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  • 99
    ATCC f nucleatum atcc 25586
    Effects of exogenous indole on planktonic and biofilm cells of F. <t>nucleatum</t> ATCC 25586. (A) Relative amounts of planktonic and biofilm cells grown in the absence or presence of exogenous indole are shown. Bacteria were incubated for 48 h in 96-well PVC
    F Nucleatum Atcc 25586, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 695 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC f nucleatum atcc 23726
    Biofilm formation on DBR disc surfaces. Representative images after crystal violet staining of biofilms formed on DBR discs by F. <t>nucleatum</t> <t>ATCC</t> 23726 (A) T. forsythia ATCC 43037 (B) V. atypica PK 1910 (C) K. pneumoniae IA 565 (D) For each set, the image on the left was a control DBR disc without biofilms growing on the surface, the image on the right was a DBR disc with biofilms growing on the surface. The experiment was performed in triplicate.
    F Nucleatum Atcc 23726, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 387 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    ATCC f nucleatum atcc 10953
    The effect of the environmental conditions on the activity of H 2 S-producing enzymes was tested for Fusobacterium <t>nucleatum</t> polymorphum ATCC 10953. The bacteria were grown in different broths before protein extraction and 1D gel electrophoresis followed by in-gel activity assay
    F Nucleatum Atcc 10953, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 244 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC f nucleatum atcc 49256
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    F Nucleatum Atcc 49256, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    ATCC f nucleatum atcc 25286
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    F Nucleatum Atcc 25286, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    ATCC f nucleatum atcc 10596
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    F Nucleatum Atcc 10596, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC f nucleatum atcc 23276 competent cells
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    F Nucleatum Atcc 23276 Competent Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    ATCC f nucleatum atcc 23727 attachment
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    F Nucleatum Atcc 23727 Attachment, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effects of exogenous indole on planktonic and biofilm cells of F. nucleatum ATCC 25586. (A) Relative amounts of planktonic and biofilm cells grown in the absence or presence of exogenous indole are shown. Bacteria were incubated for 48 h in 96-well PVC

    Journal: Applied and Environmental Microbiology

    Article Title: Production of Indole from l-Tryptophan and Effects of These Compounds on Biofilm Formation by Fusobacterium nucleatum ATCC 25586 ▿

    doi: 10.1128/AEM.00166-10

    Figure Lengend Snippet: Effects of exogenous indole on planktonic and biofilm cells of F. nucleatum ATCC 25586. (A) Relative amounts of planktonic and biofilm cells grown in the absence or presence of exogenous indole are shown. Bacteria were incubated for 48 h in 96-well PVC

    Article Snippet: However, the transcription start site of the tna operon in F. nucleatum ATCC 25586 was 67 or 152 bp upstream from the initiation codon of tnaA (Fig. ), revealing that the region corresponding to tnaL in F. nucleatum was much shorter than that in E. coli.

    Techniques: Incubation

    Characterization of purified protein encoded by fn1943 of F. nucleatum ATCC 25586. (A) SDS-PAGE analysis of recombinant Fn1943 of F. nucleatum ATCC 25586. Proteins were purified by affinity chromatography on glutathione-Sepharose 4B resin and digested

    Journal: Applied and Environmental Microbiology

    Article Title: Production of Indole from l-Tryptophan and Effects of These Compounds on Biofilm Formation by Fusobacterium nucleatum ATCC 25586 ▿

    doi: 10.1128/AEM.00166-10

    Figure Lengend Snippet: Characterization of purified protein encoded by fn1943 of F. nucleatum ATCC 25586. (A) SDS-PAGE analysis of recombinant Fn1943 of F. nucleatum ATCC 25586. Proteins were purified by affinity chromatography on glutathione-Sepharose 4B resin and digested

    Article Snippet: However, the transcription start site of the tna operon in F. nucleatum ATCC 25586 was 67 or 152 bp upstream from the initiation codon of tnaA (Fig. ), revealing that the region corresponding to tnaL in F. nucleatum was much shorter than that in E. coli.

