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  • 99
    ATCC p intermedia atcc 25611
    I. guayusa Loes and P. marginatum Jacq fraction antimicrobial activity against P. intermedia <t>ATCC</t> 25611 at three concentrations. (a) Antimicrobial activities (inhibitory halos mm) from I. guayusa Loes and P. marginatum Jacq fractions against P. intermedia. (b) 1: P. marginatum Jacq 4 mg/mL ethanol : water fraction, 12.3 mm inhibitory halo; 2: I. guayusa Loes 4 mg/mL acetone fraction, 12.0 mm inhibitory halo; 3: P. marginatum Jacq; 4 mg/mL acetone fraction, 11.3 mm inhibitory halo; 4: I. guayusa Loes 4 mg/mL hexane fraction, 13.3 mm inhibitory halo; 5: 50 IU/mL erythromycin positive control, 40 mm inhibitory halo.
    P Intermedia Atcc 25611, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 496 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    ATCC p intermedia atcc 49046
    Biovolumes of P. intermedia <t>ATCC</t> 49046 and P. gingivalis ATCC 33277 biofilms after 96 h of growth on different implant surfaces. Error bars represent standard deviations over three experiments with different discs of each material and separately cultured bacteria. *Significantly ( P
    P Intermedia Atcc 49046, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    ATCC p intermedia
    Biovolumes of P. intermedia <t>ATCC</t> 49046 and P. gingivalis ATCC 33277 biofilms after 96 h of growth on different implant surfaces. Error bars represent standard deviations over three experiments with different discs of each material and separately cultured bacteria. *Significantly ( P
    P Intermedia, supplied by ATCC, used in various techniques. Bioz Stars score: 89/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC p intermedia atcc 25611t
    Biovolumes of P. intermedia <t>ATCC</t> 49046 and P. gingivalis ATCC 33277 biofilms after 96 h of growth on different implant surfaces. Error bars represent standard deviations over three experiments with different discs of each material and separately cultured bacteria. *Significantly ( P
    P Intermedia Atcc 25611t, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Difco p intermedia cultures
    Biovolumes of P. intermedia <t>ATCC</t> 49046 and P. gingivalis ATCC 33277 biofilms after 96 h of growth on different implant surfaces. Error bars represent standard deviations over three experiments with different discs of each material and separately cultured bacteria. *Significantly ( P
    P Intermedia Cultures, supplied by Difco, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    ATCC p intermedia strains 25261
    Cleavage of 125 I-sCD14 and 125 I-lipopolysaccharide-binding protein (LBP) by various concentrations of Prevotella intermedia ATCC 25611 cell suspension ( a , b ). Cleavage of 125 I-sCD14 or 125 I-LBP by various concentrations of P. intermedia ATCC 25611 cell supernatant ( c ). SDS-PAGE (10% polyacrylamide) analysis of 125 I-sCD14 to show the purity of the sCD14 used in the experiments and its cleavage to less than 1-kDa fragments by P. intermedia strain 25611 enzyme; MW molecular mass ( d ). Zymographic analysis of the cleavage of 125 I-sCD14 by electrophoretically separated proteases from <t>strains</t> 25261 and 25611 and by the heat-inactivated proteases from both strains ( e ). Zymographic analysis of the cleavage of 125 I-LBP by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( f ). a All points represent mean and SEM of triplicate values; a–f one out of three separate experiments is shown
    P Intermedia Strains 25261, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    I. guayusa Loes and P. marginatum Jacq fraction antimicrobial activity against P. intermedia ATCC 25611 at three concentrations. (a) Antimicrobial activities (inhibitory halos mm) from I. guayusa Loes and P. marginatum Jacq fractions against P. intermedia. (b) 1: P. marginatum Jacq 4 mg/mL ethanol : water fraction, 12.3 mm inhibitory halo; 2: I. guayusa Loes 4 mg/mL acetone fraction, 12.0 mm inhibitory halo; 3: P. marginatum Jacq; 4 mg/mL acetone fraction, 11.3 mm inhibitory halo; 4: I. guayusa Loes 4 mg/mL hexane fraction, 13.3 mm inhibitory halo; 5: 50 IU/mL erythromycin positive control, 40 mm inhibitory halo.

