against P. gingivalis invasion. Semi-confluent (80%) monolayers of HOECs were either unchallenged or challenged with F. nucleatum cell wall fraction (FnCW) (10 μg/ml) for approximately 18 hrs. P. gingivalis was then added at a multiplicity of infection (MOI) of 10:1 or 100:1, 90 min, 37°C, 5% CO 2 . After 1 h incubation with gentamycin and metronidazole, cells were harvested and subjected to flow cytometric analysis. Results revealed a 54.3 and 67.2% reduction in P. gingivalis invasion for the 100:1 and 10:1 MOI's respectively, when compared to non F. nucleatum challenged HOECs. (B–D) Immunogold transmission electron microscopy (TEM) of F. nucleatum and P. gingivalis incubated with rhBD-2. Overnight cultures of F. nucleatum (ATCC strain 25586) and P. gingivalis (ATCC strain 33277) (1.6 × 10 9 cells/ml) were incubated with recombinant hBD-2 (rhBD-2) (10 μg/ml), 3 h, 37°C anaerobically, and embedded in 1.5% low gel temperature agarose (Bio-Rad), respectively. Samples were fixed, 10 min at room temperature with 1% formaldehyde and 0.1% glutaraldehyde in 1x HEPES-buffered saline (pH 7.4), followed by washing 3X with 1X phosphate buffered saline (PBS) containing 0.05M glycine to block glutaraldehyde groups remaining on the cell surface. Samples were blocked in PBS with 1% BSA (bovine serum albumin; PBS-BSA), followed by incubation with goat anti-hBD-2 antibody (Cell Sciences, Canton, MA) (1:100) in PBS-BSA, 2 h, room temperature. After washing, samples were incubated, 2 h, in 5 nm gold-conjugated rabbit anti-goat IgG (BB International) (1:30) in PBS-BSA. To stabilize the gold particles, the samples were fixed with glutaraldehyde and post-fixed in 1% osmium tetroxide for 1 h. Samples were then block-stained in 0.5% of aqueous uranyl acetate, dehydrated in ascending concentrations of ethanol and embedded in Epon 812. Ultrathin sections were then stained with 2% uranyl acetate in 50% methanol and lead citrate, and examined in an electron microscope (Model Zeiss CEM902, Oberkochen, Germany). Black arrow points to F. nucleatum amorphous-like structures emanating from the organism's outer membrane to which immunogold labeled rhBD-2 (green circles) is sequestered, keeping it from interacting with the bacterium's outer membrane (red arrows) (C) . Yellow arrow points to intact F. nucleatum cytoplasmic membrane. Extensive P. gingivalis cellular debris of outer (red arrow) and cytoplasmic membrane (yellow arrow) with rhBD-2 sequestered to these structures (green circles) are also shown (D) . (E) Semi-confluent HOECs were treated with 10 μg/ml of either FnCW or recombinant FAD-I (rFAD-I) for 18 h. Levels of IL-8 and TNF-α in the supernatants were measured by ELISA (R D systems, MN, US). Fold change in IL-8 and TNF- α released by each of the treatment compared to untreated cells were calculated.

    Techniques Used: Infection, Incubation, Flow Cytometry, Transmission Assay, Electron Microscopy, Transmission Electron Microscopy, Recombinant, Blocking Assay, Staining, Microscopy, Labeling, Enzyme-linked Immunosorbent Assay

    (A–D) Representative F. nucleatum (A,C) and P. gingivalis (B,D) susceptibility to hBD-2 (A,B) and−3 (C,D) , 2 × 10 5 bacteria were incubated with recombinant hBD-2 and 3 (indicated micro-molar concentrations) anaerobically, for 3 h, followed by serial dilutions and plating on sheep red blood agar plates.
    Figure Legend Snippet: (A–D) Representative F. nucleatum (A,C) and P. gingivalis (B,D) susceptibility to hBD-2 (A,B) and−3 (C,D) , 2 × 10 5 bacteria were incubated with recombinant hBD-2 and 3 (indicated micro-molar concentrations) anaerobically, for 3 h, followed by serial dilutions and plating on sheep red blood agar plates.

    Techniques Used: Incubation, Recombinant

    21) Product Images from "Regulation of somatostatin receptor 2 by proinflammatory, microbial and obesity-related signals in periodontal cells and tissues"

    Article Title: Regulation of somatostatin receptor 2 by proinflammatory, microbial and obesity-related signals in periodontal cells and tissues

    Journal: Head & Face Medicine

    doi: 10.1186/s13005-018-0185-1

    Effects of IL-1β (1 ng/ml), F. nucleatum (OD: 0.025), leptin (3 ng/ml) or visfatin (100 ng/ml) on SSTR2 protein levels in PDL fibroblasts at 1 d, as analyzed by immunocytochemistry. Untreated cells served as control. Experiments were performed in triplicates and representative images of cells from one donor are shown
    Figure Legend Snippet: Effects of IL-1β (1 ng/ml), F. nucleatum (OD: 0.025), leptin (3 ng/ml) or visfatin (100 ng/ml) on SSTR2 protein levels in PDL fibroblasts at 1 d, as analyzed by immunocytochemistry. Untreated cells served as control. Experiments were performed in triplicates and representative images of cells from one donor are shown

    Techniques Used: Immunocytochemistry

    ( a ) SSTR2 expression in the presence or absence of IL-1β (1 ng/ml) or F. nucleatum (OD: 0.025) at 1 d. Untreated cells served as control. Mean ± SEM ( n = 6), * significantly ( p
    Figure Legend Snippet: ( a ) SSTR2 expression in the presence or absence of IL-1β (1 ng/ml) or F. nucleatum (OD: 0.025) at 1 d. Untreated cells served as control. Mean ± SEM ( n = 6), * significantly ( p

    Techniques Used: Expressing

    22) Product Images from "Coaggregation of Candida dubliniensis with Fusobacterium nucleatum"

    Article Title: Coaggregation of Candida dubliniensis with Fusobacterium nucleatum

    Journal: Journal of Clinical Microbiology

    doi:

    Visual CoAg testing of C. albicans or C. dubliniensis with F. nucleatum . For each pair of tubes, the left tube contains C. albicans grown at 37°C plus F. nucleatum , and the right tube contains C. dubliniensis grown at 37°C plus F. nucleatum . The tubes are shown 45 s (A) or 5 min (B) after mixing (CoAg score of 4+).
    Figure Legend Snippet: Visual CoAg testing of C. albicans or C. dubliniensis with F. nucleatum . For each pair of tubes, the left tube contains C. albicans grown at 37°C plus F. nucleatum , and the right tube contains C. dubliniensis grown at 37°C plus F. nucleatum . The tubes are shown 45 s (A) or 5 min (B) after mixing (CoAg score of 4+).

    Techniques Used:

    23) Product Images from "The Protective Effect of Recombinant FomA-expressing Lactobacillus acidophilus Against Periodontal Infection"

    Article Title: The Protective Effect of Recombinant FomA-expressing Lactobacillus acidophilus Against Periodontal Infection

    Journal: Inflammation

    doi: 10.1007/s10753-013-9651-x

    Results of adhesion assays. After P. gingivalis and F. nucleatum were co-cultured with KB cells for 1, 2, or 4 h, the number of P. gingivalis cells adhered to the KB cells, mediated by F. nucleatum , was assessed. The level of P. gingivalis in the experimental group was lower than in the control group at all three time points ( p
    Figure Legend Snippet: Results of adhesion assays. After P. gingivalis and F. nucleatum were co-cultured with KB cells for 1, 2, or 4 h, the number of P. gingivalis cells adhered to the KB cells, mediated by F. nucleatum , was assessed. The level of P. gingivalis in the experimental group was lower than in the control group at all three time points ( p

    Techniques Used: Cell Culture

    Levels of IL-1β in oral mucosal tissues of mice. After 3 days of injection, the mandibular and tongue mucosal tissues of the mice were collected, and 100 mg/ml PBS buffer was added. After homogenisation, the supernatant was collected by centrifugation at 20,000× g at 4 °C for 20 min. The IL-1β levels in the serum and oral mucosal tissues were determined using ELISA kits (Thermo Scientific, USA). The IL-1β levels in the experimental group of mice were lower than in the control group following injections with both F. nucleatum alone and with F. nucleatum plus P. gingivalis (*, # p
    Figure Legend Snippet: Levels of IL-1β in oral mucosal tissues of mice. After 3 days of injection, the mandibular and tongue mucosal tissues of the mice were collected, and 100 mg/ml PBS buffer was added. After homogenisation, the supernatant was collected by centrifugation at 20,000× g at 4 °C for 20 min. The IL-1β levels in the serum and oral mucosal tissues were determined using ELISA kits (Thermo Scientific, USA). The IL-1β levels in the experimental group of mice were lower than in the control group following injections with both F. nucleatum alone and with F. nucleatum plus P. gingivalis (*, # p

    Techniques Used: Mouse Assay, Injection, Homogenization, Centrifugation, Enzyme-linked Immunosorbent Assay

    Morphologies of swollen gums in mice treated with P. gingivalis plus F. nucleatum . After 3 days of injection, the gums surrounding the lower incisors were red and swollen, and abscesses had formed. The gingival abscesses in the mice in the experimental group were less severe than in the control and blank groups. a The mice immunised with PBS served as the blank group. b The mice immunised with the recombinant strain La-pMG36e served as the control. c The mice immunised with the recombinant strain La-fomA.
    Figure Legend Snippet: Morphologies of swollen gums in mice treated with P. gingivalis plus F. nucleatum . After 3 days of injection, the gums surrounding the lower incisors were red and swollen, and abscesses had formed. The gingival abscesses in the mice in the experimental group were less severe than in the control and blank groups. a The mice immunised with PBS served as the blank group. b The mice immunised with the recombinant strain La-pMG36e served as the control. c The mice immunised with the recombinant strain La-fomA.

