escherichia coli Search Results


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  • 99
    New England Biolabs dna polymerase
    Dna Polymerase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 4972 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC e coli atcc 25922
    E Coli Atcc 25922, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 10655 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher total rna
    Total Rna, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 475535 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore lps
    Volcano plot for chicken challenged with <t>Escherichia</t> coli lipopolysaccharide endotoxin versus saline group. Volcano plot of fold changes (x-axis) and their associated log10 transformed p-values (y-axis) for the 571 peptides analysed by LC-MS. Peptides significantly different between saline and LPS groups (log10 p > 1.3) are in black, non-significant peptides (log10 p
    Lps, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 55220 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    lps - by Bioz Stars, 2020-10
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    Millipore escherichia coli
    Volcano plot for chicken challenged with <t>Escherichia</t> coli lipopolysaccharide endotoxin versus saline group. Volcano plot of fold changes (x-axis) and their associated log10 transformed p-values (y-axis) for the 571 peptides analysed by LC-MS. Peptides significantly different between saline and LPS groups (log10 p > 1.3) are in black, non-significant peptides (log10 p
    Escherichia Coli, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 14091 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore e coli bl21
    Volcano plot for chicken challenged with <t>Escherichia</t> coli lipopolysaccharide endotoxin versus saline group. Volcano plot of fold changes (x-axis) and their associated log10 transformed p-values (y-axis) for the 571 peptides analysed by LC-MS. Peptides significantly different between saline and LPS groups (log10 p > 1.3) are in black, non-significant peptides (log10 p
    E Coli Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 11108 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    R&D Systems bmp 2
    Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and <t>BMP-2,</t> and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.
    Bmp 2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 99/100, based on 3008 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC e coli o157 h7
    Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and <t>BMP-2,</t> and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.
    E Coli O157 H7, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1874 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs exonuclease i
    Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and <t>BMP-2,</t> and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.
    Exonuclease I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 5008 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher escherichia coli dh5α
    Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and <t>BMP-2,</t> and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.
    Escherichia Coli Dh5α, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2614 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher competent e coli
    Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and <t>BMP-2,</t> and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.
    Competent E Coli, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5958 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher e coli top10
    Silencing results for RFP and GFP expressed by the Plux-RG and Plux-GR synthetic operons in the <t>TOP10</t> strain. a Silencing of the target gene (RFP) and the non-target gene (GFP) via the silencing device sRFP. b Unspecific silencing of RFP and GFP, in the
    E Coli Top10, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 4044 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher e coli bl21
    Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli <t>BL21.</t> Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p
    E Coli Bl21, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 4872 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore escherichia coli strain bl21
    Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli <t>BL21.</t> Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p
    Escherichia Coli Strain Bl21, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2381 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Stratagene e coli bl21
    SDS-PAGE analysis of purified protein recombinant SllB in E. coli <t>BL21</t> cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.
    E Coli Bl21, supplied by Stratagene, used in various techniques. Bioz Stars score: 93/100, based on 3182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Stratagene e coli xl1 blue
    Immunoblot showing OmpL1 expression at different IPTG concentrations. A culture of E. coli <t>XL1-Blue</t> containing plasmid pMMB66-OmpL1 was grown to log phase, separated into four equal volumes, and treated with various concentrations of IPTG. Cells were incubated for an additional 3 h in a shaker incubator at 37°C, pelleted in a microcentrifuge, resuspended in final sample buffer, and analyzed by SDS-PAGE and immunoblotting. A companion SDS-polyacrylamide gel loaded with the same four samples was stained with Coomassie brilliant blue to verify that all four lanes contained comparable amounts of material (data not shown). The locations of molecular size standards are shown (in kilodaltons) on the left. Even though use of the tac promoter typically results in relatively high background expression levels, expression using plasmid pMMB66-OmpL1 was not detectable without IPTG induction.
    E Coli Xl1 Blue, supplied by Stratagene, used in various techniques. Bioz Stars score: 92/100, based on 1750 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC e coli atcc 35218
    Immunoblot showing OmpL1 expression at different IPTG concentrations. A culture of E. coli <t>XL1-Blue</t> containing plasmid pMMB66-OmpL1 was grown to log phase, separated into four equal volumes, and treated with various concentrations of IPTG. Cells were incubated for an additional 3 h in a shaker incubator at 37°C, pelleted in a microcentrifuge, resuspended in final sample buffer, and analyzed by SDS-PAGE and immunoblotting. A companion SDS-polyacrylamide gel loaded with the same four samples was stained with Coomassie brilliant blue to verify that all four lanes contained comparable amounts of material (data not shown). The locations of molecular size standards are shown (in kilodaltons) on the left. Even though use of the tac promoter typically results in relatively high background expression levels, expression using plasmid pMMB66-OmpL1 was not detectable without IPTG induction.
    E Coli Atcc 35218, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1043 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare escherichia coli bl21
    Immunoblot showing OmpL1 expression at different IPTG concentrations. A culture of E. coli <t>XL1-Blue</t> containing plasmid pMMB66-OmpL1 was grown to log phase, separated into four equal volumes, and treated with various concentrations of IPTG. Cells were incubated for an additional 3 h in a shaker incubator at 37°C, pelleted in a microcentrifuge, resuspended in final sample buffer, and analyzed by SDS-PAGE and immunoblotting. A companion SDS-polyacrylamide gel loaded with the same four samples was stained with Coomassie brilliant blue to verify that all four lanes contained comparable amounts of material (data not shown). The locations of molecular size standards are shown (in kilodaltons) on the left. Even though use of the tac promoter typically results in relatively high background expression levels, expression using plasmid pMMB66-OmpL1 was not detectable without IPTG induction.
    Escherichia Coli Bl21, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 1560 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher escherichia coli
    Mucosal-associated invariant T (MAIT) cells are activated by pneumococci. A , Gating strategy for analysis of MAIT cell–derived interferon γ (IFN-γ) following activation of peripheral blood mononuclear cells. B , Example fluorescence-activated cell-sorting plots showing upregulation of CD69 and IFN-γ in unstimulated and stimulated MAIT cells (gating on CD3 + CD8 + live T cells). C and D , Ten Pneumococcal Molecular Epidemiological Network (PMEN) reference strains were used to probe the activation of MAIT cells following coculture of peripheral blood mononuclear cells in the presence of the monocytic cell line, THP1. <t>Escherichia</t> coli was added as a positive control. Frequency of cells expressing IFN-γ among MAIT cells ( C ) or CD161 − CD8 + T cells ( D ) are shown (n = 9). E and F , CD69 expression measured by geometric mean fluorescence intensity (gMFI) in MAIT cells ( E ) or CD161 − CD8 + T cells ( F ) are shown (n = 6). ** P
    Escherichia Coli, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 6904 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Volcano plot for chicken challenged with Escherichia coli lipopolysaccharide endotoxin versus saline group. Volcano plot of fold changes (x-axis) and their associated log10 transformed p-values (y-axis) for the 571 peptides analysed by LC-MS. Peptides significantly different between saline and LPS groups (log10 p > 1.3) are in black, non-significant peptides (log10 p