    Techniques: Purification, SDS Page, Recombinant, Affinity Chromatography

    Genetic organization and transcriptional analyses of the tnaA region of F. nucleatum ATCC 25586. (A) Gene arrangements of the tnaA region in F. nucleatum ATCC 25586, E. coli K-12, and P. gingivalis W83. The DNA sequence of each region was obtained from

    Journal: Applied and Environmental Microbiology

    Article Title: Production of Indole from l-Tryptophan and Effects of These Compounds on Biofilm Formation by Fusobacterium nucleatum ATCC 25586 ▿

    doi: 10.1128/AEM.00166-10

    Figure Lengend Snippet: Genetic organization and transcriptional analyses of the tnaA region of F. nucleatum ATCC 25586. (A) Gene arrangements of the tnaA region in F. nucleatum ATCC 25586, E. coli K-12, and P. gingivalis W83. The DNA sequence of each region was obtained from

    Article Snippet: However, the transcription start site of the tna operon in F. nucleatum ATCC 25586 was 67 or 152 bp upstream from the initiation codon of tnaA (Fig. ), revealing that the region corresponding to tnaL in F. nucleatum was much shorter than that in E. coli.

    Techniques: Sequencing

    Expression levels of tnaA in several cell growth phases of F. nucleatum ATCC 25586. The OD 595 of cells incubated for 4, 8, 12, or 24 h for RNA extraction is indicated as an inset. The amounts of tnaA cDNA in each sample were analyzed by real-time quantitative

    Journal: Applied and Environmental Microbiology

    Article Title: Production of Indole from l-Tryptophan and Effects of These Compounds on Biofilm Formation by Fusobacterium nucleatum ATCC 25586 ▿

    doi: 10.1128/AEM.00166-10

    Figure Lengend Snippet: Expression levels of tnaA in several cell growth phases of F. nucleatum ATCC 25586. The OD 595 of cells incubated for 4, 8, 12, or 24 h for RNA extraction is indicated as an inset. The amounts of tnaA cDNA in each sample were analyzed by real-time quantitative

    Article Snippet: However, the transcription start site of the tna operon in F. nucleatum ATCC 25586 was 67 or 152 bp upstream from the initiation codon of tnaA (Fig. ), revealing that the region corresponding to tnaL in F. nucleatum was much shorter than that in E. coli.

    Techniques: Expressing, Incubation, RNA Extraction

    Effects of tryptophan on indole production and biofilm formation by F. nucleatum ATCC 25586. (A) Indole production by F. nucleatum ATCC 25586 cells grown in the absence or presence of tryptophan; (B) relative amounts of planktonic and biofilm cells grown

    Journal: Applied and Environmental Microbiology

    Article Title: Production of Indole from l-Tryptophan and Effects of These Compounds on Biofilm Formation by Fusobacterium nucleatum ATCC 25586 ▿

    doi: 10.1128/AEM.00166-10

    Figure Lengend Snippet: Effects of tryptophan on indole production and biofilm formation by F. nucleatum ATCC 25586. (A) Indole production by F. nucleatum ATCC 25586 cells grown in the absence or presence of tryptophan; (B) relative amounts of planktonic and biofilm cells grown

    Article Snippet: However, the transcription start site of the tna operon in F. nucleatum ATCC 25586 was 67 or 152 bp upstream from the initiation codon of tnaA (Fig. ), revealing that the region corresponding to tnaL in F. nucleatum was much shorter than that in E. coli.

    Techniques:

    (A) Western immunoblot of FAD-I protein in whole-cell lysates of F. nucleatum ATCC 25586, ATCC 23726, ATCC 10953, ATCC 10953 Δ fadI , and ATCC 10953 Δ fadI /pFAD-I 23726 (ATCC 10953 Δ fadI with plasmid-based expression of FAD-I from

    Journal: Infection and Immunity

    Article Title: FAD-I, a Fusobacterium nucleatum Cell Wall-Associated Diacylated Lipoprotein That Mediates Human Beta Defensin 2 Induction through Toll-Like Receptor-1/2 (TLR-1/2) and TLR-2/6

    doi: 10.1128/IAI.01311-15

    Figure Lengend Snippet: (A) Western immunoblot of FAD-I protein in whole-cell lysates of F. nucleatum ATCC 25586, ATCC 23726, ATCC 10953, ATCC 10953 Δ fadI , and ATCC 10953 Δ fadI /pFAD-I 23726 (ATCC 10953 Δ fadI with plasmid-based expression of FAD-I from

    Article Snippet: The full-length FAD-I gene (FN1527) ( ) was amplified by PCR from genomic DNA of F. nucleatum strain ATCC 25586 using primers (see Table S2 in the supplemental material) with Nde1 and Xho1 restriction sites at their ends (New England BioLabs).