    Journal: International Journal of Microbiology

    Article Title: Antimicrobial Activity of Piper marginatum Jacq and Ilex guayusa Loes on Microorganisms Associated with Periodontal Disease

    doi: 10.1155/2018/4147383

    Figure Lengend Snippet: I. guayusa Loes and P. marginatum Jacq fraction antimicrobial activity against P. intermedia ATCC 25611 at three concentrations. (a) Antimicrobial activities (inhibitory halos mm) from I. guayusa Loes and P. marginatum Jacq fractions against P. intermedia. (b) 1: P. marginatum Jacq 4 mg/mL ethanol : water fraction, 12.3 mm inhibitory halo; 2: I. guayusa Loes 4 mg/mL acetone fraction, 12.0 mm inhibitory halo; 3: P. marginatum Jacq; 4 mg/mL acetone fraction, 11.3 mm inhibitory halo; 4: I. guayusa Loes 4 mg/mL hexane fraction, 13.3 mm inhibitory halo; 5: 50 IU/mL erythromycin positive control, 40 mm inhibitory halo.

    Article Snippet: Piper marginatum Jacq total ethanol extract presented antimicrobial activity against all three bacteria, whereas Ilex guayusa Loes was only efficient against P. gingivalis ATCC 33277 and P. intermedia ATCC 25611, with inhibition halos from 9.3 to 30 mm.

    Techniques: Activity Assay, Positive Control

    Cleavage of 125 I-sCD14 and 125 I-lipopolysaccharide-binding protein (LBP) by various concentrations of Prevotella intermedia ATCC 25611 cell suspension ( a , b ). Cleavage of 125 I-sCD14 or 125 I-LBP by various concentrations of P. intermedia ATCC 25611 cell supernatant ( c ). SDS-PAGE (10% polyacrylamide) analysis of 125 I-sCD14 to show the purity of the sCD14 used in the experiments and its cleavage to less than 1-kDa fragments by P. intermedia strain 25611 enzyme; MW molecular mass ( d ). Zymographic analysis of the cleavage of 125 I-sCD14 by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( e ). Zymographic analysis of the cleavage of 125 I-LBP by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( f ). a All points represent mean and SEM of triplicate values; a–f one out of three separate experiments is shown

    Journal: Archives of microbiology

    Article Title: Cleavage of CD14 and LBP by a protease from Prevotella intermedia

    doi: 10.1007/s00203-003-0548-1

    Figure Lengend Snippet: Cleavage of 125 I-sCD14 and 125 I-lipopolysaccharide-binding protein (LBP) by various concentrations of Prevotella intermedia ATCC 25611 cell suspension ( a , b ). Cleavage of 125 I-sCD14 or 125 I-LBP by various concentrations of P. intermedia ATCC 25611 cell supernatant ( c ). SDS-PAGE (10% polyacrylamide) analysis of 125 I-sCD14 to show the purity of the sCD14 used in the experiments and its cleavage to less than 1-kDa fragments by P. intermedia strain 25611 enzyme; MW molecular mass ( d ). Zymographic analysis of the cleavage of 125 I-sCD14 by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( e ). Zymographic analysis of the cleavage of 125 I-LBP by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( f ). a All points represent mean and SEM of triplicate values; a–f one out of three separate experiments is shown

    Article Snippet: Incubation of 125 I-sCD14 or 125 I-LBP with suspensions of various numbers of P. intermedia ATCC 25611 cells resulted in a concentration-dependent cleavage of 125 I-sCD14 and 125 I-LBP, respectively ( ).

    Techniques: Binding Assay, SDS Page

    Effect of P. gingivalis administration on clinical features and serum levels of antibodies in a CIA model. ( A ) Representative image of the hind paw of sham-, P. gingivalis -, and P. intermedia -administered mice following CII immunisation. ( B ) Visual assessment score (VAS) of sham-, P. gingivalis -, and P. intermedia -administered mice. ( C ) Micro-computed tomographic appearance of the paws of sham-, P. gingivalis -, and P. intermedia -administered mice. ( D ) Histological analysis of the knee joints of sham-, P. gingivalis -, and P. intermedia -administered mice. Sections were stained with haematoxylin and eosin, and tartrate-resistant acid phosphatase in combination with haematoxylin. Serum levels of anti-CII antibodies ( E ), anti-cyclic citrullinated protein (CCP) antibodies ( F ), and IgG antibodies against P. gingivalis W83 and P. intermedia ATCC 25611 ( G ) were compared between sham-, P. gingivalis -, and P. intermedia -administered mice. Sera were obtained immediately before immunisation (day 35) and after induction of CIA (day 77). Data represent the mean ± standard error of the mean (SEM) (N = 6 for ( A , B , E , F and G ). *p