    Journal: Data in Brief

    Article Title: Integrated dataset on acute phase protein response in chicken challenged with Escherichia coli lipopolysaccharide endotoxin

    doi: 10.1016/j.dib.2018.09.103

    Figure Lengend Snippet: Volcano plot for chicken challenged with Escherichia coli lipopolysaccharide endotoxin versus saline group. Volcano plot of fold changes (x-axis) and their associated log10 transformed p-values (y-axis) for the 571 peptides analysed by LC-MS. Peptides significantly different between saline and LPS groups (log10 p > 1.3) are in black, non-significant peptides (log10 p

    Article Snippet: Twenty four birds were injected subcutaneously (SC) at time point 0, with Escherichia coli lipopolysaccharide (LPS from E. coli O111:B4 purified by phenol extraction, L2630-25MG; Sigma-Aldrich, Dorset, UK) (2 mg/kg body weight) in a volume of 0.5 mL as the treatment group and another 24 birds injected SC by sterile normal saline (0.5 mL) as a control group.

    Techniques: Transformation Assay, Liquid Chromatography with Mass Spectroscopy

    Interactome of pathways differentially expressed between chicken challenged with Escherichia coli lipopolysaccharide endotoxin and saline, and their intermediate proteins. Gene ontology analysed pathways and proteins over-represented in LPS compared with saline samples. This analyse have been done with the Cytoscape application ClueGO and the REVIGO tool for GO terms selection. GO terms and proteins over-expressed in LPS are in green, lower-expressed in LPS are in red. GO terms in grey could not be attributed specifically to over or lower expressed terms/proteins. GO terms in bold represent GO terms selected to be the most representative of their GO group defined by the REVIGO tool. The yFiles radial layout algorithm was applied.

    Journal: Data in Brief

    Article Title: Integrated dataset on acute phase protein response in chicken challenged with Escherichia coli lipopolysaccharide endotoxin

    doi: 10.1016/j.dib.2018.09.103

    Figure Lengend Snippet: Interactome of pathways differentially expressed between chicken challenged with Escherichia coli lipopolysaccharide endotoxin and saline, and their intermediate proteins. Gene ontology analysed pathways and proteins over-represented in LPS compared with saline samples. This analyse have been done with the Cytoscape application ClueGO and the REVIGO tool for GO terms selection. GO terms and proteins over-expressed in LPS are in green, lower-expressed in LPS are in red. GO terms in grey could not be attributed specifically to over or lower expressed terms/proteins. GO terms in bold represent GO terms selected to be the most representative of their GO group defined by the REVIGO tool. The yFiles radial layout algorithm was applied.

    Article Snippet: Twenty four birds were injected subcutaneously (SC) at time point 0, with Escherichia coli lipopolysaccharide (LPS from E. coli O111:B4 purified by phenol extraction, L2630-25MG; Sigma-Aldrich, Dorset, UK) (2 mg/kg body weight) in a volume of 0.5 mL as the treatment group and another 24 birds injected SC by sterile normal saline (0.5 mL) as a control group.

    Techniques: Selection

    Time-affected proteins in chicken challenged with Escherichia coli lipopolysaccharide endotoxin (LPS group). Barplot of the mean and SEM of 19 proteins differentially expressed for the different time points (0 h, 12 h, 24 h, 48 h, 72 h) in LPS group. Proteins have been grouped according to their pattern of expression: A or B and C. Patterns have been defined according to the evolution of fold changes among time.

    Journal: Data in Brief

    Article Title: Integrated dataset on acute phase protein response in chicken challenged with Escherichia coli lipopolysaccharide endotoxin

    doi: 10.1016/j.dib.2018.09.103

    Figure Lengend Snippet: Time-affected proteins in chicken challenged with Escherichia coli lipopolysaccharide endotoxin (LPS group). Barplot of the mean and SEM of 19 proteins differentially expressed for the different time points (0 h, 12 h, 24 h, 48 h, 72 h) in LPS group. Proteins have been grouped according to their pattern of expression: A or B and C. Patterns have been defined according to the evolution of fold changes among time.

    Article Snippet: Twenty four birds were injected subcutaneously (SC) at time point 0, with Escherichia coli lipopolysaccharide (LPS from E. coli O111:B4 purified by phenol extraction, L2630-25MG; Sigma-Aldrich, Dorset, UK) (2 mg/kg body weight) in a volume of 0.5 mL as the treatment group and another 24 birds injected SC by sterile normal saline (0.5 mL) as a control group.

    Techniques: Expressing

    Interactome of pathways differentially expressed among time in chicken challenged with Escherichia coli lipopolysaccharide (LPS group) and their intermediate proteins. Gene ontology analysed pathways over-represented in the list of 19 proteins differentially expressed among time in LPS group. This analyse have been done with the Cytoscape application ClueGO and the REVIGO tool for GO terms selection. GO terms in bold represent GO terms selected to be the most representative of their GO group defined by the REVIGO tool. For each proteins, 4 fold changes among the 5 different time points have been represented using colour intensity to figure fold change value. Positive fold changes are in green, negative are in red, fold change values close to 0 are in white. Proteins have been gather in 3 groups defined by their fold changes pattern. The A pattern correspond to a quick increase of a protein, then go back to the initial situation, while the pattern B correspond to a quick decrease of a protein and then a go back to the initial situation. The C pattern correspond to a decrease which happen later in the infection process. For each pattern, evolution of one protein mean among time has been represented with histogram to illustrate the pattern properties.

    Journal: Data in Brief

    Article Title: Integrated dataset on acute phase protein response in chicken challenged with Escherichia coli lipopolysaccharide endotoxin

    doi: 10.1016/j.dib.2018.09.103

    Figure Lengend Snippet: Interactome of pathways differentially expressed among time in chicken challenged with Escherichia coli lipopolysaccharide (LPS group) and their intermediate proteins. Gene ontology analysed pathways over-represented in the list of 19 proteins differentially expressed among time in LPS group. This analyse have been done with the Cytoscape application ClueGO and the REVIGO tool for GO terms selection. GO terms in bold represent GO terms selected to be the most representative of their GO group defined by the REVIGO tool. For each proteins, 4 fold changes among the 5 different time points have been represented using colour intensity to figure fold change value. Positive fold changes are in green, negative are in red, fold change values close to 0 are in white. Proteins have been gather in 3 groups defined by their fold changes pattern. The A pattern correspond to a quick increase of a protein, then go back to the initial situation, while the pattern B correspond to a quick decrease of a protein and then a go back to the initial situation. The C pattern correspond to a decrease which happen later in the infection process. For each pattern, evolution of one protein mean among time has been represented with histogram to illustrate the pattern properties.