    Techniques Used: Mouse Assay, Injection, Recombinant

    Levels of IL-1β in mouse serum samples. After 3 days of injection, blood was collected from the heart, and the serum was isolated. The levels of IL-1β in the mouse serum were determined using ELISA kits in accordance with the manufacturer's instructions (Thermo Scientific, USA). Following injection with both F. nucleatum alone and F. nucleatum plus P. gingivalis , the mean IL-1β levels in the experimental group of mice were lower than in the control group (*, # p
    Figure Legend Snippet: Levels of IL-1β in mouse serum samples. After 3 days of injection, blood was collected from the heart, and the serum was isolated. The levels of IL-1β in the mouse serum were determined using ELISA kits in accordance with the manufacturer's instructions (Thermo Scientific, USA). Following injection with both F. nucleatum alone and F. nucleatum plus P. gingivalis , the mean IL-1β levels in the experimental group of mice were lower than in the control group (*, # p

    Techniques Used: Injection, Isolation, Enzyme-linked Immunosorbent Assay, Mouse Assay

    24) Product Images from "Induction of Apoptotic Cell Death in Peripheral Blood Mononuclear and Polymorphonuclear Cells by an Oral Bacterium, Fusobacterium nucleatum"

    Article Title: Induction of Apoptotic Cell Death in Peripheral Blood Mononuclear and Polymorphonuclear Cells by an Oral Bacterium, Fusobacterium nucleatum

    Journal: Infection and Immunity

    doi:

    Dose-dependent induction of apoptotic cell death of PBMCs by F. nucleatum . PBMCs were cocultured in the presence of F. nucleatum at the indicated ratios. The levels of apoptotic cell death were determined by using flow cytometric analysis of propidium iodide-stained cells.
    Figure Legend Snippet: Dose-dependent induction of apoptotic cell death of PBMCs by F. nucleatum . PBMCs were cocultured in the presence of F. nucleatum at the indicated ratios. The levels of apoptotic cell death were determined by using flow cytometric analysis of propidium iodide-stained cells.

    Techniques Used: Flow Cytometry, Staining

    Induction of cell death in peripheral blood PMNs by F. nucleatum . PMNs at a concentration of 2 × 10 6 per ml were cocultured in the presence of F. nucleatum for 16 h. The numbers of viable cells were counted by trypan blue staining.
    Figure Legend Snippet: Induction of cell death in peripheral blood PMNs by F. nucleatum . PMNs at a concentration of 2 × 10 6 per ml were cocultured in the presence of F. nucleatum for 16 h. The numbers of viable cells were counted by trypan blue staining.

    Techniques Used: Concentration Assay, Staining

    25) Product Images from "Epigenetic regulation of human ?-defensin 2 and CC chemokine ligand 20 expression in gingival epithelial cells in response to oral bacteria"

    Article Title: Epigenetic regulation of human ?-defensin 2 and CC chemokine ligand 20 expression in gingival epithelial cells in response to oral bacteria

    Journal: Mucosal Immunology

    doi: 10.1038/mi.2010.83

    mRNA expression of innate immune markers human β-defensin 2 (hBD-2) are increased when histone deacetylase (HDAC) and DNA methyltransferase (DNMT) are inhibited. Gingival epithelial cells (GECs) were pretreated with trichostatin A (TSA; 9 and 45 m), sodium butyrate (SB; 0.5 and 2.0 m) or 5′-azacytidine (AZA; 1 and 10 μ) for 4 h, and subsequently exposed to Porphyromonas gingivalis (multiplicity of infection (MOI) 100:1) or Fusobacterium nucleatum (MOI 100:1) for 16 h. Gene expression of hBD2 was evaluated by quantitative real-time PCR (QRT-PCR) compared with unstimulated control after normalization with glyceraldehydes-3-phosphate dehydrogenase (GAPDH). Controls include unstimulated control, bacteria-alone treatment, and various inhibitors alone as indicated. No significant changes were found in the gene expression of hBD2 in GECs treated with inhibitor only: ( a ) SB, ( b ) TSA, ( c ) SB+TSA, and ( d ) AZA compared with unstimulated control. Data are expressed as means of fold change±s.e.m. from three donors evaluated in duplicate. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P
    Figure Legend Snippet: mRNA expression of innate immune markers human β-defensin 2 (hBD-2) are increased when histone deacetylase (HDAC) and DNA methyltransferase (DNMT) are inhibited. Gingival epithelial cells (GECs) were pretreated with trichostatin A (TSA; 9 and 45 m), sodium butyrate (SB; 0.5 and 2.0 m) or 5′-azacytidine (AZA; 1 and 10 μ) for 4 h, and subsequently exposed to Porphyromonas gingivalis (multiplicity of infection (MOI) 100:1) or Fusobacterium nucleatum (MOI 100:1) for 16 h. Gene expression of hBD2 was evaluated by quantitative real-time PCR (QRT-PCR) compared with unstimulated control after normalization with glyceraldehydes-3-phosphate dehydrogenase (GAPDH). Controls include unstimulated control, bacteria-alone treatment, and various inhibitors alone as indicated. No significant changes were found in the gene expression of hBD2 in GECs treated with inhibitor only: ( a ) SB, ( b ) TSA, ( c ) SB+TSA, and ( d ) AZA compared with unstimulated control. Data are expressed as means of fold change±s.e.m. from three donors evaluated in duplicate. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P

    Techniques Used: Expressing, Histone Deacetylase Assay, Infection, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, CTL Assay

    mRNA expression of innate immune markers CC chemokine ligand 20 (CCL20) are increased when histone deacetylase (HDAC) and DNA methyltransferase (DNMT) are inhibited. Gingival epithelial cells (GECs) were pretreated with trichostatin A (TSA; 9 and 45 m), sodium butyrate (SB; 0.5 and 2.0 m), or 5′-azacytidine (AZA; 1 and 10 μ) for 4 h, and subsequently exposed to Porphyromonas gingivalis (multiplicity of infection (MOI) 100:1) or Fusobacterium nucleatum (MOI 100:1) for 16 h. Gene expression of ( b ) CCL20 was evaluated by quantitative real-time PCR (QRT-PCR) compared with unstimulated control after normalization with glyceraldehydes-3-phosphate dehydrogenase (GAPDH). Controls include unstimulated control, bacteria-alone treatment, and various inhibitors alone as indicated. No significant changes were found in the gene expression of CCL20 in GECs treated with inhibitor only: ( a ) SB, ( b ) TSA, ( c ) SB+TSA, and ( d ) AZA compared with unstimulated control. Data are expressed as means of fold change±s.e.m. from three donors evaluated in duplicate. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P
    Figure Legend Snippet: mRNA expression of innate immune markers CC chemokine ligand 20 (CCL20) are increased when histone deacetylase (HDAC) and DNA methyltransferase (DNMT) are inhibited. Gingival epithelial cells (GECs) were pretreated with trichostatin A (TSA; 9 and 45 m), sodium butyrate (SB; 0.5 and 2.0 m), or 5′-azacytidine (AZA; 1 and 10 μ) for 4 h, and subsequently exposed to Porphyromonas gingivalis (multiplicity of infection (MOI) 100:1) or Fusobacterium nucleatum (MOI 100:1) for 16 h. Gene expression of ( b ) CCL20 was evaluated by quantitative real-time PCR (QRT-PCR) compared with unstimulated control after normalization with glyceraldehydes-3-phosphate dehydrogenase (GAPDH). Controls include unstimulated control, bacteria-alone treatment, and various inhibitors alone as indicated. No significant changes were found in the gene expression of CCL20 in GECs treated with inhibitor only: ( a ) SB, ( b ) TSA, ( c ) SB+TSA, and ( d ) AZA compared with unstimulated control. Data are expressed as means of fold change±s.e.m. from three donors evaluated in duplicate. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P

    Techniques Used: Expressing, Histone Deacetylase Assay, Infection, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, CTL Assay

    Differential decreased mRNA expression of HDAC1, HDAC2 and DNMT1 in gingival epithelial cells in response to various doses of oral bacteria. mRNA expression of ( a ) DNA methyltransferase (DNMT1), ( b ) histone deacetylase 1 (HDAC1), and ( c ) histone deacetylase 2 (HDAC2) are differentially decreased in gingival epithelial cells (GECs) in response to various doses of Porphyromonas gingivalis vs. Fusobacterium nucleatum . GECs were stimulated with P. gingivalis (Pg) or F. nucleatum (Fn) at multiplicities of infection (MOIs) of 10:1, 50:1, 100:1, and 200:1 for 24 h. Changes in mRNA expression were evaluated by quantitative real-time PCR (QRT-PCR) and results are expressed as fold change in gene expression compared with the unstimulated control after normalization with the housekeeping gene glyceraldehydes-3-phosphate dehydrogenase ( GAPDH ). The data are derived from three different cell donors tested in duplicate. Error bars indicate s.e.m. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P
    Figure Legend Snippet: Differential decreased mRNA expression of HDAC1, HDAC2 and DNMT1 in gingival epithelial cells in response to various doses of oral bacteria. mRNA expression of ( a ) DNA methyltransferase (DNMT1), ( b ) histone deacetylase 1 (HDAC1), and ( c ) histone deacetylase 2 (HDAC2) are differentially decreased in gingival epithelial cells (GECs) in response to various doses of Porphyromonas gingivalis vs. Fusobacterium nucleatum . GECs were stimulated with P. gingivalis (Pg) or F. nucleatum (Fn) at multiplicities of infection (MOIs) of 10:1, 50:1, 100:1, and 200:1 for 24 h. Changes in mRNA expression were evaluated by quantitative real-time PCR (QRT-PCR) and results are expressed as fold change in gene expression compared with the unstimulated control after normalization with the housekeeping gene glyceraldehydes-3-phosphate dehydrogenase ( GAPDH ). The data are derived from three different cell donors tested in duplicate. Error bars indicate s.e.m. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P

    Techniques Used: Expressing, Histone Deacetylase Assay, Infection, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Derivative Assay, CTL Assay

    Protein levels of histone H3 methylated at Lys4 were evaluated with PathScan enzyme-linked immunosorbent assay (ELISA). Gingival epithelial cells (GECs) were exposed to Porphyromonas gingivalis or Fusobacterium nucleatum for 24 h at multiplicity of infection (MOI) of 100:1, and then nuclear protein was extracted followed by sonication. The H3 tri-methylated at Lys4 was captured by coated antibody after incubation with cell lysates, and histone H3 protein level was quantified according to the absorbance readings at 450 nm. Protein expression was expressed as the ratio of absorbance readings normalized to relative protein amount. The data are average from three different donor cells tested with standard error deviation. The asterisks indicate the significant difference vs. the respective unstimulated control (** P
    Figure Legend Snippet: Protein levels of histone H3 methylated at Lys4 were evaluated with PathScan enzyme-linked immunosorbent assay (ELISA). Gingival epithelial cells (GECs) were exposed to Porphyromonas gingivalis or Fusobacterium nucleatum for 24 h at multiplicity of infection (MOI) of 100:1, and then nuclear protein was extracted followed by sonication. The H3 tri-methylated at Lys4 was captured by coated antibody after incubation with cell lysates, and histone H3 protein level was quantified according to the absorbance readings at 450 nm. Protein expression was expressed as the ratio of absorbance readings normalized to relative protein amount. The data are average from three different donor cells tested with standard error deviation. The asterisks indicate the significant difference vs. the respective unstimulated control (** P

    Techniques Used: Methylation, Enzyme-linked Immunosorbent Assay, Infection, Sonication, Incubation, Expressing

    Protein levels of histone deacetylases 1 and 2 (HDAC1 and HDAC2) and DNA methyltransferase (DNMT1) are differentially expressed in gingival epithelial cells (GECs) in response to Porphyromonas gingivalis (Pg) and Fusobacterium nucleatum (Fn). GECs were stimulated with P. gingivalis (Pg) or F. nucleatum (Fn) at multiplicities of infection (MOIs) of 100:1 for 24 h. Nuclear proteins were extracted, denatured at 70 °C for 10 min, and separated by NuPAGE electrophoresis system. Nuclear extracts of Hela cells probed with individual primary antibody were used as positive controls. The data are derived from two different cell donors tested in duplicate.
    Figure Legend Snippet: Protein levels of histone deacetylases 1 and 2 (HDAC1 and HDAC2) and DNA methyltransferase (DNMT1) are differentially expressed in gingival epithelial cells (GECs) in response to Porphyromonas gingivalis (Pg) and Fusobacterium nucleatum (Fn). GECs were stimulated with P. gingivalis (Pg) or F. nucleatum (Fn) at multiplicities of infection (MOIs) of 100:1 for 24 h. Nuclear proteins were extracted, denatured at 70 °C for 10 min, and separated by NuPAGE electrophoresis system. Nuclear extracts of Hela cells probed with individual primary antibody were used as positive controls. The data are derived from two different cell donors tested in duplicate.