    Journal: Scientific Reports

    Article Title: Aggravation of collagen-induced arthritis by orally administered Porphyromonas gingivalis through modulation of the gut microbiota and gut immune system

    doi: 10.1038/s41598-017-07196-7

    Figure Lengend Snippet: Effect of P. gingivalis administration on clinical features and serum levels of antibodies in a CIA model. ( A ) Representative image of the hind paw of sham-, P. gingivalis -, and P. intermedia -administered mice following CII immunisation. ( B ) Visual assessment score (VAS) of sham-, P. gingivalis -, and P. intermedia -administered mice. ( C ) Micro-computed tomographic appearance of the paws of sham-, P. gingivalis -, and P. intermedia -administered mice. ( D ) Histological analysis of the knee joints of sham-, P. gingivalis -, and P. intermedia -administered mice. Sections were stained with haematoxylin and eosin, and tartrate-resistant acid phosphatase in combination with haematoxylin. Serum levels of anti-CII antibodies ( E ), anti-cyclic citrullinated protein (CCP) antibodies ( F ), and IgG antibodies against P. gingivalis W83 and P. intermedia ATCC 25611 ( G ) were compared between sham-, P. gingivalis -, and P. intermedia -administered mice. Sera were obtained immediately before immunisation (day 35) and after induction of CIA (day 77). Data represent the mean ± standard error of the mean (SEM) (N = 6 for ( A , B , E , F and G ). *p

    Article Snippet: Bacterial infection P. gingivalis strain W83 and P. intermedia strain ATCC 25611 maintained in our laboratory were used in the present study.

    Techniques: Mouse Assay, Staining

    C4BP and FH bound to P. intermedia ATCC 25611 retain their cofactor activity. P. intermedia ATCC 25611 was incubated for 30 min at 56°C and subsequently incubated with C4BP (5–15 µg) (final concentration 125 ng/µl (0.22 µM), 250 ng/µl (0.44 µM) and 375 ng/µl (0.66 µM)) (A) and B)) or FH (1–5 µg) (final concentration 0.025 µg/µl (0.16 µM), 0.05 µg/µl (0.32 µM), 0.125 µg/µl (0.8 µM)) (D) and E)) for 1 h at RT. Samples without C4BP and FH were used as a reference. Bacteria were washed and transferred to fresh reaction tubes. A) and B) Bacteria were mixed with E-64, C4met, FI and trace amounts of 125 I-C4b. Samples were incubated for 1.5 h at 37°C, centrifuged and proteins separated on a 10–15% SDS-PAGE gradient gel under reducing conditions. Samples without bacteria, which contained C4BP but no FI served as negative controls. Samples supplemented with C4BP and FI were positive controls in this experimental setup. B) and E) Protein bands were quantified using the Image Gauge Software. C) and F) P. intermedia ATCC 25611 was incubated at 56°C for 30 min and binding assays were performed as described earlier with 125 I-labeled protein. D) and E) Bacterial suspensions were mixed with E-64, C3met, FI and trace amounts of 125 I-C3b. Samples were incubated for 1.5 h at 37°C and separated as described above. A negative control without bacteria was included, in which FI was omitted. A positive control without bacteria supplemented with FH and FI was prepared. All experiments were performed in triplicates, the mean values and SD were calculated. One-way ANOVA and Tukey's post-hoc test were used for statistical analysis on bacteria containing samples. Degradation mediated by cofactors bound to P. intermedia was evaluated by comparing the ratios of C4d or α′43 degradation products to α-chains of samples where protein was omitted during preincubation (*** p≤0.001; ** p