    Article Snippet: Twenty four birds were injected subcutaneously (SC) at time point 0, with Escherichia coli lipopolysaccharide (LPS from E. coli O111:B4 purified by phenol extraction, L2630-25MG; Sigma-Aldrich, Dorset, UK) (2 mg/kg body weight) in a volume of 0.5 mL as the treatment group and another 24 birds injected SC by sterile normal saline (0.5 mL) as a control group.

    Techniques: Selection, Infection

    Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and BMP-2, and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.

    Journal: Nature biotechnology

    Article Title: Scaffolds that induce bone marrow-like features to enhance T-cell immunity in vivo after hematopoietic stem cell transplantation.

    doi: 10.1038/s41587-019-0017-2

    Figure Lengend Snippet: Alginate-PEG-DLL4 based bone marrow cryogel (BMC) presents DLL4 and BMP-2, and preferentially expands common lymphoid progenitors (CLPs). (a) Schematic for the fabrication of covalently crosslinked BMC. (b) Representative cross sectional scanning electron micrograph (SEM) image of a BMC. Scale bar, 1mm. (c) Representative SEM of the pore shape and structure within the cross section of the BMC. Scale bar = 200μm. (d) Release kinetics of the encapsulated BMP-2 (red line) and covalently tethered DLL4 (green line) (n=5 per group) (e) Surface plasmon resonance measuring the binding kinetics of the DLL4 before and after modification with the methacrylate linker. (f) In vitro differentiation of isolated mouse and human hematopoietic stem and progenitor cells into CLPs as a function of the degree of functionalization of methacrylate groups on the polymer backbone (n = 5). (g) Proportion of Lin - common lymphoid and myeloid mouse progenitor cells quantified in growth medium, blank, single factor and dual factor BMCs. Images and pore size quantification in b, c are representative of ten independent replicates. Data in d, f, g represent the mean ± s.d. of five experimental replicates and are representative of three independent experiments. Distinct samples were assayed individually.

    Article Snippet: BMP-2 (R & D Systems) was added to the polymer solution before cryopolymerization.

    Techniques: SPR Assay, Binding Assay, Modification, In Vitro, Isolation

    Enhancement of T-cell reconstitution mediated by the BMC (a) The sum of CD3 + CD4 + and CD3 + CD8 + in the peripheral blood of mice post-HSCT. B6 mice were irradiated with 1 × 1000 cGy L-TBI dose. Mice were subsequently transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI and treated as indicated in the figure. Measurement of the recovery in CD4 + to CD8 + T-cell ratios in the (b) blood, (c) spleen and (d) bone marrow, as a function of time, with non-irradiated mice as for comparison for the same groups as in (a). In (a - d) Post-HSCT mice with no BMC (Transplant only), post-HSCT mice treated with bolus BMP-2 and DLL-4 injection, a BMC containing BMP-2 (BMP-2 BMC), and post-HSCT mice treated with a BMC containing BMP-2 and DLL4 (Dual BMC) were analyzed. In (e-j) B6 mice were irradiated with 500 cGy SL-TBI and subsequently transplanted with 5 × 10 5 lineage-depleted bone marrow cells within 48 hours post-radiation. Total number of (e) DP (f) SP4 and (g) SP8 thymocytes and peripheral (h) CD4 + and (i) CD8 + T-cells and (j) B-cells in the spleens of SL-TBI syn-HSCT mice that were treated with and without a dual BMC 28 days post-transplant. Data in a-d represent the mean ± s.d. of n = 8 mice per group for each time point and are representative of at least 3 independent experiments. Data in e-j represent the mean ± s.d. of n= 10 mice and are representative of 2 independent experiments. (*P

    Journal: Nature biotechnology

    Article Title: Scaffolds that induce bone marrow-like features to enhance T-cell immunity in vivo after hematopoietic stem cell transplantation.

    doi: 10.1038/s41587-019-0017-2

    Figure Lengend Snippet: Enhancement of T-cell reconstitution mediated by the BMC (a) The sum of CD3 + CD4 + and CD3 + CD8 + in the peripheral blood of mice post-HSCT. B6 mice were irradiated with 1 × 1000 cGy L-TBI dose. Mice were subsequently transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI and treated as indicated in the figure. Measurement of the recovery in CD4 + to CD8 + T-cell ratios in the (b) blood, (c) spleen and (d) bone marrow, as a function of time, with non-irradiated mice as for comparison for the same groups as in (a). In (a - d) Post-HSCT mice with no BMC (Transplant only), post-HSCT mice treated with bolus BMP-2 and DLL-4 injection, a BMC containing BMP-2 (BMP-2 BMC), and post-HSCT mice treated with a BMC containing BMP-2 and DLL4 (Dual BMC) were analyzed. In (e-j) B6 mice were irradiated with 500 cGy SL-TBI and subsequently transplanted with 5 × 10 5 lineage-depleted bone marrow cells within 48 hours post-radiation. Total number of (e) DP (f) SP4 and (g) SP8 thymocytes and peripheral (h) CD4 + and (i) CD8 + T-cells and (j) B-cells in the spleens of SL-TBI syn-HSCT mice that were treated with and without a dual BMC 28 days post-transplant. Data in a-d represent the mean ± s.d. of n = 8 mice per group for each time point and are representative of at least 3 independent experiments. Data in e-j represent the mean ± s.d. of n= 10 mice and are representative of 2 independent experiments. (*P

    Article Snippet: BMP-2 (R & D Systems) was added to the polymer solution before cryopolymerization.

    Techniques: Mouse Assay, Irradiation, Injection

    In vivo recruitment of donor cells to BMC and enhanced seeding of thymic progenitors. (a) Total number and type of donor derived, GFP + cells in the BMC containing combinations of BMP-2 and DLL-4 and blank BMCs. (b) Absolute number of donor GFP + CLPs and the percentage of Ly6D - CLPs in BMP-2- and dual factor- BMCs. (c) Schematic of experimental setup for surgical transplantation of harvested BMCs from post-HSCT mice into sub-lethally irradiated mice. (d) DP, SP CD4 + and SP CD8 + cells quantified in the thymus 20-days post surgical transplantation of BMC. (e) Total number of early T-lineage progenitors (ETP; CD44 + CD25 − c-kit + ) quantified as a function of lineage-depleted transplanted cell dose compared with BMC treatment with the lowest cell dose at multiple time points post transplant with representative FACS plots (five experimental replicates at each time point, 2 independent experiments). (f-k) Total number of early T-lineage progenitors (ETP; CD44 + CD25 − c-kit + ), DN2 (CD44 + CD25 − ), DN3 (CD44 + CD25 − ), DP, SP4, SP8 thymocyte subsets compared across different treatment conditions at multiple time points post transplant. For a, b, f-k the mice were transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI (1 × 1000 cGy). In c, d an initial set of mice were transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI. A subsequent set of mice received SL-TBI (1 × 500 cGy) without a subsequent cell transplant. In e, the mice were transplanted with 5 × 10 4 to 5 × 10 5 lineage depleted GFP cells. All groups are compared with transplant only control (*P

