amoebophilus asiaticus Search Results


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  • 97
    ATCC acanthamoeba sp
    Acanthamoeba Sp, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 64 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore dnase i
    Dnase I, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 33921 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    5a2  (ATCC)
    95
    ATCC 5a2
    Ultrastructure of “ Ca . Amoebophilus asiaticus” <t>5a2</t> within its Acanthamoeba host cell. (A) Transmission electron micrograph showing the distribution of “ Ca . Amoebophilus asiaticus” in its Acanthamoeba host cell. (B and C)
    5a2, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore rna
    Ultrastructure of “ Ca . Amoebophilus asiaticus” <t>5a2</t> within its Acanthamoeba host cell. (A) Transmission electron micrograph showing the distribution of “ Ca . Amoebophilus asiaticus” in its Acanthamoeba host cell. (B and C)
    Rna, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5994 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Basler vibrio cholerae
    Sheath formation in Hcp‐limited cells Fluorescence timelapse images of Vibrio <t>cholerae</t> vipA‐N3‐msfGFP in hcp1/2 mutant background, complemented with hcp expressed from L‐arabinose‐inducible vector pBAD24. Scale bars are 2 μm.
    Vibrio Cholerae, supplied by Basler, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC acanthamoeba castellanii
    Sheath formation in Hcp‐limited cells Fluorescence timelapse images of Vibrio <t>cholerae</t> vipA‐N3‐msfGFP in hcp1/2 mutant background, complemented with hcp expressed from L‐arabinose‐inducible vector pBAD24. Scale bars are 2 μm.
    Acanthamoeba Castellanii, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 321 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    t6ss  (Basler)
    90
    Basler t6ss
    Morphology of the sheath distal end Two orthogonal slices through the raw sheath–distal‐end reconstruction shown. Ring numbers N, (N−1), and (N−2) correspond to the topmost ring and the two previous rings, and are separated by dashed red lines. Representative reference‐free 2D class averages of the distal‐end particles, extracted from cryo‐EM images. Left and center: Side and top views of putative docking of refitted sheath domain of the VipA‐N3 sheath–tube (PDB 5MXN) into distal end. Right: Putative pseudo atomic model of the distal end with refitted sheath domain of the VipA‐N3 sheath–tube, refitted topmost sheath–tube ring and three rings below (PDB 5MXN). Topmost sheath rings are outlined with dashed blue circles. Putative dockings of low‐resolution EM reconstruction EAEC TssA (EMD‐3282) into distal end of <t>T6SS.</t> Topmost sheath ring N, two previous sheath rings (N‐1) and (N‐2), and two tube rings (N‐1) and (N‐2) are outlined with dashed blue circles.
    T6ss, supplied by Basler, used in various techniques. Bioz Stars score: 90/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher trizol
    Morphology of the sheath distal end Two orthogonal slices through the raw sheath–distal‐end reconstruction shown. Ring numbers N, (N−1), and (N−2) correspond to the topmost ring and the two previous rings, and are separated by dashed red lines. Representative reference‐free 2D class averages of the distal‐end particles, extracted from cryo‐EM images. Left and center: Side and top views of putative docking of refitted sheath domain of the VipA‐N3 sheath–tube (PDB 5MXN) into distal end. Right: Putative pseudo atomic model of the distal end with refitted sheath domain of the VipA‐N3 sheath–tube, refitted topmost sheath–tube ring and three rings below (PDB 5MXN). Topmost sheath rings are outlined with dashed blue circles. Putative dockings of low‐resolution EM reconstruction EAEC TssA (EMD‐3282) into distal end of <t>T6SS.</t> Topmost sheath ring N, two previous sheath rings (N‐1) and (N‐2), and two tube rings (N‐1) and (N‐2) are outlined with dashed blue circles.
    Trizol, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 326033 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Ultrastructure of “ Ca . Amoebophilus asiaticus” 5a2 within its Acanthamoeba host cell. (A) Transmission electron micrograph showing the distribution of “ Ca . Amoebophilus asiaticus” in its Acanthamoeba host cell. (B and C)

    Journal: Journal of Bacteriology

    Article Title: The Genome of the Amoeba Symbiont “Candidatus Amoebophilus asiaticus” Reveals Common Mechanisms for Host Cell Interaction among Amoeba-Associated Bacteria

    doi: 10.1128/JB.01379-09

    Figure Lengend Snippet: Ultrastructure of “ Ca . Amoebophilus asiaticus” 5a2 within its Acanthamoeba host cell. (A) Transmission electron micrograph showing the distribution of “ Ca . Amoebophilus asiaticus” in its Acanthamoeba host cell. (B and C)

    Article Snippet: Amoebophilus asiaticus” 5a2 (ATCC number PRA-228) was isolated from lake sediment in Austria ( ) and cultivated using peptone-yeast-glucose-medium (PYG) [containing 20 g/liter proteose peptone, 18 g/liter glucose, 2 g/liter yeast extract, 3.4 mM sodium citrate-dihydrate, 4 mM MgSO4 ·7H2 O, 2 mM Na2 HPO4 ·2H2 O, 1.7 mM KH2 PO4 , 0.05 mM Fe(NH4 )2 (SO4 )2 ·6H2 O] as described previously ( ).