    Techniques Used: Infection, Electrophoresis, Derivative Assay

    Differential mRNA expression of HDAC1, HDAC2 and DNMT1 in human TERT cells in response to oral bacteria. Differential mRNA expression of ( a ) histone deacetylases 1 and 2 (HDAC1 and HDAC2) and ( b ) DNA methyltransferase (DNMT1) in human TERT cells in response to Porphyromonas gingivalis vs. Fusobacterium nucleatum . Human TERT cells were stimulated with P. gingivalis (Pg) or F. nucleatum (Fn) at multiplicities of infection (MOIs) of 10:1, 50:1, and 100:1 for 4 or 24 h. Unstimulated cells at 4 and 24 h served as controls. Changes in mRNA expression were evaluated by quantitative real-time PCR (QRT-PCR) and results are expressed as fold change in gene expression compared with the corresponding unstimulated controls (4 and 24 h) after normalization with glyceraldehydes-3-phosphate dehydrogenase (GAPDH). The experiment was repeated twice using TERT cells. Error bars indicate s.e.m. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P
    Figure Legend Snippet: Differential mRNA expression of HDAC1, HDAC2 and DNMT1 in human TERT cells in response to oral bacteria. Differential mRNA expression of ( a ) histone deacetylases 1 and 2 (HDAC1 and HDAC2) and ( b ) DNA methyltransferase (DNMT1) in human TERT cells in response to Porphyromonas gingivalis vs. Fusobacterium nucleatum . Human TERT cells were stimulated with P. gingivalis (Pg) or F. nucleatum (Fn) at multiplicities of infection (MOIs) of 10:1, 50:1, and 100:1 for 4 or 24 h. Unstimulated cells at 4 and 24 h served as controls. Changes in mRNA expression were evaluated by quantitative real-time PCR (QRT-PCR) and results are expressed as fold change in gene expression compared with the corresponding unstimulated controls (4 and 24 h) after normalization with glyceraldehydes-3-phosphate dehydrogenase (GAPDH). The experiment was repeated twice using TERT cells. Error bars indicate s.e.m. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P

    Techniques Used: Expressing, Infection, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, CTL Assay

    Interleukin-8 (IL-8) secretion is increased when histone deacetylase (HDAC) and DNA methyltransferase (DNMT) are inhibited. Gingival epithelial cells (GECs) were pretreated with trichostatin A (TSA; 9 and 45 m), sodium butyrate (SB; 0.5 and 2.0 m), or 5′-azacytidine (AZA; 1 and 10 μ) for 4 h, and subsequently exposed to Porphyromonas gingivalis (multiplicity of infection (MOI) 100:1) or Fusobacterium nucleatum (MOI 100:1) for 16 h. Secretion of IL-8 in response to various oral bacteria is evaluated by enzyme-linked immunosorbent assay (ELISA). Cell-free supernatant was collected and the amount of IL-8 secreted is shown in pg ml –1 . Unstimulated cells (UN) are used as controls in each experiment. Data from duplicates with cells from three different donors are shown. No significant changes were found in the secretion of IL-8 in GECs treated with inhibitor only: ( a ) SB, ( b ) TSA, ( c ) SB+TSA, and ( d ) AZA compared with unstimulated control. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P
    Figure Legend Snippet: Interleukin-8 (IL-8) secretion is increased when histone deacetylase (HDAC) and DNA methyltransferase (DNMT) are inhibited. Gingival epithelial cells (GECs) were pretreated with trichostatin A (TSA; 9 and 45 m), sodium butyrate (SB; 0.5 and 2.0 m), or 5′-azacytidine (AZA; 1 and 10 μ) for 4 h, and subsequently exposed to Porphyromonas gingivalis (multiplicity of infection (MOI) 100:1) or Fusobacterium nucleatum (MOI 100:1) for 16 h. Secretion of IL-8 in response to various oral bacteria is evaluated by enzyme-linked immunosorbent assay (ELISA). Cell-free supernatant was collected and the amount of IL-8 secreted is shown in pg ml –1 . Unstimulated cells (UN) are used as controls in each experiment. Data from duplicates with cells from three different donors are shown. No significant changes were found in the secretion of IL-8 in GECs treated with inhibitor only: ( a ) SB, ( b ) TSA, ( c ) SB+TSA, and ( d ) AZA compared with unstimulated control. Asterisks indicate statistically significant difference compared with unstimulated control (Ctl) (* P

    Techniques Used: Histone Deacetylase Assay, Infection, Enzyme-linked Immunosorbent Assay, CTL Assay

    26) Product Images from "Synergic phototoxic effect of visible light or Gallium-Arsenide laser in the presence of different photo-sensitizers on Porphyromonas gingivalis and Fusobacterium nucleatum"

    Article Title: Synergic phototoxic effect of visible light or Gallium-Arsenide laser in the presence of different photo-sensitizers on Porphyromonas gingivalis and Fusobacterium nucleatum

    Journal: Dental Research Journal

    doi: 10.4103/1735-3327.161432

    The synergic effect of each photosensitizers with visible light or laser on Porphyromonas gingivals survival rate (a and b) and Fusobacterium nucleatum survival rate (c and d).
    Figure Legend Snippet: The synergic effect of each photosensitizers with visible light or laser on Porphyromonas gingivals survival rate (a and b) and Fusobacterium nucleatum survival rate (c and d).

    Techniques Used:

    Distribution of Fusobacterium nucleatum after various time and treatments.
    Figure Legend Snippet: Distribution of Fusobacterium nucleatum after various time and treatments.

    Techniques Used:

    The effect of photosensitizers in the absence of light exposure for Porphyromonas gingivalis (a) and Fusobacterium nucleatum (b).
    Figure Legend Snippet: The effect of photosensitizers in the absence of light exposure for Porphyromonas gingivalis (a) and Fusobacterium nucleatum (b).

    Techniques Used:

    Synergic phototoxic effects of laser and visible light in the presence of each photosensitizers (a-c) on Fusobacterium nucleatum.
    Figure Legend Snippet: Synergic phototoxic effects of laser and visible light in the presence of each photosensitizers (a-c) on Fusobacterium nucleatum.

    Techniques Used:

    The effect of laser and visible light on Fusobacterium nucleatum (a) and Porphyromonas gingivalis (b) in the absence of photosensitizers.
    Figure Legend Snippet: The effect of laser and visible light on Fusobacterium nucleatum (a) and Porphyromonas gingivalis (b) in the absence of photosensitizers.

    Techniques Used:

    27) Product Images from "A novel vaccine targeting Fusobacterium nucleatum against abscesses and halitosis"

    Article Title: A novel vaccine targeting Fusobacterium nucleatum against abscesses and halitosis

    Journal: Vaccine

    doi: 10.1016/j.vaccine.2008.12.058

    The production of antibody (IgG) to F. nucleatum. For immunization, cultured F. nucleatum and S. mutans were irradiated by UV at a total energy of 7000 J/m 2 . F. nucleatum lysate (20 µg) was separated by 10% SDS-PAGE and then subjected to Western
    Figure Legend Snippet: The production of antibody (IgG) to F. nucleatum. For immunization, cultured F. nucleatum and S. mutans were irradiated by UV at a total energy of 7000 J/m 2 . F. nucleatum lysate (20 µg) was separated by 10% SDS-PAGE and then subjected to Western

    Techniques Used: Cell Culture, Irradiation, SDS Page, Western Blot

    An abscess induced by the injection of live F. nucleatum into the gums of lower incisors of ICR mice. One hundred micro liter of PBS (A, C and E) or F. nucleatum (4 × 10 8 CFU in PBS) (B, D and F) was inoculated into a mouse oral cavity for 3 days,
    Figure Legend Snippet: An abscess induced by the injection of live F. nucleatum into the gums of lower incisors of ICR mice. One hundred micro liter of PBS (A, C and E) or F. nucleatum (4 × 10 8 CFU in PBS) (B, D and F) was inoculated into a mouse oral cavity for 3 days,

    Techniques Used: Injection, Mouse Assay

    Detection of VSC production and biofilm formation of F. nucleatum . F. nucleatum (4 × 10 9 CFU/well) was cultured on a 6-well nonpyrogenic polystyrene plate for 6, 12, 24 and 36 h. (A) After removing the media, each well containing attached bacteria
    Figure Legend Snippet: Detection of VSC production and biofilm formation of F. nucleatum . F. nucleatum (4 × 10 9 CFU/well) was cultured on a 6-well nonpyrogenic polystyrene plate for 6, 12, 24 and 36 h. (A) After removing the media, each well containing attached bacteria

    Techniques Used: Cell Culture

    In vivo protective immunity. A gum pocket model with abscesses and swollen tissues was created, as described in and Section 2. After inoculation with live F. nucleatum (4 × 10 8 CFU) for 3 days, the change in the volume of gum swelling
    Figure Legend Snippet: In vivo protective immunity. A gum pocket model with abscesses and swollen tissues was created, as described in and Section 2. After inoculation with live F. nucleatum (4 × 10 8 CFU) for 3 days, the change in the volume of gum swelling