    Journal: Nature biotechnology

    Article Title: Scaffolds that induce bone marrow-like features to enhance T-cell immunity in vivo after hematopoietic stem cell transplantation.

    doi: 10.1038/s41587-019-0017-2

    Figure Lengend Snippet: In vivo recruitment of donor cells to BMC and enhanced seeding of thymic progenitors. (a) Total number and type of donor derived, GFP + cells in the BMC containing combinations of BMP-2 and DLL-4 and blank BMCs. (b) Absolute number of donor GFP + CLPs and the percentage of Ly6D - CLPs in BMP-2- and dual factor- BMCs. (c) Schematic of experimental setup for surgical transplantation of harvested BMCs from post-HSCT mice into sub-lethally irradiated mice. (d) DP, SP CD4 + and SP CD8 + cells quantified in the thymus 20-days post surgical transplantation of BMC. (e) Total number of early T-lineage progenitors (ETP; CD44 + CD25 − c-kit + ) quantified as a function of lineage-depleted transplanted cell dose compared with BMC treatment with the lowest cell dose at multiple time points post transplant with representative FACS plots (five experimental replicates at each time point, 2 independent experiments). (f-k) Total number of early T-lineage progenitors (ETP; CD44 + CD25 − c-kit + ), DN2 (CD44 + CD25 − ), DN3 (CD44 + CD25 − ), DP, SP4, SP8 thymocyte subsets compared across different treatment conditions at multiple time points post transplant. For a, b, f-k the mice were transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI (1 × 1000 cGy). In c, d an initial set of mice were transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI. A subsequent set of mice received SL-TBI (1 × 500 cGy) without a subsequent cell transplant. In e, the mice were transplanted with 5 × 10 4 to 5 × 10 5 lineage depleted GFP cells. All groups are compared with transplant only control (*P

    Article Snippet: BMP-2 (R & D Systems) was added to the polymer solution before cryopolymerization.

    Techniques: In Vivo, Derivative Assay, Transplantation Assay, Mouse Assay, Irradiation, FACS

    In vivo deployment and host integration of BMCs. (a) Schedule of administration of L-TBI, HSCT and simultaneous injection of the BMCs. B6 mice were irradiated with 1000 cGy (1 dose) and subsequently transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI. (b) The volume of the BMC nodule in vivo as a function of time post-delivery with various combinations of the BMP-2 and DLL-4 included in the BMC. (c) Confocal microscopy image of donor GFP+ cells (green) identified within the BMC (red) (d) Representative microcomputed tomography (microCT, scale bar = 1mm) imaging and (e) histology (scale bar = 1mm) of the dual functionalized BMC at 3 weeks post injection with the bone shell (green arrow) and the hematopoietic tissue (yellow arrow). (f) Images of the BMC (blue) in the subcutaneous tissue at various timepoints post-injection. (g) Histological Verhoeff–Van Gieson stained sections of the BMC with blood vessels identified (blue arrows) at Day 10, 30, 40 and 90 post-transplant and (h) quantification of the blood vessel density within these sections. (i) Histological Safranin-O stained sections of the BMC with alginate identified (red thread-like staining) at Day 10, 20, 40, 60 and 90 post-transplant and (j) quantification of the accessible area of alginate within these sections. Data in b represent the mean ± s.d. of five experimental replicates and are representative of two independent experiments. (*P

    Journal: Nature biotechnology

    Article Title: Scaffolds that induce bone marrow-like features to enhance T-cell immunity in vivo after hematopoietic stem cell transplantation.

    doi: 10.1038/s41587-019-0017-2

    Figure Lengend Snippet: In vivo deployment and host integration of BMCs. (a) Schedule of administration of L-TBI, HSCT and simultaneous injection of the BMCs. B6 mice were irradiated with 1000 cGy (1 dose) and subsequently transplanted with 5 × 10 5 lineage depleted syngeneic GFP BM cells within 48 hours after L-TBI. (b) The volume of the BMC nodule in vivo as a function of time post-delivery with various combinations of the BMP-2 and DLL-4 included in the BMC. (c) Confocal microscopy image of donor GFP+ cells (green) identified within the BMC (red) (d) Representative microcomputed tomography (microCT, scale bar = 1mm) imaging and (e) histology (scale bar = 1mm) of the dual functionalized BMC at 3 weeks post injection with the bone shell (green arrow) and the hematopoietic tissue (yellow arrow). (f) Images of the BMC (blue) in the subcutaneous tissue at various timepoints post-injection. (g) Histological Verhoeff–Van Gieson stained sections of the BMC with blood vessels identified (blue arrows) at Day 10, 30, 40 and 90 post-transplant and (h) quantification of the blood vessel density within these sections. (i) Histological Safranin-O stained sections of the BMC with alginate identified (red thread-like staining) at Day 10, 20, 40, 60 and 90 post-transplant and (j) quantification of the accessible area of alginate within these sections. Data in b represent the mean ± s.d. of five experimental replicates and are representative of two independent experiments. (*P

    Article Snippet: BMP-2 (R & D Systems) was added to the polymer solution before cryopolymerization.

    Techniques: In Vivo, Injection, Mouse Assay, Irradiation, Confocal Microscopy, Imaging, Staining

    Quantitative analysis of T-cell output, the immune repertoire and vaccination in mice with regenerated T-cells. T-cell receptor excision circle analysis from the (a) isolated thymus and (b) spleen in mice. (c) The diversity in antigen receptors of T-cells as analyzed by the sequenced V and J segments of the CDR3 beta chain in the BMC and transplant mice. Each bar represents a single clone. The plot provides depth (length of bar) and diversity (number of bars) of T-cells in the mice. Samples were pooled from five mice for each group and the combined data are represented. (d) Schedule of analyzing antigen-specific donor T-cell response through vaccination. (e) Donor SIINFEKL + CD8 + T-cells enumerated in vaccinated mice after syn-HSCT and (f) allo-HSCT. (g, h) At day 22 and 42 after HSCT, splenocytes of the OP9-DL1 T-cell precursor group and the dual-BMC treated group were stimulated and stained for surface markers and intracellular cytokines using antibodies specific for CD45.1, CD4, IFN-γ and TNF-α. Cells were gated on CD4 + or CD8 + donor cells, and analyzed for IFN-γ– and TNF-α–positive cells. In a-c and e, B6 recipients received 1000 cGy L-TBI and 5 × 10 5 lineage depleted syngeneic GFP BM cells. Post-HSCT mice with no BMC (Transplant only), post-HSCT mice treated with a BMP-2 BMC, and post-HSCT mice treated with a Dual BMC were analyzed and compared with non-irradiated mice that had not received a transplant or vaccine. In (f-h) Balb/cJ recipient mice received 850Gy L-TBI and were either provided OP9-DL1 culture derived 5 × 10 6 allogeneic GFP T-cell progenitors + 10 3 syngeneic HSCs or dual BMC + 5 × 10 5 lineage depleted allogeneic GFP BM cells. Data in a, b are mean ± s.d. of n = 10 mice, data in e, f are mean ± s.d. of n = 5 mice, data in (g, h) are mean ± s.d. of n = 7 mice. All experiments are representative of two independent experiments. (*P