    Techniques: Transmission Assay

    Sheath formation in Hcp‐limited cells Fluorescence timelapse images of Vibrio cholerae vipA‐N3‐msfGFP in hcp1/2 mutant background, complemented with hcp expressed from L‐arabinose‐inducible vector pBAD24. Scale bars are 2 μm.

    Journal: The EMBO Journal

    Article Title: Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

    doi: 10.15252/embj.201797103

    Figure Lengend Snippet: Sheath formation in Hcp‐limited cells Fluorescence timelapse images of Vibrio cholerae vipA‐N3‐msfGFP in hcp1/2 mutant background, complemented with hcp expressed from L‐arabinose‐inducible vector pBAD24. Scale bars are 2 μm.

    Article Snippet: The whole T6SS was first observed at low resolution using cryo‐electron tomography (cryo‐ET) in Vibrio cholerae (Basler et al , ) and more recently in Myxococcus xanthus (Chang et al , ) and Amoebophilus asiaticus (Böck et al , ).

    Techniques: Fluorescence, Mutagenesis, Plasmid Preparation

    Morphology of the sheath distal end Two orthogonal slices through the raw sheath–distal‐end reconstruction shown. Ring numbers N, (N−1), and (N−2) correspond to the topmost ring and the two previous rings, and are separated by dashed red lines. Representative reference‐free 2D class averages of the distal‐end particles, extracted from cryo‐EM images. Left and center: Side and top views of putative docking of refitted sheath domain of the VipA‐N3 sheath–tube (PDB 5MXN) into distal end. Right: Putative pseudo atomic model of the distal end with refitted sheath domain of the VipA‐N3 sheath–tube, refitted topmost sheath–tube ring and three rings below (PDB 5MXN). Topmost sheath rings are outlined with dashed blue circles. Putative dockings of low‐resolution EM reconstruction EAEC TssA (EMD‐3282) into distal end of T6SS. Topmost sheath ring N, two previous sheath rings (N‐1) and (N‐2), and two tube rings (N‐1) and (N‐2) are outlined with dashed blue circles.

    Journal: The EMBO Journal

    Article Title: Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

    doi: 10.15252/embj.201797103

    Figure Lengend Snippet: Morphology of the sheath distal end Two orthogonal slices through the raw sheath–distal‐end reconstruction shown. Ring numbers N, (N−1), and (N−2) correspond to the topmost ring and the two previous rings, and are separated by dashed red lines. Representative reference‐free 2D class averages of the distal‐end particles, extracted from cryo‐EM images. Left and center: Side and top views of putative docking of refitted sheath domain of the VipA‐N3 sheath–tube (PDB 5MXN) into distal end. Right: Putative pseudo atomic model of the distal end with refitted sheath domain of the VipA‐N3 sheath–tube, refitted topmost sheath–tube ring and three rings below (PDB 5MXN). Topmost sheath rings are outlined with dashed blue circles. Putative dockings of low‐resolution EM reconstruction EAEC TssA (EMD‐3282) into distal end of T6SS. Topmost sheath ring N, two previous sheath rings (N‐1) and (N‐2), and two tube rings (N‐1) and (N‐2) are outlined with dashed blue circles.

    Article Snippet: The whole T6SS was first observed at low resolution using cryo‐electron tomography (cryo‐ET) in Vibrio cholerae (Basler et al , ) and more recently in Myxococcus xanthus (Chang et al , ) and Amoebophilus asiaticus (Böck et al , ).

    Techniques:

    Central spike, tube, and sheath densities with a cavity for effector proteins Cutaway view of the density corresponding to the baseplate and spike with fitted X‐ray crystallographic structures of VgrG‐1 trimer (PDB 4MTK) and PAAR monomer (PDB 4JIV). Putative cavity for T6SS effectors is outlined in green. Side view of the density corresponding to the sheath next to the baseplate fitted with the atomic model of the VipA‐N3 sheath–tube (PDB 5MXN). In panels (B–D), odd sheath rings are colored in red, even in blue. Sheath rings are numbered starting from the first ring next to the baseplate. Side cutaway view of the baseplate reconstruction with the fitted atomic model of VipA‐N3 sheath–tube (PDB 5MXN). Top cutaway views of (C) with the fitted atomic model of VipA‐N3 sheath–tube (PDB 5MXN). Slices through the raw sheath–baseplate reconstruction, as in (D).