    Techniques Used: In Vivo

    Inhibition of VSC production and biofilm formation by anti- F. nucleatum serum. F. nucleatum (4 × 10 9 CFU) was pre-incubated with 2.5% (v/v) anti- F. nucleatum (Anti-N) or anti- S. mutans (Anti-M) sera without activated complements for 2 h. Afterwards,
    Figure Legend Snippet: Inhibition of VSC production and biofilm formation by anti- F. nucleatum serum. F. nucleatum (4 × 10 9 CFU) was pre-incubated with 2.5% (v/v) anti- F. nucleatum (Anti-N) or anti- S. mutans (Anti-M) sera without activated complements for 2 h. Afterwards,

    Techniques Used: Inhibition, Incubation

    28) Product Images from "Co-Localized or Randomly Distributed? Pair Cross Correlation of In Vivo Grown Subgingival Biofilm Bacteria Quantified by Digital Image Analysis"

    Article Title: Co-Localized or Randomly Distributed? Pair Cross Correlation of In Vivo Grown Subgingival Biofilm Bacteria Quantified by Digital Image Analysis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0037583

    Pair cross correlation results. The mean PCC function g ( r) (continuous line) and the 95% confidence interval (dotted lines) are plotted against distances r spaced at intervals of ∼0.5 µm. The dashed horizontal reference line on the level of g ( r ) = 1 corresponds to the value of randomness and provides an internal ‘null hypothesis’ for testing attraction or repulsion between cellular units. (A) Representative, individual-related PCC of T. forsythia and F. nucleatum/periodonticum calculated for 25 images obtained from patient 01. A pronounced peak of 2.5 PCC values at 1.5 µm indicated co-localization of T. forsythia and F. nucleatum/periodonticum cells within short distances from 0–6 µm. (B) Outlier evaluation. PCC of T. forsythia and F. nucleatum/periodonticum calculated for 25 images obtained from patient 10. An initially prominent peak was in contrast to Figure 3A embedded in a wide CI, which lower boundary (−95%) dropped below the reference line, indicating a high variance in PCC values within the first 3 µm. (C) Representative, individual-related PCC of P. gingivalis and P. intermedia calculated for 32 images obtained from patient 05. P. gingivalis and P. intermedia cells are randomly distributed within the entire distance range. (D) Outlier evaluation. PCC of P. gingivalis and P. intermedia was calculated for 30 images obtained from patient 04. Similar to the outlier results of T. forsythia and F. nucleatum/periodonticum ( Figure 3 B), the high variance of PCC values at distances
    Figure Legend Snippet: Pair cross correlation results. The mean PCC function g ( r) (continuous line) and the 95% confidence interval (dotted lines) are plotted against distances r spaced at intervals of ∼0.5 µm. The dashed horizontal reference line on the level of g ( r ) = 1 corresponds to the value of randomness and provides an internal ‘null hypothesis’ for testing attraction or repulsion between cellular units. (A) Representative, individual-related PCC of T. forsythia and F. nucleatum/periodonticum calculated for 25 images obtained from patient 01. A pronounced peak of 2.5 PCC values at 1.5 µm indicated co-localization of T. forsythia and F. nucleatum/periodonticum cells within short distances from 0–6 µm. (B) Outlier evaluation. PCC of T. forsythia and F. nucleatum/periodonticum calculated for 25 images obtained from patient 10. An initially prominent peak was in contrast to Figure 3A embedded in a wide CI, which lower boundary (−95%) dropped below the reference line, indicating a high variance in PCC values within the first 3 µm. (C) Representative, individual-related PCC of P. gingivalis and P. intermedia calculated for 32 images obtained from patient 05. P. gingivalis and P. intermedia cells are randomly distributed within the entire distance range. (D) Outlier evaluation. PCC of P. gingivalis and P. intermedia was calculated for 30 images obtained from patient 04. Similar to the outlier results of T. forsythia and F. nucleatum/periodonticum ( Figure 3 B), the high variance of PCC values at distances

    Techniques Used: Periodic Counter-current Chromatography

    PCC curves of consolidated patient groups for T. forsythia versus F. nucleatum/periodonticum ( n = 8) and P. gingivalis versus P. intermedia ( n = 6). To compare the results of co-localization and randomness the patient group of each bacterial pair was merged by calculating the arithmetic mean curve with respective 95% CI by applying the equation 95% CI = m±1.96* SEM . The mean PCC curve for T. forsythia versus F. nucleatum/periodonticum (gray line, unfilled circles) and P. gingivalis /versus P. intermedia (black line, diamonds) were plotted with their respective 95% CI (dotted lines) against distances r in a range from 0–25 µm. The two curves were clearly distinguished from each other, by peak-levels and by convergence with the reference line. The fact that the lower CI of the co-localized bacteria was evidently separated from the upper CI of the randomly distributed pair of species within a wide range of 0–19 µm indicated a significant difference of both curves.
    Figure Legend Snippet: PCC curves of consolidated patient groups for T. forsythia versus F. nucleatum/periodonticum ( n = 8) and P. gingivalis versus P. intermedia ( n = 6). To compare the results of co-localization and randomness the patient group of each bacterial pair was merged by calculating the arithmetic mean curve with respective 95% CI by applying the equation 95% CI = m±1.96* SEM . The mean PCC curve for T. forsythia versus F. nucleatum/periodonticum (gray line, unfilled circles) and P. gingivalis /versus P. intermedia (black line, diamonds) were plotted with their respective 95% CI (dotted lines) against distances r in a range from 0–25 µm. The two curves were clearly distinguished from each other, by peak-levels and by convergence with the reference line. The fact that the lower CI of the co-localized bacteria was evidently separated from the upper CI of the randomly distributed pair of species within a wide range of 0–19 µm indicated a significant difference of both curves.

    Techniques Used: Periodic Counter-current Chromatography

    Representative micrograph of spatial interaction between T. forsythia and F. nucleatum/periodonticum . FISH was performed on sections of 7-day-old subgingival biofilm grown on e-PTFE carriers in gingival pockets of GAP patient 01. T. forsythia and F. nucleatum/periodonticum were fluorescently labeled with the species-specific probes TAFO-Cy3 (red) and FUNU-Cy5 (green), respectively. The spatial expansion of the entire biofilm was revealed with the domain-specific probe EUB338-FITC (blue). (A) The overlay of the Cy3, Cy5 and FITC channels shows the periodontal plaque between the gingival surface at the right edge and the carrier surface on the left. F. nucleatum/periodonticum (green) is densely packed together with T. forsythia (red) and appear to co-localize within an amorphous interwoven cluster focused on the carrier adjacent side. (B) Species-specific channels Cy3 and Cy5 in higher magnification. Single cells of T. forsythia , dispersed in the middle and right part of the biofilm, were found in close contact to F. nucleatum/periodonticum cells (arrowheads). (C–E) shows the respective binary masks of the micrograph (A) prepared for spatial arrangement analysis provided by the software daime . (C) The EUB338-FITC-channel served as reference mask to limit the calculation to the area of the biomass. (D–E) Between the segmented masks of species-specific channels TAFO-Cy3 (D) and FUNU-Cy5 (E) daime calculated the pair cross correlation function g(r) .
    Figure Legend Snippet: Representative micrograph of spatial interaction between T. forsythia and F. nucleatum/periodonticum . FISH was performed on sections of 7-day-old subgingival biofilm grown on e-PTFE carriers in gingival pockets of GAP patient 01. T. forsythia and F. nucleatum/periodonticum were fluorescently labeled with the species-specific probes TAFO-Cy3 (red) and FUNU-Cy5 (green), respectively. The spatial expansion of the entire biofilm was revealed with the domain-specific probe EUB338-FITC (blue). (A) The overlay of the Cy3, Cy5 and FITC channels shows the periodontal plaque between the gingival surface at the right edge and the carrier surface on the left. F. nucleatum/periodonticum (green) is densely packed together with T. forsythia (red) and appear to co-localize within an amorphous interwoven cluster focused on the carrier adjacent side. (B) Species-specific channels Cy3 and Cy5 in higher magnification. Single cells of T. forsythia , dispersed in the middle and right part of the biofilm, were found in close contact to F. nucleatum/periodonticum cells (arrowheads). (C–E) shows the respective binary masks of the micrograph (A) prepared for spatial arrangement analysis provided by the software daime . (C) The EUB338-FITC-channel served as reference mask to limit the calculation to the area of the biomass. (D–E) Between the segmented masks of species-specific channels TAFO-Cy3 (D) and FUNU-Cy5 (E) daime calculated the pair cross correlation function g(r) .

    Techniques Used: Fluorescence In Situ Hybridization, Labeling, Software

    29) Product Images from "Synergistic Antibacterial Effects of Nanoparticles Encapsulated with Scutellaria baicalensis and Pure Chlorhexidine on Oral Bacterial Biofilms"

    Article Title: Synergistic Antibacterial Effects of Nanoparticles Encapsulated with Scutellaria baicalensis and Pure Chlorhexidine on Oral Bacterial Biofilms

    Journal: Nanomaterials

    doi: 10.3390/nano6040061

    Effect of the Nano-MIX on the multi-species biofilms of S. mutans , F. nucleatum , A. actinomycetemcomitans , and P. gingivalis at 24 h. The confocal scanning laser microscopy (CLSM) ( A , B ) and scanning electron microscopy (SEM) images ( C , D ) showing comparative antibacterial effects of the Nano-MIX treatment ( B , D ) on the mixed-species oral biofilms with reference to the blank nanoparticles ( A , C ), respectively.
    Figure Legend Snippet: Effect of the Nano-MIX on the multi-species biofilms of S. mutans , F. nucleatum , A. actinomycetemcomitans , and P. gingivalis at 24 h. The confocal scanning laser microscopy (CLSM) ( A , B ) and scanning electron microscopy (SEM) images ( C , D ) showing comparative antibacterial effects of the Nano-MIX treatment ( B , D ) on the mixed-species oral biofilms with reference to the blank nanoparticles ( A , C ), respectively.

    Techniques Used: Microscopy, Confocal Laser Scanning Microscopy, Electron Microscopy

    30) Product Images from "The effect of supragingival glycine air polishing on periodontitis during maintenance therapy: a randomized controlled trial"

    Article Title: The effect of supragingival glycine air polishing on periodontitis during maintenance therapy: a randomized controlled trial

    Journal: PeerJ

    doi: 10.7717/peerj.4371

    The prevalence of four periodontal pathogens at different time points. SGAP group, supragingival glycine air polishing group; SUSP group, supragingival ultrasonic scaling group. (A) P. ginigvalis , (B) T. forsythia , (C) T. denticola , (D) F. nucleatum .
    Figure Legend Snippet: The prevalence of four periodontal pathogens at different time points. SGAP group, supragingival glycine air polishing group; SUSP group, supragingival ultrasonic scaling group. (A) P. ginigvalis , (B) T. forsythia , (C) T. denticola , (D) F. nucleatum .