    Journal: Nature biotechnology

    Article Title: Scaffolds that induce bone marrow-like features to enhance T-cell immunity in vivo after hematopoietic stem cell transplantation.

    doi: 10.1038/s41587-019-0017-2

    Figure Lengend Snippet: Quantitative analysis of T-cell output, the immune repertoire and vaccination in mice with regenerated T-cells. T-cell receptor excision circle analysis from the (a) isolated thymus and (b) spleen in mice. (c) The diversity in antigen receptors of T-cells as analyzed by the sequenced V and J segments of the CDR3 beta chain in the BMC and transplant mice. Each bar represents a single clone. The plot provides depth (length of bar) and diversity (number of bars) of T-cells in the mice. Samples were pooled from five mice for each group and the combined data are represented. (d) Schedule of analyzing antigen-specific donor T-cell response through vaccination. (e) Donor SIINFEKL + CD8 + T-cells enumerated in vaccinated mice after syn-HSCT and (f) allo-HSCT. (g, h) At day 22 and 42 after HSCT, splenocytes of the OP9-DL1 T-cell precursor group and the dual-BMC treated group were stimulated and stained for surface markers and intracellular cytokines using antibodies specific for CD45.1, CD4, IFN-γ and TNF-α. Cells were gated on CD4 + or CD8 + donor cells, and analyzed for IFN-γ– and TNF-α–positive cells. In a-c and e, B6 recipients received 1000 cGy L-TBI and 5 × 10 5 lineage depleted syngeneic GFP BM cells. Post-HSCT mice with no BMC (Transplant only), post-HSCT mice treated with a BMP-2 BMC, and post-HSCT mice treated with a Dual BMC were analyzed and compared with non-irradiated mice that had not received a transplant or vaccine. In (f-h) Balb/cJ recipient mice received 850Gy L-TBI and were either provided OP9-DL1 culture derived 5 × 10 6 allogeneic GFP T-cell progenitors + 10 3 syngeneic HSCs or dual BMC + 5 × 10 5 lineage depleted allogeneic GFP BM cells. Data in a, b are mean ± s.d. of n = 10 mice, data in e, f are mean ± s.d. of n = 5 mice, data in (g, h) are mean ± s.d. of n = 7 mice. All experiments are representative of two independent experiments. (*P

    Article Snippet: BMP-2 (R & D Systems) was added to the polymer solution before cryopolymerization.

    Techniques: Mouse Assay, Isolation, Staining, Irradiation, Derivative Assay

    BMP signalling pathway is not affected by PAWS1 Expression of pSMAD1 in dissociated animals cap cells. Embryos were injected into the animal pole of both blastomeres at the two‐cell stage with a total of either 1 ng of BMP4 or 1 ng BMP4 and 500 pg of Myc‐tagged(MT)xPAWS1 mRNAs. Dissociated cells were stained with antibodies against MYC‐tag (xPAWS1, green) and for phospho‐SMAD1 (p‐SMAD1, red). Scale bars are 50 μm. Expression of ventral markers in animal caps cells injected at the two‐cell stage with a total of either 1 ng of BMP4 or 1 ng BMP4 and 500 pg of MTxPAWS1 mRNA ( n = 3, error bars represent ± SD, ns—not significant, t ‐test, unpaired, two‐tailed with unequal variance). U2OS wild‐type (WT), PAWS1 −/− and PAWS1 WT rescue cells were serum‐deprived for 16 h. Cells were subsequently stimulated with either 6.25 ng/ml BMP2 or 50 pM TGFβ1 for 1 h prior to lysis. Cell extracts (15 μg) were resolved by SDS–PAGE and immunoblotted with the indicated antibodies. Note that the upper band in the P‐SMAD3 blot is a result of the antibody cross‐reacting with P‐SMAD1. Source data are available online for this figure.

    Journal: EMBO Reports

    Article Title: PAWS1 controls Wnt signalling through association with casein kinase 1α

    doi: 10.15252/embr.201744807

    Figure Lengend Snippet: BMP signalling pathway is not affected by PAWS1 Expression of pSMAD1 in dissociated animals cap cells. Embryos were injected into the animal pole of both blastomeres at the two‐cell stage with a total of either 1 ng of BMP4 or 1 ng BMP4 and 500 pg of Myc‐tagged(MT)xPAWS1 mRNAs. Dissociated cells were stained with antibodies against MYC‐tag (xPAWS1, green) and for phospho‐SMAD1 (p‐SMAD1, red). Scale bars are 50 μm. Expression of ventral markers in animal caps cells injected at the two‐cell stage with a total of either 1 ng of BMP4 or 1 ng BMP4 and 500 pg of MTxPAWS1 mRNA ( n = 3, error bars represent ± SD, ns—not significant, t ‐test, unpaired, two‐tailed with unequal variance). U2OS wild‐type (WT), PAWS1 −/− and PAWS1 WT rescue cells were serum‐deprived for 16 h. Cells were subsequently stimulated with either 6.25 ng/ml BMP2 or 50 pM TGFβ1 for 1 h prior to lysis. Cell extracts (15 μg) were resolved by SDS–PAGE and immunoblotted with the indicated antibodies. Note that the upper band in the P‐SMAD3 blot is a result of the antibody cross‐reacting with P‐SMAD1. Source data are available online for this figure.

    Article Snippet: Recombinant TGFβ1 and BMP2 were purchased from R & D Systems.

    Techniques: Expressing, Injection, Staining, Two Tailed Test, Lysis, SDS Page

    Silencing results for RFP and GFP expressed by the Plux-RG and Plux-GR synthetic operons in the TOP10 strain. a Silencing of the target gene (RFP) and the non-target gene (GFP) via the silencing device sRFP. b Unspecific silencing of RFP and GFP, in the

    Journal: Systems and Synthetic Biology

    Article Title: Quantification of the gene silencing performances of rationally-designed synthetic small RNAs

    doi: 10.1007/s11693-015-9177-7

    Figure Lengend Snippet: Silencing results for RFP and GFP expressed by the Plux-RG and Plux-GR synthetic operons in the TOP10 strain. a Silencing of the target gene (RFP) and the non-target gene (GFP) via the silencing device sRFP. b Unspecific silencing of RFP and GFP, in the

    Article Snippet: The E. coli TOP10 (Invitrogen) strain was used for cloning.