    Techniques: Western Blot, Plasmid Preparation, Expressing

    Induction of hBD-2 mRNA by live bacterial cells (A) and cell wall preparations (10 μg/ml cell wall F. nucleatum [Fn] ATCC 25586, ATCC 23726, and ATCC 10953 (B). The data presented are means ± standard deviations (SD) of the results of

    Journal: Infection and Immunity

    Article Title: FAD-I, a Fusobacterium nucleatum Cell Wall-Associated Diacylated Lipoprotein That Mediates Human Beta Defensin 2 Induction through Toll-Like Receptor-1/2 (TLR-1/2) and TLR-2/6

    doi: 10.1128/IAI.01311-15

    Figure Lengend Snippet: Induction of hBD-2 mRNA by live bacterial cells (A) and cell wall preparations (10 μg/ml cell wall F. nucleatum [Fn] ATCC 25586, ATCC 23726, and ATCC 10953 (B). The data presented are means ± standard deviations (SD) of the results of

    Article Snippet: The full-length FAD-I gene (FN1527) ( ) was amplified by PCR from genomic DNA of F. nucleatum strain ATCC 25586 using primers (see Table S2 in the supplemental material) with Nde1 and Xho1 restriction sites at their ends (New England BioLabs).

    Techniques:

    Effect of DNase I and proteinase K on the biofilm formation (time zero) and on 48-h-old biofilm. Fusobacterium nucleatum type strain ATCC 25586 (F.n) and Porphyromonas gingivalis type strain ATCC 33277 (P.g 33277) bacterial species were tested when they were grown as monoculture or as dual species culture. (A) DNase I effect on biofilm formation, (B) DNase I effect on 48-h biofilm, (C) Proteinase K effect on biofilm formation, (D) Proteinase K effect on 48-h biofilm. The colored columns refer to the enzyme concentrations (0.125, 0.25, 0.5, and 1 mg/ml). The y-axis represents absorbance at 570 nm. The bars represent the means with standard deviations for 3–5 samples.

    Journal: Journal of Oral Microbiology

    Article Title: Characterization of extracellular polymeric matrix, and treatment of Fusobacterium nucleatum and Porphyromonas gingivalis biofilms with DNase I and proteinase K

    doi: 10.3402/jom.v5i0.20015

    Figure Lengend Snippet: Effect of DNase I and proteinase K on the biofilm formation (time zero) and on 48-h-old biofilm. Fusobacterium nucleatum type strain ATCC 25586 (F.n) and Porphyromonas gingivalis type strain ATCC 33277 (P.g 33277) bacterial species were tested when they were grown as monoculture or as dual species culture. (A) DNase I effect on biofilm formation, (B) DNase I effect on 48-h biofilm, (C) Proteinase K effect on biofilm formation, (D) Proteinase K effect on 48-h biofilm. The colored columns refer to the enzyme concentrations (0.125, 0.25, 0.5, and 1 mg/ml). The y-axis represents absorbance at 570 nm. The bars represent the means with standard deviations for 3–5 samples.

    Article Snippet: F. nucleatum type strain ATCC 25586 and P. gingivalis type strain ATCC 33277 were tested when they were grown as a monoculture or as a dual species culture.

    Techniques:

    (A) Biomass and maximum thickness of Fusobacterium nucleatum ATCC 25586 (F.n) when grown alone or together with Porphyromonas gingivalis W50 (P.g) biofilm and calculated from one point z-stack confocal microscopy images taken from the middle of the flow cell and analysed by COMSTAT software program. (B) Representative CLSM images of 24-h- (left), 48-h- (middle), and 72-h- (right) old biofilms showing mutualistic growth of F. nucleatum ATCC 25586 and P. gingivalis W50 (upper) compared to mono-species F. nucleatum ATCC 25586 (lower). The biofilms were grown in flow cells and were stained with Cyto9 (green) and propidium iodide (red).