    Journal: PLoS ONE

    Article Title: Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

    doi: 10.1371/journal.pone.0034852

    Figure Lengend Snippet: C4BP and FH bound to P. intermedia ATCC 25611 retain their cofactor activity. P. intermedia ATCC 25611 was incubated for 30 min at 56°C and subsequently incubated with C4BP (5–15 µg) (final concentration 125 ng/µl (0.22 µM), 250 ng/µl (0.44 µM) and 375 ng/µl (0.66 µM)) (A) and B)) or FH (1–5 µg) (final concentration 0.025 µg/µl (0.16 µM), 0.05 µg/µl (0.32 µM), 0.125 µg/µl (0.8 µM)) (D) and E)) for 1 h at RT. Samples without C4BP and FH were used as a reference. Bacteria were washed and transferred to fresh reaction tubes. A) and B) Bacteria were mixed with E-64, C4met, FI and trace amounts of 125 I-C4b. Samples were incubated for 1.5 h at 37°C, centrifuged and proteins separated on a 10–15% SDS-PAGE gradient gel under reducing conditions. Samples without bacteria, which contained C4BP but no FI served as negative controls. Samples supplemented with C4BP and FI were positive controls in this experimental setup. B) and E) Protein bands were quantified using the Image Gauge Software. C) and F) P. intermedia ATCC 25611 was incubated at 56°C for 30 min and binding assays were performed as described earlier with 125 I-labeled protein. D) and E) Bacterial suspensions were mixed with E-64, C3met, FI and trace amounts of 125 I-C3b. Samples were incubated for 1.5 h at 37°C and separated as described above. A negative control without bacteria was included, in which FI was omitted. A positive control without bacteria supplemented with FH and FI was prepared. All experiments were performed in triplicates, the mean values and SD were calculated. One-way ANOVA and Tukey's post-hoc test were used for statistical analysis on bacteria containing samples. Degradation mediated by cofactors bound to P. intermedia was evaluated by comparing the ratios of C4d or α′43 degradation products to α-chains of samples where protein was omitted during preincubation (*** p≤0.001; ** p

    Article Snippet: Therefore, in order to minimize background degradation by P. intermedia ATCC 25611 aliquots (20 µl, approximately 2×109 bacteria) of the bacterial suspensions were incubated for 30 min at 56°C besides adding 2 mM E-64 (Sigma-Aldrich, St. Louis, MO) together with the substrates C3 or C4 later when preparing samples for the degradation reaction.

    Techniques: Activity Assay, Incubation, Concentration Assay, SDS Page, Software, Binding Assay, Labeling, Negative Control, Positive Control

    Specificity and sensitivity of C4BP and FH binding by P. intermedia ATCC 25611. A) Binding of 250 kcpm 125 I-C4BP was competed by using 30 µg (final concentration 1.32 µM) unlabeled C4BP, C) 125 I-FH binding by P. intermedia ATCC 25611 was competed by 7.5 µg (final concentration 1.25 µM) unlabeled FH. The decrease of 125 I-C4BP and 125 I-FH binding was evaluated comparing the results of samples with and without radiolabeled protein and bacteria. Samples without bacteria served as negative controls. The sensitivity of the interaction to ionic strength was tested adding increasing concentrations of NaCl to binding reactions with B) 125 I-C4BP and D) 125 I-FH. Three independent experiments were performed in duplicates; averages and SD were calculated and binding expressed as protein bound relative to protein bound without addition of competitor. One-way ANOVA followed by Tukey's post-hoc test was applied for statistical evaluation of the data (** p

    Journal: PLoS ONE

    Article Title: Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

    doi: 10.1371/journal.pone.0034852

    Figure Lengend Snippet: Specificity and sensitivity of C4BP and FH binding by P. intermedia ATCC 25611. A) Binding of 250 kcpm 125 I-C4BP was competed by using 30 µg (final concentration 1.32 µM) unlabeled C4BP, C) 125 I-FH binding by P. intermedia ATCC 25611 was competed by 7.5 µg (final concentration 1.25 µM) unlabeled FH. The decrease of 125 I-C4BP and 125 I-FH binding was evaluated comparing the results of samples with and without radiolabeled protein and bacteria. Samples without bacteria served as negative controls. The sensitivity of the interaction to ionic strength was tested adding increasing concentrations of NaCl to binding reactions with B) 125 I-C4BP and D) 125 I-FH. Three independent experiments were performed in duplicates; averages and SD were calculated and binding expressed as protein bound relative to protein bound without addition of competitor. One-way ANOVA followed by Tukey's post-hoc test was applied for statistical evaluation of the data (** p

    Article Snippet: Therefore, in order to minimize background degradation by P. intermedia ATCC 25611 aliquots (20 µl, approximately 2×109 bacteria) of the bacterial suspensions were incubated for 30 min at 56°C besides adding 2 mM E-64 (Sigma-Aldrich, St. Louis, MO) together with the substrates C3 or C4 later when preparing samples for the degradation reaction.