    Techniques:

    Lactate dehydrogenase assay results for sLDH characterization in TOP10 and W. Specific enzymatic activity of LdhA in the strain without sRNA, in the strain with an unspecific sRNA (sRFP) and in the strain with the sRNA targeting LdhA (sLDH). Bars represent

    Journal: Systems and Synthetic Biology

    Article Title: Quantification of the gene silencing performances of rationally-designed synthetic small RNAs

    doi: 10.1007/s11693-015-9177-7

    Figure Lengend Snippet: Lactate dehydrogenase assay results for sLDH characterization in TOP10 and W. Specific enzymatic activity of LdhA in the strain without sRNA, in the strain with an unspecific sRNA (sRFP) and in the strain with the sRNA targeting LdhA (sLDH). Bars represent

    Article Snippet: The E. coli TOP10 (Invitrogen) strain was used for cloning.

    Techniques: Lactate Dehydrogenase Assay, Activity Assay

    Silencing results for RFP or GFP expressed by a single-gene cassette driven by P lux (Plux-R or Plux-G). a Specific silencing of the target gene (RFP) via sRFP in TOP10 and W. b Unspecific silencing of RFP or GFP via different sRNAs in TOP10 and W. Bars

    Journal: Systems and Synthetic Biology

    Article Title: Quantification of the gene silencing performances of rationally-designed synthetic small RNAs

    doi: 10.1007/s11693-015-9177-7

    Figure Lengend Snippet: Silencing results for RFP or GFP expressed by a single-gene cassette driven by P lux (Plux-R or Plux-G). a Specific silencing of the target gene (RFP) via sRFP in TOP10 and W. b Unspecific silencing of RFP or GFP via different sRNAs in TOP10 and W. Bars

    Article Snippet: The E. coli TOP10 (Invitrogen) strain was used for cloning.

    Techniques:

    Silencing results for RFP expressed by a single-gene cassette driven by BBa_J23101 (J101-R). a Specific silencing of the target gene (RFP) via the specific silencing device (sRFP) in TOP10 and W. b Experimental S cell results and values predicted by the

    Journal: Systems and Synthetic Biology

    Article Title: Quantification of the gene silencing performances of rationally-designed synthetic small RNAs

    doi: 10.1007/s11693-015-9177-7

    Figure Lengend Snippet: Silencing results for RFP expressed by a single-gene cassette driven by BBa_J23101 (J101-R). a Specific silencing of the target gene (RFP) via the specific silencing device (sRFP) in TOP10 and W. b Experimental S cell results and values predicted by the

    Article Snippet: The E. coli TOP10 (Invitrogen) strain was used for cloning.

    Techniques:

    RFP silencing as a function of target mRNA and sRNA levels in TOP10 with the Plux-R construct. Data points represent average S cell values in presence of sRFP in three different copy number conditions (corresponding to three different sRFP levels), as

    Journal: Systems and Synthetic Biology

    Article Title: Quantification of the gene silencing performances of rationally-designed synthetic small RNAs

    doi: 10.1007/s11693-015-9177-7

    Figure Lengend Snippet: RFP silencing as a function of target mRNA and sRNA levels in TOP10 with the Plux-R construct. Data points represent average S cell values in presence of sRFP in three different copy number conditions (corresponding to three different sRFP levels), as

    Article Snippet: The E. coli TOP10 (Invitrogen) strain was used for cloning.

    Techniques: Construct

    Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli BL21. Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Journal: Vaccines

    Article Title: Gut Microbiota Abrogates Anti-α-Gal IgA Response in Lungs and Protects against Experimental Aspergillus Infection in Poultry

    doi: 10.3390/vaccines8020285

    Figure Lengend Snippet: Oral administration of E. coli O86:B7 induces a significant decrease in the levels of anti-Galα1-3Galβ1-4GlcNAc IgY Abs in A. fumigatus -infected turkeys. The levels of circulating anti-α-Gal IgY Abs to Galα1-3Gal ( A ) and Galα1-3Galβ1-4GlcNAc ( B ) were measured by ELISA. Anti-Galα1-3Gal IgY Abs increased in the sera of turkeys treated with E. coli O86:B7 and E. coli BL21. Oral administration of E. coli O86:B7 produces a significant reduction in anti-Galα1-3Galβ1-4GlcNAc IgY Abs when compared with turkeys that were treated or not E. coli BL21. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Article Snippet: Bacteria Culture and Oral Administration of Bacteria The bacterium E. coli O86:B7 (ATCC 12701) expresses high levels of α-Gal on its surface [ , ], which is not the case for E. coli BL21 (DE3, Invitrogen, Carlsbad, CA, USA) [ ].

    Techniques: Infection, Enzyme-linked Immunosorbent Assay, Standard Deviation

    Oral administration of E. coli O86:B7 protects turkeys against aspergillosis. Clinical examination revealed that A. fumigatus infection produces open-mouthed breathing (OMB) in turkeys treated with PBS or E. coli BL21. Turkeys treated with E. coli O86:B7 were protected from developing OMB ( A ). Pulmonary lesions (i.e., granulomas, delimited area and white arrow heads) were scored (see methods). Examples of lungs with scores 0 to 3 are shown ( B ). Granuloma score was lower in turkeys treated with E. coli O86:B7 ( C ). Lung samples were processed for histopathology and stained with hematoxylin-eosin-saffron (HES, D ) and periodic acid-schiff (PAS, E ). Histological lesions were scored (see methods). Examples of histopathology samples with scores 0 to 3 are shown. Visible peribronchial regions (asterisk) and granulomas (delimited area and black arrow heads) are shown (HES score, D ). The presence of fungal germ-tube/hyphae (black arrows) and mycelium (white arrows) was scored (see methods). Granulomas associated with fungal hyphae (delimited area and black arrow heads) are shown (PAS score, E ). HES and PAS scores were lower in turkeys treated with E. coli O86:B7 ( F , G ). The presence of viable Aspergillus in lungs was quantified by colony-forming unit (CFU) counting assay ( H ). Fungal DNA levels were measured by A. fumigatus -specific 28S qPCR normalizing against turkey actb and gapdh as host genes using the 2 −ΔΔ C t ratio method. Results are relative to 28S levels in the control group (i.e., PBS) ( I ). No significant change was observed in the amount of CFU and 28S fold change ( H , I ). Size of bars is indicated. 100X magnification. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (*** p