    Techniques Used:

    31) Product Images from "Short-Chain Fatty Acids from Periodontal Pathogens Suppress Histone Deacetylases, EZH2, and SUV39H1 To Promote Kaposi's Sarcoma-Associated Herpesvirus Replication"

    Article Title: Short-Chain Fatty Acids from Periodontal Pathogens Suppress Histone Deacetylases, EZH2, and SUV39H1 To Promote Kaposi's Sarcoma-Associated Herpesvirus Replication

    Journal: Journal of Virology

    doi: 10.1128/JVI.03326-13

    Saliva from patients with severe periodontal disease contains higher levels of SCFAs. (A) Relative levels of F. nucleatum (Fn) and P. gingivalis (Pg) in the saliva of patients with severe periodontal disease (PD) and healthy controls (Ctl). (B) Relative
    Figure Legend Snippet: Saliva from patients with severe periodontal disease contains higher levels of SCFAs. (A) Relative levels of F. nucleatum (Fn) and P. gingivalis (Pg) in the saliva of patients with severe periodontal disease (PD) and healthy controls (Ctl). (B) Relative

    Techniques Used: CTL Assay

    F. nucleatum and P. gingivalis supernatants induce KSHV lytic gene expression in acutely infected HOECs and latently infected and telomerase-immortalized human umbilical vein endothelial cells (TIVE-KSHV). (A and B) Relative mRNA levels of KSHV lytic
    Figure Legend Snippet: F. nucleatum and P. gingivalis supernatants induce KSHV lytic gene expression in acutely infected HOECs and latently infected and telomerase-immortalized human umbilical vein endothelial cells (TIVE-KSHV). (A and B) Relative mRNA levels of KSHV lytic

    Techniques Used: Expressing, Infection

    Supernatants of P. gingivalis and F. nucleatum induce KSHV lytic gene expression and replication. (A) Schematic illustration of the mutant KSHV BAC36-ORF65Δ/lucif in which the open reading frame (ORF) of the viral small capsid protein (ORF65)
    Figure Legend Snippet: Supernatants of P. gingivalis and F. nucleatum induce KSHV lytic gene expression and replication. (A) Schematic illustration of the mutant KSHV BAC36-ORF65Δ/lucif in which the open reading frame (ORF) of the viral small capsid protein (ORF65)

    Techniques Used: Expressing, Mutagenesis

    P. gingivalis and F. nucleatum produce multiple SCFAs to synergistically induce KSHV lytic replication.
    Figure Legend Snippet: P. gingivalis and F. nucleatum produce multiple SCFAs to synergistically induce KSHV lytic replication.

    Techniques Used:

    32) Product Images from "In vitro Increased Respiratory Activity of Selected Oral Bacteria May Explain Competitive and Collaborative Interactions in the Oral Microbiome"

    Article Title: In vitro Increased Respiratory Activity of Selected Oral Bacteria May Explain Competitive and Collaborative Interactions in the Oral Microbiome

    Journal: Frontiers in Cellular and Infection Microbiology

    doi: 10.3389/fcimb.2017.00235

    Specific groups of metabolites influenced respiratory activity of each bacterial community. Principal Coordinate Analysis assisted to explain the grouping trends in the cluster analysis, and highlighted similarities in the respiratory activity among the selected oral bacteria at 24 h (A) and 48 h (B) . Aa, Aggregatibacter actinomycetemcomitans (ATCC 43718); Fn, Fusobacterium nucleatum (ATCC 10953); Pg, Porphyromonas gingivalis (ATCC 33277); Pi, Prevotella intermedia (ATCC 25611); Sm, Streptococcus mutans (ATCC 25175); Ssob, Streptococcus sobrinus (ATCC 33478); Tf, Tannerella forsythia (ATCC 43037); An, Actinomyces naeslundii (ATCC 51655); Csput, Capnocytophaga sputigena (ATCC 33612); Sgord, Streptococcus gordonii (ATCC 49818); Avisc, Actinomyces viscosus (ATCC 15987); Smitis, Streptococcus mitis (ATCC 49456); Vparv, Veillonella parvula (DSM 2007); Ssang, Streptococcus sanguinis (LMG 14657), and Ssal, Streptococcus salivarius strain TOVE-R.
    Figure Legend Snippet: Specific groups of metabolites influenced respiratory activity of each bacterial community. Principal Coordinate Analysis assisted to explain the grouping trends in the cluster analysis, and highlighted similarities in the respiratory activity among the selected oral bacteria at 24 h (A) and 48 h (B) . Aa, Aggregatibacter actinomycetemcomitans (ATCC 43718); Fn, Fusobacterium nucleatum (ATCC 10953); Pg, Porphyromonas gingivalis (ATCC 33277); Pi, Prevotella intermedia (ATCC 25611); Sm, Streptococcus mutans (ATCC 25175); Ssob, Streptococcus sobrinus (ATCC 33478); Tf, Tannerella forsythia (ATCC 43037); An, Actinomyces naeslundii (ATCC 51655); Csput, Capnocytophaga sputigena (ATCC 33612); Sgord, Streptococcus gordonii (ATCC 49818); Avisc, Actinomyces viscosus (ATCC 15987); Smitis, Streptococcus mitis (ATCC 49456); Vparv, Veillonella parvula (DSM 2007); Ssang, Streptococcus sanguinis (LMG 14657), and Ssal, Streptococcus salivarius strain TOVE-R.

    Techniques Used: Activity Assay

    33) Product Images from "Combined antioxidant effects of Neem extract, bacteria, red blood cells and Lysozyme: possible relation to periodontal disease"

    Article Title: Combined antioxidant effects of Neem extract, bacteria, red blood cells and Lysozyme: possible relation to periodontal disease

    Journal: BMC Complementary and Alternative Medicine

    doi: 10.1186/s12906-017-1900-3

    Modulation of luminescence by F. nucleatum alone or complexed with Neem leaf extract (50 μM GAE), when incubated with one of the following peptides: Lysozyme (LYS, 20 μl of 20 μg/ml) or chlorhexidine (CHX, 20 μl of 0.2% solution)
    Figure Legend Snippet: Modulation of luminescence by F. nucleatum alone or complexed with Neem leaf extract (50 μM GAE), when incubated with one of the following peptides: Lysozyme (LYS, 20 μl of 20 μg/ml) or chlorhexidine (CHX, 20 μl of 0.2% solution)

    Techniques Used: Incubation

    Bacterial growth kinetics of P. gingivalis ( a ) and F. nucleatum ( b ) during 48 h and 24 h incubation, respectively. Six experimental groups were compared for each bacterial strain: two control groups (Neem-free bacterial suspensions, containing ethanol or PBS), and six Neem leaf extract groups with increasing concentrations, expressed as Gallic Acid Equivalent (GAE). n = 6 for each experimental group. * P
    Figure Legend Snippet: Bacterial growth kinetics of P. gingivalis ( a ) and F. nucleatum ( b ) during 48 h and 24 h incubation, respectively. Six experimental groups were compared for each bacterial strain: two control groups (Neem-free bacterial suspensions, containing ethanol or PBS), and six Neem leaf extract groups with increasing concentrations, expressed as Gallic Acid Equivalent (GAE). n = 6 for each experimental group. * P

    Techniques Used: Incubation

    34) Product Images from "Diverse Toll-Like Receptors Mediate Cytokine Production by Fusobacterium nucleatum and Aggregatibacter actinomycetemcomitans in Macrophages"

    Article Title: Diverse Toll-Like Receptors Mediate Cytokine Production by Fusobacterium nucleatum and Aggregatibacter actinomycetemcomitans in Macrophages

    Journal: Infection and Immunity

    doi: 10.1128/IAI.01226-13

    Cytokines production by WT and MyD88-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans infection. BMDMs from WT and MyD88-deficient mice were infected with F. nucleatum or A. actinomycetemcomitans for 6 h, and, as indicated, the
    Figure Legend Snippet: Cytokines production by WT and MyD88-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans infection. BMDMs from WT and MyD88-deficient mice were infected with F. nucleatum or A. actinomycetemcomitans for 6 h, and, as indicated, the

    Techniques Used: Infection, Mouse Assay

    Production of IL-6 and TNF-α in WT and TLR2/4- and MyD88-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans infection. WT and TLR2/4-, and MyD88-deficient BMDMs were infected with F. nucleatum and A. actinomycetemcomitans
    Figure Legend Snippet: Production of IL-6 and TNF-α in WT and TLR2/4- and MyD88-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans infection. WT and TLR2/4-, and MyD88-deficient BMDMs were infected with F. nucleatum and A. actinomycetemcomitans

    Techniques Used: Infection

    Effect of NF-κB and MAPKs on F. nucleatum - and A. actinomycetemcomitans -induced production of cytokines by macrophages. WT BMDMs were pretreated with various doses of each inhibitor 2 h before infection. The cells were then infected with F. nucleatum
    Figure Legend Snippet: Effect of NF-κB and MAPKs on F. nucleatum - and A. actinomycetemcomitans -induced production of cytokines by macrophages. WT BMDMs were pretreated with various doses of each inhibitor 2 h before infection. The cells were then infected with F. nucleatum

    Techniques Used: Infection

    Effect of endosomal TLRs and bacterial DNA on cytokine production by macrophages in response to F. nucleatum or A. actinomycetemcomitans infection. TLR2/4-deficient BMDMs were pretreated with chloroquine (CLQ) 2 h before infection. The cells were then
    Figure Legend Snippet: Effect of endosomal TLRs and bacterial DNA on cytokine production by macrophages in response to F. nucleatum or A. actinomycetemcomitans infection. TLR2/4-deficient BMDMs were pretreated with chloroquine (CLQ) 2 h before infection. The cells were then

    Techniques Used: Infection

    Production of IL-6 and TNF-α by WT and TLR2-, TLR4-, and TLR2/4-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans . BMDMs were infected with F. nucleatum or A. actinomycetemcomitans at the indicated MOI. At 6 (A to D) or
    Figure Legend Snippet: Production of IL-6 and TNF-α by WT and TLR2-, TLR4-, and TLR2/4-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans . BMDMs were infected with F. nucleatum or A. actinomycetemcomitans at the indicated MOI. At 6 (A to D) or

    Techniques Used: Infection

    NF-κB and MAPK activation in WT and TLR2/4-, and MyD88-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans infection. Cells were infected with F. nucleatum or A. actinomycetemcomitans at an MOI of 1/100, and cellular protein
    Figure Legend Snippet: NF-κB and MAPK activation in WT and TLR2/4-, and MyD88-deficient BMDMs in response to F. nucleatum and A. actinomycetemcomitans infection. Cells were infected with F. nucleatum or A. actinomycetemcomitans at an MOI of 1/100, and cellular protein