    Techniques: Binding Assay, Concentration Assay

    Degradation of 125 I-C4b by FI bound to P. intermedia . A) P. intermedia ATCC 25611 was incubated at 56°C for 30 min and subsequently 5 µg, 10 µg, and 15 µg FI (final concentration 125 ng/µl (1.42 µM), 250 ng/µl (2.84 µM) and 375 ng/µl (4.26 µM)) were added to the bacterial suspension and samples incubated for 1 h at RT. Thereafter, bacteria were washed and mixed with E-64, C4met, C4BP and 125 I-C4b. Samples were incubated for 4 h at 37°C, centrifuged to remove bacteria followed by separation of proteins on a 10–15% SDS-PAGE gradient gel under reducing conditions. Gels were dried and 125 I-C4b was detected using a phosphorimager. Controls were samples only containing purified proteins without bacteria; either FI and C4BP (positive control) or only FI without cofactor (negative control) were added to degradation reactions. B) Data were quantified using the Image Gauge Software. Averages of four independent experiments are shown, error bars denoting the SD. The ratio of C4d/α-chain was calculated and data from samples containing FI bound to bacteria compared to the control containing bacteria without FI using one-way ANOVA followed by Tukey's post-hoc test applied to samples containing bacteria (*** p

    Journal: PLoS ONE

    Article Title: Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

    doi: 10.1371/journal.pone.0034852

    Figure Lengend Snippet: Degradation of 125 I-C4b by FI bound to P. intermedia . A) P. intermedia ATCC 25611 was incubated at 56°C for 30 min and subsequently 5 µg, 10 µg, and 15 µg FI (final concentration 125 ng/µl (1.42 µM), 250 ng/µl (2.84 µM) and 375 ng/µl (4.26 µM)) were added to the bacterial suspension and samples incubated for 1 h at RT. Thereafter, bacteria were washed and mixed with E-64, C4met, C4BP and 125 I-C4b. Samples were incubated for 4 h at 37°C, centrifuged to remove bacteria followed by separation of proteins on a 10–15% SDS-PAGE gradient gel under reducing conditions. Gels were dried and 125 I-C4b was detected using a phosphorimager. Controls were samples only containing purified proteins without bacteria; either FI and C4BP (positive control) or only FI without cofactor (negative control) were added to degradation reactions. B) Data were quantified using the Image Gauge Software. Averages of four independent experiments are shown, error bars denoting the SD. The ratio of C4d/α-chain was calculated and data from samples containing FI bound to bacteria compared to the control containing bacteria without FI using one-way ANOVA followed by Tukey's post-hoc test applied to samples containing bacteria (*** p

    Article Snippet: Therefore, in order to minimize background degradation by P. intermedia ATCC 25611 aliquots (20 µl, approximately 2×109 bacteria) of the bacterial suspensions were incubated for 30 min at 56°C besides adding 2 mM E-64 (Sigma-Aldrich, St. Louis, MO) together with the substrates C3 or C4 later when preparing samples for the degradation reaction.

    Techniques: Incubation, Concentration Assay, SDS Page, Purification, Positive Control, Negative Control, Software

    P. intermedia  strains bind purified  125 I-FI and FI from HI-NHS. A)  P. intermedia  ATCC 25611, OMZ 248, OMZ 324, MH6,  S. aureus  strains ATCC 25923 and Newman (FI binding positive control) as well as  E. coli  DH5α (FI binding negative control) were incubated with  125 I-FI (250 kcpm). Bound and free FI were separated by centrifugation through sucrose, the radioactivity associated with pellets and supernatants was measured in a gamma counter and the percentage of radioactivity bound to the pellet was calculated. Samples containing  125 I-labeled FI that was incubated with buffer alone served as a negative control. Averages of three independent experiments performed in duplicates are shown; error bars show SD. One-way ANOVA followed by Tukey's post-hoc test was used for statistical evaluation of the data as compared to the negative control (*** p

    Journal: PLoS ONE

    Article Title: Acquisition of Complement Inhibitor Serine Protease Factor I and Its Cofactors C4b-Binding Protein and Factor H by Prevotella intermedia

    doi: 10.1371/journal.pone.0034852

    Figure Lengend Snippet: P. intermedia strains bind purified 125 I-FI and FI from HI-NHS. A) P. intermedia ATCC 25611, OMZ 248, OMZ 324, MH6, S. aureus strains ATCC 25923 and Newman (FI binding positive control) as well as E. coli DH5α (FI binding negative control) were incubated with 125 I-FI (250 kcpm). Bound and free FI were separated by centrifugation through sucrose, the radioactivity associated with pellets and supernatants was measured in a gamma counter and the percentage of radioactivity bound to the pellet was calculated. Samples containing 125 I-labeled FI that was incubated with buffer alone served as a negative control. Averages of three independent experiments performed in duplicates are shown; error bars show SD. One-way ANOVA followed by Tukey's post-hoc test was used for statistical evaluation of the data as compared to the negative control (*** p