    Journal: Journal of Oral Microbiology

    Article Title: Characterization of extracellular polymeric matrix, and treatment of Fusobacterium nucleatum and Porphyromonas gingivalis biofilms with DNase I and proteinase K

    doi: 10.3402/jom.v5i0.20015

    Figure Lengend Snippet: (A) Biomass and maximum thickness of Fusobacterium nucleatum ATCC 25586 (F.n) when grown alone or together with Porphyromonas gingivalis W50 (P.g) biofilm and calculated from one point z-stack confocal microscopy images taken from the middle of the flow cell and analysed by COMSTAT software program. (B) Representative CLSM images of 24-h- (left), 48-h- (middle), and 72-h- (right) old biofilms showing mutualistic growth of F. nucleatum ATCC 25586 and P. gingivalis W50 (upper) compared to mono-species F. nucleatum ATCC 25586 (lower). The biofilms were grown in flow cells and were stained with Cyto9 (green) and propidium iodide (red).

    Article Snippet: F. nucleatum type strain ATCC 25586 and P. gingivalis type strain ATCC 33277 were tested when they were grown as a monoculture or as a dual species culture.

    Techniques: Confocal Microscopy, Flow Cytometry, Software, Confocal Laser Scanning Microscopy, Staining

    Representative CLSM image shows proteins in EPM of 24-h dual species biofilm ( Fusobacterium nucleatum ATCC 25586 and Porphyromonas gingivalis W50) grown in flow cells. The proteins were stained with SYPRO ® Ruby stain (blue). Sideviews, XZ (top) and YZ (right) are sagittal sections of the biofilm. Scale Bar = 20 µm.

    Journal: Journal of Oral Microbiology

    Article Title: Characterization of extracellular polymeric matrix, and treatment of Fusobacterium nucleatum and Porphyromonas gingivalis biofilms with DNase I and proteinase K

    doi: 10.3402/jom.v5i0.20015

    Figure Lengend Snippet: Representative CLSM image shows proteins in EPM of 24-h dual species biofilm ( Fusobacterium nucleatum ATCC 25586 and Porphyromonas gingivalis W50) grown in flow cells. The proteins were stained with SYPRO ® Ruby stain (blue). Sideviews, XZ (top) and YZ (right) are sagittal sections of the biofilm. Scale Bar = 20 µm.

    Article Snippet: F. nucleatum type strain ATCC 25586 and P. gingivalis type strain ATCC 33277 were tested when they were grown as a monoculture or as a dual species culture.

    Techniques: Confocal Laser Scanning Microscopy, Flow Cytometry, Staining

    Gel electrophoresis (0.8% agarose gel) of the extracellular DNA. The eDNA was extracted from the matrix of 5-day-old biofilm of these species. F.n, Fusobacterium nucleatum ATCC 25586; P.g W50, Porphyromonas gingivalis W50; P.g 381, P. gingivalis FDC381; P.g 33277, P. gingivalis ATCC 33277. Lane M, EZ load 100-bp molecular ruler (Bio-Rad).

    Journal: Journal of Oral Microbiology

    Article Title: Characterization of extracellular polymeric matrix, and treatment of Fusobacterium nucleatum and Porphyromonas gingivalis biofilms with DNase I and proteinase K

    doi: 10.3402/jom.v5i0.20015

    Figure Lengend Snippet: Gel electrophoresis (0.8% agarose gel) of the extracellular DNA. The eDNA was extracted from the matrix of 5-day-old biofilm of these species. F.n, Fusobacterium nucleatum ATCC 25586; P.g W50, Porphyromonas gingivalis W50; P.g 381, P. gingivalis FDC381; P.g 33277, P. gingivalis ATCC 33277. Lane M, EZ load 100-bp molecular ruler (Bio-Rad).

    Article Snippet: F. nucleatum type strain ATCC 25586 and P. gingivalis type strain ATCC 33277 were tested when they were grown as a monoculture or as a dual species culture.

    Techniques: Nucleic Acid Electrophoresis, Agarose Gel Electrophoresis

    Effect of DNase I and proteinase K enzymes at a concentration of 1 mg/ml on biofilm formation, (A) time zero and (B) 48-h-old biofilm. The graphs show the biomass (µm 3 /µm 2 ), maximum thickness (µm), and average thickness (µm) of one point z-stack confocal images analysed by COMSTAT software program. F.n, Fusobacterium nucleatum ATCC 25586; P.g 33277, Porphyromonas gingivalis ATCC 33277.