    Techniques Used: Activation Assay, Infection

    35) Product Images from "Indoleamine 2,3-dioxygenase expression regulates the survival and proliferation of Fusobacterium nucleatum in THP-1-derived macrophages"

    Article Title: Indoleamine 2,3-dioxygenase expression regulates the survival and proliferation of Fusobacterium nucleatum in THP-1-derived macrophages

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-018-0389-0

    Involvement of IL-6 and TNF-α in the induction of IDO by F. nucleatum -infected THP-1 cells. TNF-α ( a ) and IL-6 ( b ) levels in the supernatants of Fn - or heat-killed Fn -infected dTHP1 cells at an MOI of 10:1 for the indicated times. c IDO expression was assessed by Western blot at 48 h. d mRNA expression of IL-6 and TNF-α level in the presence of PMB with the indicated dosages. IDO enzymatic activity in supernatants ( e ) and representative western blots for IDO in cells lysates ( f ) of live Fn -infected dTHP1 cells (MOI: 10:1) in the presence of neutralizing antibodies to TNF-α and/or PBM for 48 h. Bars represent the mean ± SD of the results from triplicate determinations. ^Below the detection limit. * P
    Figure Legend Snippet: Involvement of IL-6 and TNF-α in the induction of IDO by F. nucleatum -infected THP-1 cells. TNF-α ( a ) and IL-6 ( b ) levels in the supernatants of Fn - or heat-killed Fn -infected dTHP1 cells at an MOI of 10:1 for the indicated times. c IDO expression was assessed by Western blot at 48 h. d mRNA expression of IL-6 and TNF-α level in the presence of PMB with the indicated dosages. IDO enzymatic activity in supernatants ( e ) and representative western blots for IDO in cells lysates ( f ) of live Fn -infected dTHP1 cells (MOI: 10:1) in the presence of neutralizing antibodies to TNF-α and/or PBM for 48 h. Bars represent the mean ± SD of the results from triplicate determinations. ^Below the detection limit. * P

    Techniques Used: Infection, Expressing, Western Blot, Activity Assay

    F. nucleatum survives and undergoes limited intracellular proliferation in THP-1-derived macrophages. Intracellular bacteria proliferation was assessed by gentamycin protection assay. Fn -dTHP1 cells with or without treated by 1-MT were lysed at the indicated time-points after infection, and the numbers of total viable bacteria ( a ) and viable bacteria per macrophage ( b ) were determined by the serial dilution method. c Immunofluorescence staining of intracellular Fn (red) was observed by confocal microscope at 24 h and 72 h (×60). d The apoptotic cells were analyzed by flow cytometry at 72 h. Bars represent the mean ± SD of the results from triplicate determinations. * P
    Figure Legend Snippet: F. nucleatum survives and undergoes limited intracellular proliferation in THP-1-derived macrophages. Intracellular bacteria proliferation was assessed by gentamycin protection assay. Fn -dTHP1 cells with or without treated by 1-MT were lysed at the indicated time-points after infection, and the numbers of total viable bacteria ( a ) and viable bacteria per macrophage ( b ) were determined by the serial dilution method. c Immunofluorescence staining of intracellular Fn (red) was observed by confocal microscope at 24 h and 72 h (×60). d The apoptotic cells were analyzed by flow cytometry at 72 h. Bars represent the mean ± SD of the results from triplicate determinations. * P

    Techniques Used: Derivative Assay, Infection, Serial Dilution, Immunofluorescence, Staining, Microscopy, Flow Cytometry, Cytometry

    Growth of F. nucleatum is regulated by tryptophan and kynurenine in a dose-dependent manner. a Fn grew in a tryptophan dose-dependent manner. b The growth of Fn was inhibited with kynurenine in a dose-dependent manner. Bacterial growth was assessed in enriched BHI broth by spectrophotometry. Columns indicate the mean of six replicate measurements, and bars indicate the SD (** P
    Figure Legend Snippet: Growth of F. nucleatum is regulated by tryptophan and kynurenine in a dose-dependent manner. a Fn grew in a tryptophan dose-dependent manner. b The growth of Fn was inhibited with kynurenine in a dose-dependent manner. Bacterial growth was assessed in enriched BHI broth by spectrophotometry. Columns indicate the mean of six replicate measurements, and bars indicate the SD (** P

    Techniques Used: Spectrophotometry

    F. nucleatum invades THP-1-derived macrophages. THP-1-derived macrophages (dTHP1) were infected with F. nucleatum ( Fn ) at a MOI of 10:1 (bacteria:cells) for 48 h. Immunofluorescence staining of live Fn infection ( a ) and heat-killed Fn infection ( b ) were observed by confocal microscope (×60). c After 72 h co-culture, the recovery colonies numbers of average cell lysis and supernatant liquid. d Gram staining of Fn bacteria (×100) and Fn -infected dTHP1 cells (×20) were observed by light microscope. Bacteria external to the host cell were labeled with both Cy3 (red) and FITC (green), bacteria inside the cells were labeled with Cy3 (appearing red when channels were merged). Scale bar = 10 μm. *** P
    Figure Legend Snippet: F. nucleatum invades THP-1-derived macrophages. THP-1-derived macrophages (dTHP1) were infected with F. nucleatum ( Fn ) at a MOI of 10:1 (bacteria:cells) for 48 h. Immunofluorescence staining of live Fn infection ( a ) and heat-killed Fn infection ( b ) were observed by confocal microscope (×60). c After 72 h co-culture, the recovery colonies numbers of average cell lysis and supernatant liquid. d Gram staining of Fn bacteria (×100) and Fn -infected dTHP1 cells (×20) were observed by light microscope. Bacteria external to the host cell were labeled with both Cy3 (red) and FITC (green), bacteria inside the cells were labeled with Cy3 (appearing red when channels were merged). Scale bar = 10 μm. *** P

    Techniques Used: Derivative Assay, Infection, Immunofluorescence, Staining, Microscopy, Co-Culture Assay, Lysis, Light Microscopy, Labeling

    F. nucleatum infection exhibits little or no effect on the cell viability of THP-1-derived macrophages. dTHP1 cells were infected with dead F. nucleatum ( Fn ) (heat-killed- Fn , grey) or live Fn ( Fn , dark grey) at a MOI of 10:1 (bacteria:cells) for the indicated time-points. a Morphology was observed at 72 h; b cell viability was measured by an MTT assay; c , d the apoptotic cells were analyzed by flow cytometry at 72 h; e the PI3K/AKT and ERK signaling pathway were analyzed by western blot from 1 h to 4 h and f quantitation was performed using pixel density analysis. Data indicate the mean ± standard deviation (SD) of triplicate-infected cultures. Bars represent the mean ± SD of the results from replicate measurements. * P
    Figure Legend Snippet: F. nucleatum infection exhibits little or no effect on the cell viability of THP-1-derived macrophages. dTHP1 cells were infected with dead F. nucleatum ( Fn ) (heat-killed- Fn , grey) or live Fn ( Fn , dark grey) at a MOI of 10:1 (bacteria:cells) for the indicated time-points. a Morphology was observed at 72 h; b cell viability was measured by an MTT assay; c , d the apoptotic cells were analyzed by flow cytometry at 72 h; e the PI3K/AKT and ERK signaling pathway were analyzed by western blot from 1 h to 4 h and f quantitation was performed using pixel density analysis. Data indicate the mean ± standard deviation (SD) of triplicate-infected cultures. Bars represent the mean ± SD of the results from replicate measurements. * P

    Techniques Used: Infection, Derivative Assay, MTT Assay, Flow Cytometry, Cytometry, Western Blot, Quantitation Assay, Standard Deviation

    F. nucleatum infection induces IDO expression in THP-1-derived macrophages in a dose-dependent and time-dependent manner. a IDO mRNA expression assessed by qRT-PCR, b induction of IDO enzymatic activity by HPLC, and c , d representative western blots for IDO protein expression in dTHP1 cells infected with live Fn or heat-killed- Fn for 48 h at different dosages; e IDO mRNA expression assessed by qRT-PCR, f induction of IDO enzymatic activity by HPLC and g , h representative western blots for IDO protein expression in dTHP1 cells infected with live Fn or heat-killed- Fn at a MOI of 10:1 for the indicated time-points; i Fn -infected dTHP1 cells exhibit positive cytoplasmic staining for IDO at a MOI of 10:1 for 48 h and j negative staining for uninfected-dTHP1 cells as detected by immunohistochemistry. Bars represent the mean ± SD of the results from replicate measurements. ^Below the detection limit. * P
    Figure Legend Snippet: F. nucleatum infection induces IDO expression in THP-1-derived macrophages in a dose-dependent and time-dependent manner. a IDO mRNA expression assessed by qRT-PCR, b induction of IDO enzymatic activity by HPLC, and c , d representative western blots for IDO protein expression in dTHP1 cells infected with live Fn or heat-killed- Fn for 48 h at different dosages; e IDO mRNA expression assessed by qRT-PCR, f induction of IDO enzymatic activity by HPLC and g , h representative western blots for IDO protein expression in dTHP1 cells infected with live Fn or heat-killed- Fn at a MOI of 10:1 for the indicated time-points; i Fn -infected dTHP1 cells exhibit positive cytoplasmic staining for IDO at a MOI of 10:1 for 48 h and j negative staining for uninfected-dTHP1 cells as detected by immunohistochemistry. Bars represent the mean ± SD of the results from replicate measurements. ^Below the detection limit. * P

    Techniques Used: Infection, Expressing, Derivative Assay, Quantitative RT-PCR, Activity Assay, High Performance Liquid Chromatography, Western Blot, Staining, Negative Staining, Immunohistochemistry

    F. nucleatum infection induces classically activated THP-1-derived macrophages. The mRNA levels of a cytokines (INF-γ, TNF-α, IL-6, IL-12p40, IL-10); b MHC class II cell surface receptors (HLA-DR, CD80); M2-polarized phenotype markers (CD206, CD163); and chemokine receptors (CCR7, CXCR4) were assessed by qRT-PCR in dTHP1 cells infected with heat-killed- Fn or live Fn at an MOI of 10:1 for 24 h. The expression of the M1-polarized phenotype marker CCR7, CXCR4, and HLA-DR in dTHP1 cells with live/heated-killed Fn at an MOI of 10:1 for 48 h was analyzed by flow cytometry ( c ) and western blot ( d ). Bars represent the mean ± SD of the results from replicate measurements. * P
    Figure Legend Snippet: F. nucleatum infection induces classically activated THP-1-derived macrophages. The mRNA levels of a cytokines (INF-γ, TNF-α, IL-6, IL-12p40, IL-10); b MHC class II cell surface receptors (HLA-DR, CD80); M2-polarized phenotype markers (CD206, CD163); and chemokine receptors (CCR7, CXCR4) were assessed by qRT-PCR in dTHP1 cells infected with heat-killed- Fn or live Fn at an MOI of 10:1 for 24 h. The expression of the M1-polarized phenotype marker CCR7, CXCR4, and HLA-DR in dTHP1 cells with live/heated-killed Fn at an MOI of 10:1 for 48 h was analyzed by flow cytometry ( c ) and western blot ( d ). Bars represent the mean ± SD of the results from replicate measurements. * P

    Techniques Used: Infection, Derivative Assay, Quantitative RT-PCR, Expressing, Marker, Flow Cytometry, Cytometry, Western Blot

    Related Articles

    Clone Assay:

    Article Title: Forward Genetic Dissection of Biofilm Development by Fusobacterium nucleatum: Novel Functions of Cell Division Proteins FtsX and EnvC
    Article Snippet: .. To construct this vector, primer sets PcatP-F/R and com-FtsX-F/R ( ) were used to amplify the catP promoter from plasmid pHS30 and the ftsX coding region from the genomic DNA of F. nucleatum ATCC 23726, appending SacI/KpnI or KpnI/XhoI sites for cloning purposes, respectively. .. The PCR products were cut by SacI/KpnI or KpnI/XhoI and cloned into the SacI and XhoI sites of pCWU6.