    Article Snippet: Therefore, in order to minimize background degradation by P. intermedia ATCC 25611 aliquots (20 µl, approximately 2×109 bacteria) of the bacterial suspensions were incubated for 30 min at 56°C besides adding 2 mM E-64 (Sigma-Aldrich, St. Louis, MO) together with the substrates C3 or C4 later when preparing samples for the degradation reaction.

    Techniques: Purification, Binding Assay, Positive Control, Negative Control, Incubation, Centrifugation, Radioactivity, Labeling

    Biovolumes of P. intermedia ATCC 49046 and P. gingivalis ATCC 33277 biofilms after 96 h of growth on different implant surfaces. Error bars represent standard deviations over three experiments with different discs of each material and separately cultured bacteria. *Significantly ( P

    Journal: International Journal of Oral Science

    Article Title: Osteoblast integration of dental implant materials after challenge by sub-gingival pathogens: a co-culture study in vitro

    doi: 10.1038/ijos.2015.45

    Figure Lengend Snippet: Biovolumes of P. intermedia ATCC 49046 and P. gingivalis ATCC 33277 biofilms after 96 h of growth on different implant surfaces. Error bars represent standard deviations over three experiments with different discs of each material and separately cultured bacteria. *Significantly ( P

    Article Snippet: U2OS cells did not demonstrate any morphological change in response to a bacterial challenge at 104 mL–1 for either P. intermedia ATCC 49046 or P. gingivalis ATCC 33277, but at 106 mL–1 near complete cellular detachment was observed after challenge with P. intermedia ATCC 49046 ( ).

    Techniques: Cell Culture

    Battles occurring on the osseointegratable part of a dental implant between an existing layer of adhering U2OS osteoblasts and challenging periodontopathogens (left panel) and on the neck of an implant between gingival fibroblasts and contaminating oral bacteria adhering to the implant surface (right panel). Left panel: a comparison of the surface coverage by U2OS cells on dental implant materials grown prior to (coloured bars) and after (black bars) of a challenge by sub-gingival, oral bacterial strains. Data represent averages over P. intermedia ATCC 49046 and P. gingivalis ATCC 33277. On TiZr alloys and ZrO 2 variants, adhering osteoblasts withstand a challenge by sub-gingival bacteria more effectively than on Ti variants, regardless of surface roughness (green coloured, well-spread cell versus red cell), making TiZr alloys and ZrO 2 variants most suitable for the osseointegratable part of an implant. Right panel: a comparison of the surface coverage by human gingival fibroblasts on dental implant materials grown in absence (coloured bars) and presence (black bars) of contamination by adhering supra-gingival, oral bacteria ( Streptococcus oralis J22, Streptococcus mitis BMS, Streptococcus salivarius HB and Staphylococcus aureus ATCC 25923). Data represent averages over the four strains indicated (data taken with permission from Zhao et al. 11 ). Displacement of contaminating supra-gingival bacteria from smooth Ti variants (green coloured, well-spread cell versus red, rounded-up cell) is easier than from the other implant materials included in this study, making smooth Ti variants most suitable for the neck of an implant. #These materials on average perform better than the other materials with respect to a bacterial challenge of an existing cellular layer or integration of a material in the presence of contaminating bacteria.

    Journal: International Journal of Oral Science

    Article Title: Osteoblast integration of dental implant materials after challenge by sub-gingival pathogens: a co-culture study in vitro