    Journal: The EMBO Journal

    Article Title: Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

    doi: 10.15252/embj.201797103

    Figure Lengend Snippet: Central spike, tube, and sheath densities with a cavity for effector proteins Cutaway view of the density corresponding to the baseplate and spike with fitted X‐ray crystallographic structures of VgrG‐1 trimer (PDB 4MTK) and PAAR monomer (PDB 4JIV). Putative cavity for T6SS effectors is outlined in green. Side view of the density corresponding to the sheath next to the baseplate fitted with the atomic model of the VipA‐N3 sheath–tube (PDB 5MXN). In panels (B–D), odd sheath rings are colored in red, even in blue. Sheath rings are numbered starting from the first ring next to the baseplate. Side cutaway view of the baseplate reconstruction with the fitted atomic model of VipA‐N3 sheath–tube (PDB 5MXN). Top cutaway views of (C) with the fitted atomic model of VipA‐N3 sheath–tube (PDB 5MXN). Slices through the raw sheath–baseplate reconstruction, as in (D).

    Article Snippet: The whole T6SS was first observed at low resolution using cryo‐electron tomography (cryo‐ET) in Vibrio cholerae (Basler et al , ) and more recently in Myxococcus xanthus (Chang et al , ) and Amoebophilus asiaticus (Böck et al , ).

    Techniques:

    Raw images and cryo‐ EM structures of T6 SS baseplate and distal‐end complexes A raw negative‐stained image of VipA‐N3 mutant sheath (scale bar: 100 nm). Extended sheath, baseplate, and distal end are highlighted with white arrows. Right insets: examples of T6SS assemblies of different lengths (shortest ˜5 sheath rings, longest ˜220 rings). Upper left insets: representative reference‐free 2D class averages of baseplate (right) and distal‐end (left) particles, extracted from negative‐stained images. A raw cryo‐EM image of VipA‐N3 mutant (scale bar: 50 nm). Baseplate reconstruction was calculated for area highlighted with red circles. Side, cutaway, and tilted views of the sheath–baseplate cryo‐EM reconstruction. 3D visualizations were rendered using UCSF Chimera. Baseplate model colored according to the local resolution variation, shown in the color bar on the right in Angstroms. Maps are shown at the contour level of 1.5σ. Side, cutaway, and top views of the sheath–distal‐end cryo‐EM reconstruction. 3D visualizations were rendered using UCSF Chimera. Distal‐end model colored according to the local resolution variation, shown in the color bar on the right in Angstroms. Maps are shown at the contour level of 1.5σ.

    Journal: The EMBO Journal

    Article Title: Cryo‐ EM reconstruction of Type VI secretion system baseplate and sheath distal end

    doi: 10.15252/embj.201797103

    Figure Lengend Snippet: Raw images and cryo‐ EM structures of T6 SS baseplate and distal‐end complexes A raw negative‐stained image of VipA‐N3 mutant sheath (scale bar: 100 nm). Extended sheath, baseplate, and distal end are highlighted with white arrows. Right insets: examples of T6SS assemblies of different lengths (shortest ˜5 sheath rings, longest ˜220 rings). Upper left insets: representative reference‐free 2D class averages of baseplate (right) and distal‐end (left) particles, extracted from negative‐stained images. A raw cryo‐EM image of VipA‐N3 mutant (scale bar: 50 nm). Baseplate reconstruction was calculated for area highlighted with red circles. Side, cutaway, and tilted views of the sheath–baseplate cryo‐EM reconstruction. 3D visualizations were rendered using UCSF Chimera. Baseplate model colored according to the local resolution variation, shown in the color bar on the right in Angstroms. Maps are shown at the contour level of 1.5σ. Side, cutaway, and top views of the sheath–distal‐end cryo‐EM reconstruction. 3D visualizations were rendered using UCSF Chimera. Distal‐end model colored according to the local resolution variation, shown in the color bar on the right in Angstroms. Maps are shown at the contour level of 1.5σ.

    Article Snippet: The whole T6SS was first observed at low resolution using cryo‐electron tomography (cryo‐ET) in Vibrio cholerae (Basler et al , ) and more recently in Myxococcus xanthus (Chang et al , ) and Amoebophilus asiaticus (Böck et al , ).

    Techniques: Staining, Mutagenesis