    Journal: Vaccines

    Article Title: Gut Microbiota Abrogates Anti-α-Gal IgA Response in Lungs and Protects against Experimental Aspergillus Infection in Poultry

    doi: 10.3390/vaccines8020285

    Figure Lengend Snippet: Oral administration of E. coli O86:B7 protects turkeys against aspergillosis. Clinical examination revealed that A. fumigatus infection produces open-mouthed breathing (OMB) in turkeys treated with PBS or E. coli BL21. Turkeys treated with E. coli O86:B7 were protected from developing OMB ( A ). Pulmonary lesions (i.e., granulomas, delimited area and white arrow heads) were scored (see methods). Examples of lungs with scores 0 to 3 are shown ( B ). Granuloma score was lower in turkeys treated with E. coli O86:B7 ( C ). Lung samples were processed for histopathology and stained with hematoxylin-eosin-saffron (HES, D ) and periodic acid-schiff (PAS, E ). Histological lesions were scored (see methods). Examples of histopathology samples with scores 0 to 3 are shown. Visible peribronchial regions (asterisk) and granulomas (delimited area and black arrow heads) are shown (HES score, D ). The presence of fungal germ-tube/hyphae (black arrows) and mycelium (white arrows) was scored (see methods). Granulomas associated with fungal hyphae (delimited area and black arrow heads) are shown (PAS score, E ). HES and PAS scores were lower in turkeys treated with E. coli O86:B7 ( F , G ). The presence of viable Aspergillus in lungs was quantified by colony-forming unit (CFU) counting assay ( H ). Fungal DNA levels were measured by A. fumigatus -specific 28S qPCR normalizing against turkey actb and gapdh as host genes using the 2 −ΔΔ C t ratio method. Results are relative to 28S levels in the control group (i.e., PBS) ( I ). No significant change was observed in the amount of CFU and 28S fold change ( H , I ). Size of bars is indicated. 100X magnification. Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (*** p

    Article Snippet: Bacteria Culture and Oral Administration of Bacteria The bacterium E. coli O86:B7 (ATCC 12701) expresses high levels of α-Gal on its surface [ , ], which is not the case for E. coli BL21 (DE3, Invitrogen, Carlsbad, CA, USA) [ ].

    Techniques: Infection, Histopathology, Staining, Real-time Polymerase Chain Reaction, Standard Deviation

    Expression of turkey and chicken cytokine genes in response to oral administration of E. coli O86:B7 and E. coli BL21 and α-Gal-BSA immunization. The figure displays the mRNA expression levels of INFγ , IL6 , IL2 , IL10 and MyD88 in ceca ( A ) and lungs ( B ) of turkeys and IL6 and IL2 in lungs of chicken ( C ). Total RNA was extracted and gene expression levels were measured by qPCR normalizing against turkey actb and gapdh as housekeeping genes, using the using the 2 −ΔΔ C t ratio method. Expression levels are relative to the control group (i.e., PBS). Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Journal: Vaccines

    Article Title: Gut Microbiota Abrogates Anti-α-Gal IgA Response in Lungs and Protects against Experimental Aspergillus Infection in Poultry

    doi: 10.3390/vaccines8020285

    Figure Lengend Snippet: Expression of turkey and chicken cytokine genes in response to oral administration of E. coli O86:B7 and E. coli BL21 and α-Gal-BSA immunization. The figure displays the mRNA expression levels of INFγ , IL6 , IL2 , IL10 and MyD88 in ceca ( A ) and lungs ( B ) of turkeys and IL6 and IL2 in lungs of chicken ( C ). Total RNA was extracted and gene expression levels were measured by qPCR normalizing against turkey actb and gapdh as housekeeping genes, using the using the 2 −ΔΔ C t ratio method. Expression levels are relative to the control group (i.e., PBS). Results shown are means and standard deviation values. Results were compared by One-way ANOVA with Dunnett’s multiple comparison test applied for individual comparisons (* p

    Article Snippet: Bacteria Culture and Oral Administration of Bacteria The bacterium E. coli O86:B7 (ATCC 12701) expresses high levels of α-Gal on its surface [ , ], which is not the case for E. coli BL21 (DE3, Invitrogen, Carlsbad, CA, USA) [ ].

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Standard Deviation

    SDS-PAGE analysis of purified protein recombinant SllB in E. coli BL21 cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: SDS-PAGE analysis of purified protein recombinant SllB in E. coli BL21 cells. Lane M: Takara Protein Marker; lane 1, SDS-PAGE analysis of the recombinant S-layer protein before purification; lane 2, SDS-PAGE analysis of the purified recombinant protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: SDS Page, Purification, Recombinant, Marker

    A transmission electron microscopic observation on the E. coli BL21 with recombinant protein. (A) Normal E. coli BL21 was treated as control. (B) The E. coli BL21 cells recombinant S-layer protein. (C) Crystal lattice structures on surface of the E. coli BL21 cells recombinant S-layer protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: A transmission electron microscopic observation on the E. coli BL21 with recombinant protein. (A) Normal E. coli BL21 was treated as control. (B) The E. coli BL21 cells recombinant S-layer protein. (C) Crystal lattice structures on surface of the E. coli BL21 cells recombinant S-layer protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: Transmission Assay, Recombinant

    Expression of sllB in E. coli BL21 cells. (A) SDS-PAGE analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; lane M represent Takara Protein Marker (Broad). (B) Western blot analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; M, Takara Protein Marker (Broad). Lane M1, Precision plus protein standards; lane M2, perfect protein marker. Note the band pointed with arrows is the recombinant S-layer protein.

    Journal: International Journal of Molecular Medicine

    Article Title: Cloning of the surface layer gene sllB from Bacillus sphaericus ATCC 14577 and its heterologous expression and purification

    doi: 10.3892/ijmm.2012.890

    Figure Lengend Snippet: Expression of sllB in E. coli BL21 cells. (A) SDS-PAGE analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; lane M represent Takara Protein Marker (Broad). (B) Western blot analysis of rSllB protein; lane 1, the whole cell lysate of E. coli BL21 cells containing pET28a(+); lane 2, the supernatant of cells containing pET28a(+); lane 3, the pellet of cells containing pET28a(+); lane 4, the whole cell lysate of E. coli BL21 cells containing pET28a(+)- sllB ; lane 5, the supernatant of cell containing pET28a(+)- sllB ; lane 6, the pellet of cells containing pET28a(+)- sllB ; M, Takara Protein Marker (Broad). Lane M1, Precision plus protein standards; lane M2, perfect protein marker. Note the band pointed with arrows is the recombinant S-layer protein.

    Article Snippet: 2.0 (Takara, no. DV801A), from which 0.5 μl was used to transform 100 μl of E. coli BL21 (DE3, Stratagene).

    Techniques: Expressing, SDS Page, Marker, Western Blot, Recombinant

    Immunoblot showing OmpL1 expression at different IPTG concentrations. A culture of E. coli XL1-Blue containing plasmid pMMB66-OmpL1 was grown to log phase, separated into four equal volumes, and treated with various concentrations of IPTG. Cells were incubated for an additional 3 h in a shaker incubator at 37°C, pelleted in a microcentrifuge, resuspended in final sample buffer, and analyzed by SDS-PAGE and immunoblotting. A companion SDS-polyacrylamide gel loaded with the same four samples was stained with Coomassie brilliant blue to verify that all four lanes contained comparable amounts of material (data not shown). The locations of molecular size standards are shown (in kilodaltons) on the left. Even though use of the tac promoter typically results in relatively high background expression levels, expression using plasmid pMMB66-OmpL1 was not detectable without IPTG induction.