    doi: 10.1038/ijos.2015.45

    Figure Lengend Snippet: Battles occurring on the osseointegratable part of a dental implant between an existing layer of adhering U2OS osteoblasts and challenging periodontopathogens (left panel) and on the neck of an implant between gingival fibroblasts and contaminating oral bacteria adhering to the implant surface (right panel). Left panel: a comparison of the surface coverage by U2OS cells on dental implant materials grown prior to (coloured bars) and after (black bars) of a challenge by sub-gingival, oral bacterial strains. Data represent averages over P. intermedia ATCC 49046 and P. gingivalis ATCC 33277. On TiZr alloys and ZrO 2 variants, adhering osteoblasts withstand a challenge by sub-gingival bacteria more effectively than on Ti variants, regardless of surface roughness (green coloured, well-spread cell versus red cell), making TiZr alloys and ZrO 2 variants most suitable for the osseointegratable part of an implant. Right panel: a comparison of the surface coverage by human gingival fibroblasts on dental implant materials grown in absence (coloured bars) and presence (black bars) of contamination by adhering supra-gingival, oral bacteria ( Streptococcus oralis J22, Streptococcus mitis BMS, Streptococcus salivarius HB and Staphylococcus aureus ATCC 25923). Data represent averages over the four strains indicated (data taken with permission from Zhao et al. 11 ). Displacement of contaminating supra-gingival bacteria from smooth Ti variants (green coloured, well-spread cell versus red, rounded-up cell) is easier than from the other implant materials included in this study, making smooth Ti variants most suitable for the neck of an implant. #These materials on average perform better than the other materials with respect to a bacterial challenge of an existing cellular layer or integration of a material in the presence of contaminating bacteria.

    Article Snippet: U2OS cells did not demonstrate any morphological change in response to a bacterial challenge at 104 mL–1 for either P. intermedia ATCC 49046 or P. gingivalis ATCC 33277, but at 106 mL–1 near complete cellular detachment was observed after challenge with P. intermedia ATCC 49046 ( ).

    Techniques:

    Phase-contrast micrographs of U2OS osteoblasts challenged with different concentrations of sub-gingival pathogens. U2OS osteoblasts initially grown in 100% DMEM/LG-complete at 37 °C in a 5% CO 2 atmosphere for 24 h in tissue culture polystyrene wells, and after pursued further anaerobic growth for 48 h in modified culture medium in absence and presence of different concentrations of P. intermedia ATCC 49046 or P. gingivalis ATCC 33277. ( a, b ) No bacteria; ( c, d ) ×10 4 mL −1 bacteria; ( e, f ) ×10 6 mL −1 bacteria. Bar markers indicate 25 μm. DMEM/LG, Dulbecco's modified Eagle's medium low glucose.

    Journal: International Journal of Oral Science

    Article Title: Osteoblast integration of dental implant materials after challenge by sub-gingival pathogens: a co-culture study in vitro

    doi: 10.1038/ijos.2015.45

    Figure Lengend Snippet: Phase-contrast micrographs of U2OS osteoblasts challenged with different concentrations of sub-gingival pathogens. U2OS osteoblasts initially grown in 100% DMEM/LG-complete at 37 °C in a 5% CO 2 atmosphere for 24 h in tissue culture polystyrene wells, and after pursued further anaerobic growth for 48 h in modified culture medium in absence and presence of different concentrations of P. intermedia ATCC 49046 or P. gingivalis ATCC 33277. ( a, b ) No bacteria; ( c, d ) ×10 4 mL −1 bacteria; ( e, f ) ×10 6 mL −1 bacteria. Bar markers indicate 25 μm. DMEM/LG, Dulbecco's modified Eagle's medium low glucose.

    Article Snippet: U2OS cells did not demonstrate any morphological change in response to a bacterial challenge at 104 mL–1 for either P. intermedia ATCC 49046 or P. gingivalis ATCC 33277, but at 106 mL–1 near complete cellular detachment was observed after challenge with P. intermedia ATCC 49046 ( ).

    Techniques: Modification

    Effect of polyP3 on viability of preformed P. intermedia biofilm. Preestablished biofilms of P. intermedia ATCC 49046 were treated with polyP3 at the indicated concentrations for 24 h. (A) Biofilm biomass was quantitated by crystal violet staining. The

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: In Vitro Effects of Polyphosphate against Prevotella intermedia in Planktonic Phase and Biofilm

    doi: 10.1128/AAC.01861-15

    Figure Lengend Snippet: Effect of polyP3 on viability of preformed P. intermedia biofilm. Preestablished biofilms of P. intermedia ATCC 49046 were treated with polyP3 at the indicated concentrations for 24 h. (A) Biofilm biomass was quantitated by crystal violet staining. The

    Article Snippet: By the agar dilution method, the MIC of polyP3 against P. intermedia ATCC 49046 was determined to be 0.075% ( ).