    Journal: Journal of Oral Microbiology

    Article Title: Characterization of extracellular polymeric matrix, and treatment of Fusobacterium nucleatum and Porphyromonas gingivalis biofilms with DNase I and proteinase K

    doi: 10.3402/jom.v5i0.20015

    Figure Lengend Snippet: Effect of DNase I and proteinase K enzymes at a concentration of 1 mg/ml on biofilm formation, (A) time zero and (B) 48-h-old biofilm. The graphs show the biomass (µm 3 /µm 2 ), maximum thickness (µm), and average thickness (µm) of one point z-stack confocal images analysed by COMSTAT software program. F.n, Fusobacterium nucleatum ATCC 25586; P.g 33277, Porphyromonas gingivalis ATCC 33277.

    Article Snippet: F. nucleatum type strain ATCC 25586 and P. gingivalis type strain ATCC 33277 were tested when they were grown as a monoculture or as a dual species culture.

    Techniques: Concentration Assay, Software

    Biofilm formation on DBR disc surfaces. Representative images after crystal violet staining of biofilms formed on DBR discs by F. nucleatum ATCC 23726 (A) T. forsythia ATCC 43037 (B) V. atypica PK 1910 (C) K. pneumoniae IA 565 (D) For each set, the image on the left was a control DBR disc without biofilms growing on the surface, the image on the right was a DBR disc with biofilms growing on the surface. The experiment was performed in triplicate.

    Journal: The Open Dentistry Journal

    Article Title: Development of In Vitro Denture Biofilm Models for Halitosis Related Bacteria and their Application in Testing the Efficacy of Antimicrobial Agents

    doi: 10.2174/1874210601509010125

    Figure Lengend Snippet: Biofilm formation on DBR disc surfaces. Representative images after crystal violet staining of biofilms formed on DBR discs by F. nucleatum ATCC 23726 (A) T. forsythia ATCC 43037 (B) V. atypica PK 1910 (C) K. pneumoniae IA 565 (D) For each set, the image on the left was a control DBR disc without biofilms growing on the surface, the image on the right was a DBR disc with biofilms growing on the surface. The experiment was performed in triplicate.

    Article Snippet: T. forsythia ATCC 43037, V. atypica PK 1910 and F. nucleatum ATCC 23726 were grown anaerobically overnight at 37°C in TF medium, TH medium containing 0.06% (w/v) lactic acid and Columbia broth (Difco, USA), respectively [ ].

    Techniques: Staining, IA

    CLSM images of biofilms on DBR disc surfaces. Biofilm formation of F. nucleatum ATCC 23726 (A) T. forsythia ATCC 43037 (B) V. atypica PK 1910 (C) K. pneumoniae IA 565 (D) on DBR discs. For each set, the image on the left was taken through a 20x objective (Scale bar, 50 μm); while the image on the right was taken through a 63x objective (Scale bar, 20 μm). Four random fields of view were examined for each sample and representative images are shown.

    Journal: The Open Dentistry Journal

    Article Title: Development of In Vitro Denture Biofilm Models for Halitosis Related Bacteria and their Application in Testing the Efficacy of Antimicrobial Agents

    doi: 10.2174/1874210601509010125

    Figure Lengend Snippet: CLSM images of biofilms on DBR disc surfaces. Biofilm formation of F. nucleatum ATCC 23726 (A) T. forsythia ATCC 43037 (B) V. atypica PK 1910 (C) K. pneumoniae IA 565 (D) on DBR discs. For each set, the image on the left was taken through a 20x objective (Scale bar, 50 μm); while the image on the right was taken through a 63x objective (Scale bar, 20 μm). Four random fields of view were examined for each sample and representative images are shown.

    Article Snippet: T. forsythia ATCC 43037, V. atypica PK 1910 and F. nucleatum ATCC 23726 were grown anaerobically overnight at 37°C in TF medium, TH medium containing 0.06% (w/v) lactic acid and Columbia broth (Difco, USA), respectively [ ].

    Techniques: Confocal Laser Scanning Microscopy, IA

    Identification of Fap2 Homologs in F. nucleatum ATCC 23726

    Journal: Journal of dental research

    Article Title: Fusobacterium nucleatum Apoptosis-inducing Outer Membrane Protein

    doi:

    Figure Lengend Snippet: Identification of Fap2 Homologs in F. nucleatum ATCC 23726

    Article Snippet: In this study, we identified homologs to the apoptosis-inducing protein Fap2 in the transformable F. nucleatum strain ATCC 23726, created an isogenic mutant for the aim 1 gene, and demonstrated that the mutation impaired the ability of F. nucleatum to induce apoptosis.