    Amplification:

    Article Title: Characterization of Fusobacterium nucleatum ATCC 23726 adhesins involved in strain-specific attachment to Porphyromonas gingivalis
    Article Snippet: .. For F. nucleatum ATCC 23726 and its mutant derivatives, a portion of the Fusobacterium -specific fomA gene was amplified with Fn-F (forward) 5′-AGTTGCTCCAGCTTGGAGACCAAAT-3′ and Fn-R (reverse) 5′-AAGTTTACTTTTGTTAAAGTTTGTAATCTTCC-3′ primers. ..

    Mutagenesis:

    Article Title: Characterization of Fusobacterium nucleatum ATCC 23726 adhesins involved in strain-specific attachment to Porphyromonas gingivalis
    Article Snippet: .. For F. nucleatum ATCC 23726 and its mutant derivatives, a portion of the Fusobacterium -specific fomA gene was amplified with Fn-F (forward) 5′-AGTTGCTCCAGCTTGGAGACCAAAT-3′ and Fn-R (reverse) 5′-AAGTTTACTTTTGTTAAAGTTTGTAATCTTCC-3′ primers. ..

    Construct:

    Article Title: Forward Genetic Dissection of Biofilm Development by Fusobacterium nucleatum: Novel Functions of Cell Division Proteins FtsX and EnvC
    Article Snippet: .. To construct this vector, primer sets PcatP-F/R and com-FtsX-F/R ( ) were used to amplify the catP promoter from plasmid pHS30 and the ftsX coding region from the genomic DNA of F. nucleatum ATCC 23726, appending SacI/KpnI or KpnI/XhoI sites for cloning purposes, respectively. .. The PCR products were cut by SacI/KpnI or KpnI/XhoI and cloned into the SacI and XhoI sites of pCWU6.

    other:

    Article Title: Insights into the Evolution of Host Association through the Isolation and Characterization of a Novel Human Periodontal Pathobiont, Desulfobulbus oralis
    Article Snippet: CFS from a type strain of F. nucleatum (ATCC 23726) also supported the growth of D. oralis , indicating its physiological dependence is not restricted to the strain it coenriched with, although we have not extended that analysis to additional strains or species.

    Binding Assay:

    Article Title: Characterization of Fusobacterium nucleatum ATCC 23726 adhesins involved in strain-specific attachment to Porphyromonas gingivalis
    Article Snippet: .. Autoaggregation of bacteria and coaggregation of F. nucleatum ATCC 23726 with P. gingivalis displays a strain-specific profile Qualitative and quantitative autoaggregation and coaggregation assays revealed a strain-dependent binding profile of F. nucleatum ATCC 23726 with the seven different strains of P. gingivalis tested in this study. .. Robust interactions were observed with P. gingivalis strains 4612 (62%±8% coaggregation), T22 (54%±8% coaggregation) binding and ATCC 33277 (65%±17% coaggregation; ).

    Plasmid Preparation:

    Article Title: Forward Genetic Dissection of Biofilm Development by Fusobacterium nucleatum: Novel Functions of Cell Division Proteins FtsX and EnvC
    Article Snippet: .. To construct this vector, primer sets PcatP-F/R and com-FtsX-F/R ( ) were used to amplify the catP promoter from plasmid pHS30 and the ftsX coding region from the genomic DNA of F. nucleatum ATCC 23726, appending SacI/KpnI or KpnI/XhoI sites for cloning purposes, respectively. .. The PCR products were cut by SacI/KpnI or KpnI/XhoI and cloned into the SacI and XhoI sites of pCWU6.

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  • 86
    ATCC f nucleatum induced increase
    (a and b) RANKL expression in PDL cells stimulated by F. <t>nucleatum</t> ATCC 25586 and/or CTSH at 1 day (a) and 3 days (b). (c and d) OPG expression in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (c) and 3 days (d). (e and f) RANKL/OPG mRNA ratio in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (e) and 3 days (f). *Significant difference compared to other groups ( P
    F Nucleatum Induced Increase, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/f nucleatum induced increase/product/ATCC
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    88
    ATCC f nucleatum binding
    F. <t>nucleatum</t> Interacts with TIGIT
    F Nucleatum Binding, supplied by ATCC, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    ATCC f nucleatum subsp
    Comparison of the QRDRs (5′ end of gyrA ) of resistant strains F. canifelinum RMA 1036 T (ATCC BAA 689 T ) and RMA 12701 (ATCC BAA 690) and closely related susceptible strains F. <t>nucleatum</t> <t>subsp.</t> nucleatum ATCC 25586 T and F. nucleatum subsp. vincentii ) was used for alignment.
    F Nucleatum Subsp, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    ATCC f nucleatum
    Levels of proinflammatory IL6 in vivo and in vitro . A and B: Local tissue Il6 mRNA levels in healthy and inflamed gingivae nine days after ligature placement are shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). * P =0.05, ** P =0.006 for healthy vs . inflamed tissues in WT and MIF KO mice and ** P =0.01 for inflamed sites in WT vs . MIF KO animals. Grey bars: WT mice (n=6), white bars: MIF KO mice (n=6). Results are shown as mean values ±SD, each sample was run in duplicate. C: Levels of IL6 released from HGFs after stimulation with HC, MIF or F. <t>nucleatum</t> (* P ) was employed. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.
    F Nucleatum, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (a and b) RANKL expression in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (a) and 3 days (b). (c and d) OPG expression in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (c) and 3 days (d). (e and f) RANKL/OPG mRNA ratio in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (e) and 3 days (f). *Significant difference compared to other groups ( P

    Journal: Mediators of Inflammation

    Article Title: Biomechanical Loading Modulates Proinflammatory and Bone Resorptive Mediators in Bacterial-Stimulated PDL Cells

    doi: 10.1155/2014/425421

    Figure Lengend Snippet: (a and b) RANKL expression in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (a) and 3 days (b). (c and d) OPG expression in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (c) and 3 days (d). (e and f) RANKL/OPG mRNA ratio in PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (e) and 3 days (f). *Significant difference compared to other groups ( P

    Article Snippet: In our study, CTS aggravated F. nucleatum -induced increase in the production of COX2 and PGE2 and reduced the expression and production of OPG, leading to an increase in RANKL/OPG ratio in this group compared to F. nucleatum ATCC 25586 alone.

    Techniques: Expressing

    (a and b) Synthesis of RANKL protein in supernatants of PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (a) and 3 days (b). (c and d) Synthesis of OPG protein in supernatants of PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (c) and 3 days (d). (e and f) RANKL/OPG protein ratio in supernatants of PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (e) and 3 days (f). *Significant difference compared to other groups ( P

    Journal: Mediators of Inflammation

    Article Title: Biomechanical Loading Modulates Proinflammatory and Bone Resorptive Mediators in Bacterial-Stimulated PDL Cells

    doi: 10.1155/2014/425421

    Figure Lengend Snippet: (a and b) Synthesis of RANKL protein in supernatants of PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (a) and 3 days (b). (c and d) Synthesis of OPG protein in supernatants of PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (c) and 3 days (d). (e and f) RANKL/OPG protein ratio in supernatants of PDL cells stimulated by F. nucleatum ATCC 25586 and/or CTSH at 1 day (e) and 3 days (f). *Significant difference compared to other groups ( P

    Article Snippet: In our study, CTS aggravated F. nucleatum -induced increase in the production of COX2 and PGE2 and reduced the expression and production of OPG, leading to an increase in RANKL/OPG ratio in this group compared to F. nucleatum ATCC 25586 alone.

    Techniques:

    (a) COX2 expression in PDL cells stimulated by F. nucleatum ATCC 25586 over time. (b) COX2 expression in PDL cells stimulated by various concentrations of F. nucleatum ATCC 25586 at 1 day. (c) OPG expression in PDL cells stimulated by F. nucleatum ATCC 25586 over time. (d) OPG expression in PDL cells stimulated by various concentrations of F. nucleatum ATCC 25586 at 1 day. (e) COX2 expression in PDL cells stimulated by F. nucleatum ATCC 25586 (OD 0.025) in the presence or in the absence of anti-TLR2 or anti-TLR4 antibodies at 1 day. *Significant difference between groups ( P

    Journal: Mediators of Inflammation

    Article Title: Biomechanical Loading Modulates Proinflammatory and Bone Resorptive Mediators in Bacterial-Stimulated PDL Cells

    doi: 10.1155/2014/425421

    Figure Lengend Snippet: (a) COX2 expression in PDL cells stimulated by F. nucleatum ATCC 25586 over time. (b) COX2 expression in PDL cells stimulated by various concentrations of F. nucleatum ATCC 25586 at 1 day. (c) OPG expression in PDL cells stimulated by F. nucleatum ATCC 25586 over time. (d) OPG expression in PDL cells stimulated by various concentrations of F. nucleatum ATCC 25586 at 1 day. (e) COX2 expression in PDL cells stimulated by F. nucleatum ATCC 25586 (OD 0.025) in the presence or in the absence of anti-TLR2 or anti-TLR4 antibodies at 1 day. *Significant difference between groups ( P

    Article Snippet: In our study, CTS aggravated F. nucleatum -induced increase in the production of COX2 and PGE2 and reduced the expression and production of OPG, leading to an increase in RANKL/OPG ratio in this group compared to F. nucleatum ATCC 25586 alone.