    Journal: Infection and Immunity

    Article Title: Leptospiral Outer Membrane Proteins OmpL1 and LipL41 Exhibit Synergistic Immunoprotection

    doi:

    Figure Lengend Snippet: Immunoblot showing OmpL1 expression at different IPTG concentrations. A culture of E. coli XL1-Blue containing plasmid pMMB66-OmpL1 was grown to log phase, separated into four equal volumes, and treated with various concentrations of IPTG. Cells were incubated for an additional 3 h in a shaker incubator at 37°C, pelleted in a microcentrifuge, resuspended in final sample buffer, and analyzed by SDS-PAGE and immunoblotting. A companion SDS-polyacrylamide gel loaded with the same four samples was stained with Coomassie brilliant blue to verify that all four lanes contained comparable amounts of material (data not shown). The locations of molecular size standards are shown (in kilodaltons) on the left. Even though use of the tac promoter typically results in relatively high background expression levels, expression using plasmid pMMB66-OmpL1 was not detectable without IPTG induction.

    Article Snippet: OmpL1-M was expressed in E. coli XL1-Blue (Stratagene), using plasmid pMMB66-OmpL1.

    Techniques: Expressing, Plasmid Preparation, Incubation, SDS Page, Staining

    Coomassie brilliant blue-stained SDS-polyacrylamide gel showing material representative of E. coli membrane fractions used to immunize hamsters. Lanes: 1 and 2, E. coli XL1-Blue with plasmids pMMB66 and pMMB66-OmpL1, respectively; 3 and 4, E. coli JM109(DE3) with plasmids pET15b and pET15b-LipL41*, respectively. Locations of the OmpL1 doublet in lane 2 and of LipL41 in lane 4 are shown (arrowheads). Positions of molecular size markers (M) are given in kilodaltons.

    Journal: Infection and Immunity

    Article Title: Leptospiral Outer Membrane Proteins OmpL1 and LipL41 Exhibit Synergistic Immunoprotection

    doi:

    Figure Lengend Snippet: Coomassie brilliant blue-stained SDS-polyacrylamide gel showing material representative of E. coli membrane fractions used to immunize hamsters. Lanes: 1 and 2, E. coli XL1-Blue with plasmids pMMB66 and pMMB66-OmpL1, respectively; 3 and 4, E. coli JM109(DE3) with plasmids pET15b and pET15b-LipL41*, respectively. Locations of the OmpL1 doublet in lane 2 and of LipL41 in lane 4 are shown (arrowheads). Positions of molecular size markers (M) are given in kilodaltons.

    Article Snippet: OmpL1-M was expressed in E. coli XL1-Blue (Stratagene), using plasmid pMMB66-OmpL1.

    Techniques: Staining

    Mucosal-associated invariant T (MAIT) cells are activated by pneumococci. A , Gating strategy for analysis of MAIT cell–derived interferon γ (IFN-γ) following activation of peripheral blood mononuclear cells. B , Example fluorescence-activated cell-sorting plots showing upregulation of CD69 and IFN-γ in unstimulated and stimulated MAIT cells (gating on CD3 + CD8 + live T cells). C and D , Ten Pneumococcal Molecular Epidemiological Network (PMEN) reference strains were used to probe the activation of MAIT cells following coculture of peripheral blood mononuclear cells in the presence of the monocytic cell line, THP1. Escherichia coli was added as a positive control. Frequency of cells expressing IFN-γ among MAIT cells ( C ) or CD161 − CD8 + T cells ( D ) are shown (n = 9). E and F , CD69 expression measured by geometric mean fluorescence intensity (gMFI) in MAIT cells ( E ) or CD161 − CD8 + T cells ( F ) are shown (n = 6). ** P

    Journal: The Journal of Infectious Diseases

    Article Title: Diverse Streptococcus pneumoniae Strains Drive a Mucosal-Associated Invariant T-Cell Response Through Major Histocompatibility Complex class I–Related Molecule–Dependent and Cytokine-Driven Pathways

    doi: 10.1093/infdis/jix647

    Figure Lengend Snippet: Mucosal-associated invariant T (MAIT) cells are activated by pneumococci. A , Gating strategy for analysis of MAIT cell–derived interferon γ (IFN-γ) following activation of peripheral blood mononuclear cells. B , Example fluorescence-activated cell-sorting plots showing upregulation of CD69 and IFN-γ in unstimulated and stimulated MAIT cells (gating on CD3 + CD8 + live T cells). C and D , Ten Pneumococcal Molecular Epidemiological Network (PMEN) reference strains were used to probe the activation of MAIT cells following coculture of peripheral blood mononuclear cells in the presence of the monocytic cell line, THP1. Escherichia coli was added as a positive control. Frequency of cells expressing IFN-γ among MAIT cells ( C ) or CD161 − CD8 + T cells ( D ) are shown (n = 9). E and F , CD69 expression measured by geometric mean fluorescence intensity (gMFI) in MAIT cells ( E ) or CD161 − CD8 + T cells ( F ) are shown (n = 6). ** P

    Article Snippet: Escherichia coli (DH5a; Invitrogen) was cultured in LB medium overnight in a shaking incubator.

    Techniques: Derivative Assay, Activation Assay, Fluorescence, FACS, Positive Control, Expressing

    Mucosal-associated invariant T (MAIT) cell activation by pneumococci in presence of monocytes is not MR1-dependent. A , Paraformaldehyde-fixed Pneumococcal Molecular Epidemiological Network (PMEN) reference strains or Escherichia coli were cultured with peripheral blood mononuclear cells and THP1 cells in the presence of anti-MR1 blocking, anti–interleukin 12 (IL-12), and anti–interleukin 18 (IL-18) blocking antibodies. Interferon γ (IFN-γ) expression from MAIT cells is shown. **** P

    Journal: The Journal of Infectious Diseases

    Article Title: Diverse Streptococcus pneumoniae Strains Drive a Mucosal-Associated Invariant T-Cell Response Through Major Histocompatibility Complex class I–Related Molecule–Dependent and Cytokine-Driven Pathways

    doi: 10.1093/infdis/jix647

    Figure Lengend Snippet: Mucosal-associated invariant T (MAIT) cell activation by pneumococci in presence of monocytes is not MR1-dependent. A , Paraformaldehyde-fixed Pneumococcal Molecular Epidemiological Network (PMEN) reference strains or Escherichia coli were cultured with peripheral blood mononuclear cells and THP1 cells in the presence of anti-MR1 blocking, anti–interleukin 12 (IL-12), and anti–interleukin 18 (IL-18) blocking antibodies. Interferon γ (IFN-γ) expression from MAIT cells is shown. **** P

    Article Snippet: Escherichia coli (DH5a; Invitrogen) was cultured in LB medium overnight in a shaking incubator.

    Techniques: Activation Assay, Cell Culture, Blocking Assay, Expressing