    Techniques:

    Structural and transcriptional analyses of wild-type and aim less1 mutant strains. (A) Schematic illustration of mutagenesis: organization of aim 1 and flanking genes on the F. nucleatum ATCC 23726 wild-type and aim less1 mutant chromosome. Arrows indicate

    Journal: Journal of dental research

    Article Title: Fusobacterium nucleatum Apoptosis-inducing Outer Membrane Protein

    doi:

    Figure Lengend Snippet: Structural and transcriptional analyses of wild-type and aim less1 mutant strains. (A) Schematic illustration of mutagenesis: organization of aim 1 and flanking genes on the F. nucleatum ATCC 23726 wild-type and aim less1 mutant chromosome. Arrows indicate

    Article Snippet: In this study, we identified homologs to the apoptosis-inducing protein Fap2 in the transformable F. nucleatum strain ATCC 23726, created an isogenic mutant for the aim 1 gene, and demonstrated that the mutation impaired the ability of F. nucleatum to induce apoptosis.

    Techniques: Mutagenesis

    Roles of fusobacterial ftsX and envC in the development of monospecies and multispecies biofilms. (A) ftsX locus in the chromosome of F. nucleatum ATCC 23726, with envC adjacent to ppnK , which encodes an NAD+ kinase. Upstream of ftsX is fadA coding for the adhesin FadA ( 6 ); expression of genes in the ftsX locus and fadA appears to be controlled by individual promoters. (B) Map of the nonreplicative vector pCWU8 used to generate unmarked, in-frame gene deletion mutants in F. nucleatum . The kanamycin resistance cassette ( kan ), chloramphenicol/thiamphenicol resistance gene ( catP ), and galK are indicated. The multiple cloning sites (MCS) contain EcoRI, SacI, KpnI, BamHI, and SalI. (C) Fusobacterial strains were evaluated for their ability to form monospecies biofilm using crystal violet staining. (D) Interaction of fusobacteria and S. oralis So34 was determined by a standard coaggregation assay, with a radD mutant used as a negative control. (E) Three-species biofilms were analyzed by confocal laser scanning microscopy at a magnification of ×20, using 16S rRNA-oligonucleotide probes specific for F. nucleatum (red), A. oris (green), and S. oralis (blue); side and top views are presented. The results are representative of three independent experiments performed in triplicate.

    Journal: mBio

    Article Title: Forward Genetic Dissection of Biofilm Development by Fusobacterium nucleatum: Novel Functions of Cell Division Proteins FtsX and EnvC

    doi: 10.1128/mBio.00360-18

    Figure Lengend Snippet: Roles of fusobacterial ftsX and envC in the development of monospecies and multispecies biofilms. (A) ftsX locus in the chromosome of F. nucleatum ATCC 23726, with envC adjacent to ppnK , which encodes an NAD+ kinase. Upstream of ftsX is fadA coding for the adhesin FadA ( 6 ); expression of genes in the ftsX locus and fadA appears to be controlled by individual promoters. (B) Map of the nonreplicative vector pCWU8 used to generate unmarked, in-frame gene deletion mutants in F. nucleatum . The kanamycin resistance cassette ( kan ), chloramphenicol/thiamphenicol resistance gene ( catP ), and galK are indicated. The multiple cloning sites (MCS) contain EcoRI, SacI, KpnI, BamHI, and SalI. (C) Fusobacterial strains were evaluated for their ability to form monospecies biofilm using crystal violet staining. (D) Interaction of fusobacteria and S. oralis So34 was determined by a standard coaggregation assay, with a radD mutant used as a negative control. (E) Three-species biofilms were analyzed by confocal laser scanning microscopy at a magnification of ×20, using 16S rRNA-oligonucleotide probes specific for F. nucleatum (red), A. oris (green), and S. oralis (blue); side and top views are presented. The results are representative of three independent experiments performed in triplicate.

    Article Snippet: A library of approximately 24,000 thiamphenicol-resistant Tn5 mutants were generated from the parental F. nucleatum ATCC 23726 strain from a single Tn5 transposome reaction that was carried out in bulk, based on reaction efficiency determined from small-scale quantitative electroporation experiments.