    Techniques: Expressing

    (a) Synthesis of COX2 in lysates of PDL cells treated with F. nucleatum ATCC 25586 and/or cyclic tensile strain (CTS) of low (CTSL, 3%) and high (CTSH, 20%) magnitudes at 36 hours. (b and c) Production of PGE2 in supernatants of PDL cells treated with F. nucleatum ATCC 25586 and/or CTSL and CTSH at 1 day (b) and 3 days (c). *Significant difference compared to other groups ( P

    Journal: Mediators of Inflammation

    Article Title: Biomechanical Loading Modulates Proinflammatory and Bone Resorptive Mediators in Bacterial-Stimulated PDL Cells

    doi: 10.1155/2014/425421

    Figure Lengend Snippet: (a) Synthesis of COX2 in lysates of PDL cells treated with F. nucleatum ATCC 25586 and/or cyclic tensile strain (CTS) of low (CTSL, 3%) and high (CTSH, 20%) magnitudes at 36 hours. (b and c) Production of PGE2 in supernatants of PDL cells treated with F. nucleatum ATCC 25586 and/or CTSL and CTSH at 1 day (b) and 3 days (c). *Significant difference compared to other groups ( P

    Article Snippet: In our study, CTS aggravated F. nucleatum -induced increase in the production of COX2 and PGE2 and reduced the expression and production of OPG, leading to an increase in RANKL/OPG ratio in this group compared to F. nucleatum ATCC 25586 alone.

    Techniques:

    F. nucleatum Interacts with TIGIT

    Journal: Immunity

    Article Title: Binding of the Fap2 Protein of Fusobacterium nucleatum to Human Inhibitory Receptor TIGIT Protects Tumors from Immune Cell Attack

    doi: 10.1016/j.immuni.2015.01.010

    Figure Lengend Snippet: F. nucleatum Interacts with TIGIT

    Article Snippet: To test whether the origin of the tumor (epithelial versus hematopoietic) is important for F. nucleatum binding, we used FITC labeled F. nucleatum ATCC strain 23726 (herein named 726) and examined its binding to the human Epstein Bar Virus (EBV) transformed B cell line 721.221, to the human erythroleukemic line K562, and to the human colorectal carcinoma cell line RKO ( ).

    Techniques:

    F. nucleatum Inhibits YTS Cytotoxicity via TIGIT

    Journal: Immunity

    Article Title: Binding of the Fap2 Protein of Fusobacterium nucleatum to Human Inhibitory Receptor TIGIT Protects Tumors from Immune Cell Attack

    doi: 10.1016/j.immuni.2015.01.010

    Figure Lengend Snippet: F. nucleatum Inhibits YTS Cytotoxicity via TIGIT

    Article Snippet: To test whether the origin of the tumor (epithelial versus hematopoietic) is important for F. nucleatum binding, we used FITC labeled F. nucleatum ATCC strain 23726 (herein named 726) and examined its binding to the human Epstein Bar Virus (EBV) transformed B cell line 721.221, to the human erythroleukemic line K562, and to the human colorectal carcinoma cell line RKO ( ).

    Techniques:

    F. nucleatum Inhibits Primary NK Cytotoxicity via TIGIT in an Hemagglutination-Dependent Manner

    Journal: Immunity

    Article Title: Binding of the Fap2 Protein of Fusobacterium nucleatum to Human Inhibitory Receptor TIGIT Protects Tumors from Immune Cell Attack

    doi: 10.1016/j.immuni.2015.01.010

    Figure Lengend Snippet: F. nucleatum Inhibits Primary NK Cytotoxicity via TIGIT in an Hemagglutination-Dependent Manner

    Article Snippet: To test whether the origin of the tumor (epithelial versus hematopoietic) is important for F. nucleatum binding, we used FITC labeled F. nucleatum ATCC strain 23726 (herein named 726) and examined its binding to the human Epstein Bar Virus (EBV) transformed B cell line 721.221, to the human erythroleukemic line K562, and to the human colorectal carcinoma cell line RKO ( ).

    Techniques:

    TIGIT Interacts with the Fap2 Protein of F. nucleatum

    Journal: Immunity

    Article Title: Binding of the Fap2 Protein of Fusobacterium nucleatum to Human Inhibitory Receptor TIGIT Protects Tumors from Immune Cell Attack

    doi: 10.1016/j.immuni.2015.01.010

    Figure Lengend Snippet: TIGIT Interacts with the Fap2 Protein of F. nucleatum

    Article Snippet: To test whether the origin of the tumor (epithelial versus hematopoietic) is important for F. nucleatum binding, we used FITC labeled F. nucleatum ATCC strain 23726 (herein named 726) and examined its binding to the human Epstein Bar Virus (EBV) transformed B cell line 721.221, to the human erythroleukemic line K562, and to the human colorectal carcinoma cell line RKO ( ).

    Techniques:

    F. nucleatum Protects Tumor Cells from NK Cell Killing

    Journal: Immunity

    Article Title: Binding of the Fap2 Protein of Fusobacterium nucleatum to Human Inhibitory Receptor TIGIT Protects Tumors from Immune Cell Attack

    doi: 10.1016/j.immuni.2015.01.010

    Figure Lengend Snippet: F. nucleatum Protects Tumor Cells from NK Cell Killing

    Article Snippet: To test whether the origin of the tumor (epithelial versus hematopoietic) is important for F. nucleatum binding, we used FITC labeled F. nucleatum ATCC strain 23726 (herein named 726) and examined its binding to the human Epstein Bar Virus (EBV) transformed B cell line 721.221, to the human erythroleukemic line K562, and to the human colorectal carcinoma cell line RKO ( ).

    Techniques:

    Comparison of the QRDRs (5′ end of gyrA ) of resistant strains F. canifelinum RMA 1036 T (ATCC BAA 689 T ) and RMA 12701 (ATCC BAA 690) and closely related susceptible strains F. nucleatum subsp. nucleatum ATCC 25586 T and F. nucleatum subsp. vincentii ) was used for alignment.

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Genetic Determinant of Intrinsic Quinolone Resistance in Fusobacterium canifelinum

    doi: 10.1128/AAC.49.1.434-437.2005

    Figure Lengend Snippet: Comparison of the QRDRs (5′ end of gyrA ) of resistant strains F. canifelinum RMA 1036 T (ATCC BAA 689 T ) and RMA 12701 (ATCC BAA 690) and closely related susceptible strains F. nucleatum subsp. nucleatum ATCC 25586 T and F. nucleatum subsp. vincentii ) was used for alignment.

    Article Snippet: By screening the proteins derived from the genome sequences of F. nucleatum subsp. nucleatum ATCC 25586 (GenBank accession no. [complete]) and F. nucleatum subsp. vincentii ATCC 49256 (GenBank accession no. AABF1000051 [almost complete]), we found that topoisomerase IV was absent.

    Techniques:

    Levels of proinflammatory IL6 in vivo and in vitro . A and B: Local tissue Il6 mRNA levels in healthy and inflamed gingivae nine days after ligature placement are shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). * P =0.05, ** P =0.006 for healthy vs . inflamed tissues in WT and MIF KO mice and ** P =0.01 for inflamed sites in WT vs . MIF KO animals. Grey bars: WT mice (n=6), white bars: MIF KO mice (n=6). Results are shown as mean values ±SD, each sample was run in duplicate. C: Levels of IL6 released from HGFs after stimulation with HC, MIF or F. nucleatum (* P ) was employed. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.

    Journal: European journal of oral sciences

    Article Title: Assessment of the involvement of the macrophage migration inhibitory factor (MIF)-glucocorticoid regulatory dyad in MMP2 expression during periodontitis

    doi: 10.1111/eos.12363

    Figure Lengend Snippet: Levels of proinflammatory IL6 in vivo and in vitro . A and B: Local tissue Il6 mRNA levels in healthy and inflamed gingivae nine days after ligature placement are shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). * P =0.05, ** P =0.006 for healthy vs . inflamed tissues in WT and MIF KO mice and ** P =0.01 for inflamed sites in WT vs . MIF KO animals. Grey bars: WT mice (n=6), white bars: MIF KO mice (n=6). Results are shown as mean values ±SD, each sample was run in duplicate. C: Levels of IL6 released from HGFs after stimulation with HC, MIF or F. nucleatum (* P ) was employed. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.

    Article Snippet: Increases in IL6 could also be observed in HGFs after stimulation with F. nucleatum (618.7 ± 220.2 pg/ml), compared with the negative control (115.7 ± 45.1 pg/ml) ( ).

    Techniques: In Vivo, In Vitro, Mouse Assay

    MIF protein release from HGFs. MIF release was inducible by hydrocortisol (HC), but not by TNF-α or F. nucleatum (* P ), were used as a positive control. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.

    Journal: European journal of oral sciences

    Article Title: Assessment of the involvement of the macrophage migration inhibitory factor (MIF)-glucocorticoid regulatory dyad in MMP2 expression during periodontitis

    doi: 10.1111/eos.12363

    Figure Lengend Snippet: MIF protein release from HGFs. MIF release was inducible by hydrocortisol (HC), but not by TNF-α or F. nucleatum (* P ), were used as a positive control. Results are shown as mean values ±SD and represent five different donors; each sample was run in triplicate.

    Article Snippet: Increases in IL6 could also be observed in HGFs after stimulation with F. nucleatum (618.7 ± 220.2 pg/ml), compared with the negative control (115.7 ± 45.1 pg/ml) ( ).

    Techniques: Positive Control

    MMP2 levels in murine gingival tissues and HGF supernatants. A : Mmp2 mRNA levels in WT and MIF KO mice in healthy and inflamed gingival sites shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). B: MMP2 release by HGFs from five different donors in cell culture experiments in response to hydrocortisol (HC), MIF and F. nucleatum (*** P =0.0003 compared to negative controls), each sample was run in triplicate wells.

    Journal: European journal of oral sciences

    Article Title: Assessment of the involvement of the macrophage migration inhibitory factor (MIF)-glucocorticoid regulatory dyad in MMP2 expression during periodontitis

    doi: 10.1111/eos.12363

    Figure Lengend Snippet: MMP2 levels in murine gingival tissues and HGF supernatants. A : Mmp2 mRNA levels in WT and MIF KO mice in healthy and inflamed gingival sites shown as relative expressions in relation to β-actin and as fold change (compared to healthy sites). B: MMP2 release by HGFs from five different donors in cell culture experiments in response to hydrocortisol (HC), MIF and F. nucleatum (*** P =0.0003 compared to negative controls), each sample was run in triplicate wells.

    Article Snippet: Increases in IL6 could also be observed in HGFs after stimulation with F. nucleatum (618.7 ± 220.2 pg/ml), compared with the negative control (115.7 ± 45.1 pg/ml) ( ).

    Techniques: Mouse Assay, Cell Culture