    Techniques: Staining

    Effect of polyP3 on beta-hemolysis produced by P. intermedia ATCC 49046. Various concentrations of polyP3 were prepared and added to 5% horse blood BHIA in the absence of hemin and vitamin K 1 . P. intermedia was incubated on the agar plates for 5 days

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: In Vitro Effects of Polyphosphate against Prevotella intermedia in Planktonic Phase and Biofilm

    doi: 10.1128/AAC.01861-15

    Figure Lengend Snippet: Effect of polyP3 on beta-hemolysis produced by P. intermedia ATCC 49046. Various concentrations of polyP3 were prepared and added to 5% horse blood BHIA in the absence of hemin and vitamin K 1 . P. intermedia was incubated on the agar plates for 5 days

    Article Snippet: By the agar dilution method, the MIC of polyP3 against P. intermedia ATCC 49046 was determined to be 0.075% ( ).

    Techniques: Produced, Incubation

    Antibacterial effect of polyP3 against P. intermedia ATCC 4906. (A) MIC determination of polyP3 by agar dilution method. The bacterial cells were spot inoculated (approximately 10 5 to 10 6 cells/spot) onto brucella blood agar plates containing polyP3 at

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: In Vitro Effects of Polyphosphate against Prevotella intermedia in Planktonic Phase and Biofilm

    doi: 10.1128/AAC.01861-15

    Figure Lengend Snippet: Antibacterial effect of polyP3 against P. intermedia ATCC 4906. (A) MIC determination of polyP3 by agar dilution method. The bacterial cells were spot inoculated (approximately 10 5 to 10 6 cells/spot) onto brucella blood agar plates containing polyP3 at

    Article Snippet: By the agar dilution method, the MIC of polyP3 against P. intermedia ATCC 49046 was determined to be 0.075% ( ).

    Techniques:

    Cleavage of 125 I-sCD14 and 125 I-lipopolysaccharide-binding protein (LBP) by various concentrations of Prevotella intermedia ATCC 25611 cell suspension ( a , b ). Cleavage of 125 I-sCD14 or 125 I-LBP by various concentrations of P. intermedia ATCC 25611 cell supernatant ( c ). SDS-PAGE (10% polyacrylamide) analysis of 125 I-sCD14 to show the purity of the sCD14 used in the experiments and its cleavage to less than 1-kDa fragments by P. intermedia strain 25611 enzyme; MW molecular mass ( d ). Zymographic analysis of the cleavage of 125 I-sCD14 by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( e ). Zymographic analysis of the cleavage of 125 I-LBP by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( f ). a All points represent mean and SEM of triplicate values; a–f one out of three separate experiments is shown

    Journal: Archives of microbiology

    Article Title: Cleavage of CD14 and LBP by a protease from Prevotella intermedia

    doi: 10.1007/s00203-003-0548-1

    Figure Lengend Snippet: Cleavage of 125 I-sCD14 and 125 I-lipopolysaccharide-binding protein (LBP) by various concentrations of Prevotella intermedia ATCC 25611 cell suspension ( a , b ). Cleavage of 125 I-sCD14 or 125 I-LBP by various concentrations of P. intermedia ATCC 25611 cell supernatant ( c ). SDS-PAGE (10% polyacrylamide) analysis of 125 I-sCD14 to show the purity of the sCD14 used in the experiments and its cleavage to less than 1-kDa fragments by P. intermedia strain 25611 enzyme; MW molecular mass ( d ). Zymographic analysis of the cleavage of 125 I-sCD14 by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( e ). Zymographic analysis of the cleavage of 125 I-LBP by electrophoretically separated proteases from strains 25261 and 25611 and by the heat-inactivated proteases from both strains ( f ). a All points represent mean and SEM of triplicate values; a–f one out of three separate experiments is shown

    Article Snippet: The remaining reagents were purchased as follows: minimal essential medium (MEM) and phosphate-buffered saline (PBS) from Life Technologies (Grand Island, N.Y., USA), P. intermedia strains 25261 and 25611 from ATCC (Rockville, Md., USA), media for P. intermedia cultures from Difco Laboratories (Detroit, Mich., USA), Mono-Q and Superose-12 columns from Pharmacia Biotech Products (Piscataway, N.J., USA), reagents for polyacrylamide gel electrophoresis (PAGE) from Biorad Laboratories (Richmond, Calif., USA), limulus amoebocyte lysate assay kit from Bio Whittaker (Walkersville, Md., USA), radioiodine from New England Nuclear, (Boston, Mass., USA), Iodogen from Pierce (Rockford, Ill., USA), and all other reagents from Sigma (St. Louis, Mo., USA).

    Techniques: Binding Assay, SDS Page