    Techniques: Expressing, Plasmid Preparation, Clone Assay, Staining, Mutagenesis, Negative Control, Confocal Laser Scanning Microscopy

    The Fap2 adhesin is involved in placental colonization. Wild-type F. nucleatum ATCC 23726 or the hemagglutination-deficient mutant K50 was injected into the tail veins of pregnant mice. After 24 h, the placentas were harvested and homogenized, and bacterial

    Journal: Infection and Immunity

    Article Title: Fap2 of Fusobacterium nucleatum Is a Galactose-Inhibitable Adhesin Involved in Coaggregation, Cell Adhesion, and Preterm Birth

    doi: 10.1128/IAI.02838-14

    Figure Lengend Snippet: The Fap2 adhesin is involved in placental colonization. Wild-type F. nucleatum ATCC 23726 or the hemagglutination-deficient mutant K50 was injected into the tail veins of pregnant mice. After 24 h, the placentas were harvested and homogenized, and bacterial

    Article Snippet: Wild-type F. nucleatum ATCC 23726, the three hemagglutination-deficient mutants, and a randomly selected control mutant, J78, were stained with carboxyfluorescein succinimidyl ester (CFSE) and incubated with HEK 293T cells.

    Techniques: Mutagenesis, Injection, Mouse Assay

    F. nucleatum ATCC 23726 hemagglutination is inhibited by d -galactose but not by l -arginine. (A) Bacteria incubated with 2% sheep red blood cells (RBC) in the absence and presence of 6 mM d -galactose (Gal) or 50 mM l -arginine (Arg). (B) Erythrocytes incubated

    Journal: Infection and Immunity

    Article Title: Fap2 of Fusobacterium nucleatum Is a Galactose-Inhibitable Adhesin Involved in Coaggregation, Cell Adhesion, and Preterm Birth

    doi: 10.1128/IAI.02838-14

    Figure Lengend Snippet: F. nucleatum ATCC 23726 hemagglutination is inhibited by d -galactose but not by l -arginine. (A) Bacteria incubated with 2% sheep red blood cells (RBC) in the absence and presence of 6 mM d -galactose (Gal) or 50 mM l -arginine (Arg). (B) Erythrocytes incubated

    Article Snippet: Wild-type F. nucleatum ATCC 23726, the three hemagglutination-deficient mutants, and a randomly selected control mutant, J78, were stained with carboxyfluorescein succinimidyl ester (CFSE) and incubated with HEK 293T cells.

    Techniques: Incubation

    The effect of the environmental conditions on the activity of H 2 S-producing enzymes was tested for Fusobacterium nucleatum polymorphum ATCC 10953. The bacteria were grown in different broths before protein extraction and 1D gel electrophoresis followed by in-gel activity assay

    Journal: BMC Microbiology

    Article Title: The proteins of Fusobacterium spp. involved in hydrogen sulfide production from L-cysteine

    doi: 10.1186/s12866-017-0967-9

    Figure Lengend Snippet: The effect of the environmental conditions on the activity of H 2 S-producing enzymes was tested for Fusobacterium nucleatum polymorphum ATCC 10953. The bacteria were grown in different broths before protein extraction and 1D gel electrophoresis followed by in-gel activity assay

    Article Snippet: For F. nucleatum ATCC 10953, the influence of other environmental conditions were tested in TH broth buffered to pH 6, pH 7, pH 8 or TH broth, pH 7.8 supplemented with glutathione (2.5 mg/ml), sodium sulfide (0.46 mg/ml), 5% serum, 50% serum or 50% serum with hemin (10 ml/l).

    Techniques: Activity Assay, Protein Extraction, Nucleic Acid Electrophoresis

    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Journal: Journal of Bacteriology

    Article Title: Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

    doi: 10.1128/JB.187.15.5330-5340.2005

    Figure Lengend Snippet: Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Article Snippet: The accession numbers for the FadA sequences from other fusobacterial strains and species are as follows: for F. nucleatum ATCC 10953 , for F. nucleatum ATCC 23726 , for F. nucleatum ATCC 25586 , for F. nucleatum ATCC 49256 , for F. nucleatum ATCC 51190 , for F. nucleatum DUMC1356 , for F. nucleatum DUMC2079 , for F. nucleatum DUMC2929 , for F. nucleatum DUMC3156 , for F. nucleatum DUMC3349 , for F. nucleatum PK1594 , for F. periodonticum ATCC 33693 , and for F. simiae ATCC 33568 .

    Techniques: Sequencing