canine distemper virus cdv strain lederle  (ATCC)


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    ATCC canine distemper virus cdv strain lederle
    Canine Distemper Virus Cdv Strain Lederle, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    canine distemper virus cdv strain lederle  (ATCC)


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    ATCC canine distemper virus cdv strain lederle
    Canine Distemper Virus Cdv Strain Lederle, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    mbics  (ATCC)


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    ATCC mbics
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    pmm 128  (ATCC)


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    ATCC pmm 128
    List of strains used as challenge organisms for biltong processing in this study.
    Pmm 128, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Evaluation of Various Lactic Acid Bacteria and Generic E. coli as Potential Nonpathogenic Surrogates for In-Plant Validation of Biltong Dried Beef Processing"

    Article Title: Evaluation of Various Lactic Acid Bacteria and Generic E. coli as Potential Nonpathogenic Surrogates for In-Plant Validation of Biltong Dried Beef Processing

    Journal: Microorganisms

    doi: 10.3390/microorganisms10081648

    List of strains used as challenge organisms for biltong processing in this study.
    Figure Legend Snippet: List of strains used as challenge organisms for biltong processing in this study.

    Techniques Used: Isolation

    novobiocin 128  (ATCC)


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    ATCC novobiocin 128
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    128 32 a baumannii b189 17 b 128  (ATCC)


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    ATCC 128 32 a baumannii b189 17 b 128
    MICs in iron-limited BM2 medium
    128 32 A Baumannii B189 17 B 128, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Iron/Heme Metabolism-Targeted Gallium(III) Nanoparticles Are Active against Extracellular and Intracellular Pseudomonas aeruginosa and Acinetobacter baumannii"

    Article Title: Iron/Heme Metabolism-Targeted Gallium(III) Nanoparticles Are Active against Extracellular and Intracellular Pseudomonas aeruginosa and Acinetobacter baumannii

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.02643-18

    MICs in iron-limited BM2 medium
    Figure Legend Snippet: MICs in iron-limited BM2 medium

    Techniques Used:

    vaccinia virus 128 dryvax  (ATCC)


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    ATCC vaccinia virus 128 dryvax
    Vaccinia Virus 128 Dryvax, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    sensitive 128 8  (ATCC)


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    ATCC sensitive 128 8
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    type 21  (ATCC)


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    ATCC type 21
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    chicken embryos  (ATCC)


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    ATCC chicken embryos
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    cdv strain lederle  (ATCC)


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    ATCC cdv strain lederle
    Transferring a linear domain of five <t>CDV</t> residues into the H stalk renders MV H capable of activating <t>CDV</t> <t>F-Lederle.</t> A, amino acid sequence alignment of a 49 residue-stretch in the H stalk domain identified in B to mediate specificity of MV H for CDV F-Lederle. The bold letters indicate residues that differ between the H variants. B, a minimal CDV H-derived microdomain spanning residues 110–114 is required for CDV F-Lederle activation by MV H variants. Quantitative fusion assays of cells co-transfected with CDV F-Lederle or MV F and MV H variants as specified below the graph. The values are expressed as the percentages of activity upon co-transfection of CDV F-Lederle or MV F with chimeric MV H (1–138 CDV) covering the area under investigation. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. C, hemadsorption activity of selected H constructs. Roman numerals specify the H variants introduced in B. The values are averages of two independent experiments; the error bars represent the range observed.
    Cdv Strain Lederle, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Functional Interaction between Paramyxovirus Fusion and Attachment Proteins"

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M801018200

    Transferring a linear domain of five CDV residues into the H stalk renders MV H capable of activating CDV F-Lederle. A, amino acid sequence alignment of a 49 residue-stretch in the H stalk domain identified in B to mediate specificity of MV H for CDV F-Lederle. The bold letters indicate residues that differ between the H variants. B, a minimal CDV H-derived microdomain spanning residues 110–114 is required for CDV F-Lederle activation by MV H variants. Quantitative fusion assays of cells co-transfected with CDV F-Lederle or MV F and MV H variants as specified below the graph. The values are expressed as the percentages of activity upon co-transfection of CDV F-Lederle or MV F with chimeric MV H (1–138 CDV) covering the area under investigation. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. C, hemadsorption activity of selected H constructs. Roman numerals specify the H variants introduced in B. The values are averages of two independent experiments; the error bars represent the range observed.
    Figure Legend Snippet: Transferring a linear domain of five CDV residues into the H stalk renders MV H capable of activating CDV F-Lederle. A, amino acid sequence alignment of a 49 residue-stretch in the H stalk domain identified in B to mediate specificity of MV H for CDV F-Lederle. The bold letters indicate residues that differ between the H variants. B, a minimal CDV H-derived microdomain spanning residues 110–114 is required for CDV F-Lederle activation by MV H variants. Quantitative fusion assays of cells co-transfected with CDV F-Lederle or MV F and MV H variants as specified below the graph. The values are expressed as the percentages of activity upon co-transfection of CDV F-Lederle or MV F with chimeric MV H (1–138 CDV) covering the area under investigation. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. C, hemadsorption activity of selected H constructs. Roman numerals specify the H variants introduced in B. The values are averages of two independent experiments; the error bars represent the range observed.

    Techniques Used: Transferring, Sequencing, Derivative Assay, Activation Assay, Transfection, Activity Assay, Cotransfection, Construct

    CDV F-ODP but not CDV F-Lederle is triggered by MV H. A, microphotographs of Vero-dogSLAM cells co-transfected with equal amounts of plasmid DNA encoding MV or CDV glycoproteins as specified. The cells were photographed at a magnification of 200× after incubation at 37 °C for seven to 11 h. Mock infected cells expressed only the H protein. B, quantification of cell-to-cell fusion activity using a firefly luciferase reporter-based fusion assay. The values reflect the average luciferase activities of at least three independent experiments ± S.D. per glycoprotein combination and are expressed as the percentages of activity measured for MV F and the respective H. C, CDV F glycoprotein variants show different strengths of interaction with MV H. Co-immunoprecipitation of CDVF-ODP and Lederle with MV H. The lysates of co-transfected cells were subjected to immunoprecipitation using specific antibodies directed against an epitope in the MV H ectodomain. Co-precipitated F (upper panel) was detected in comparison with F present in the lysates prior to precipitation (lower panel) by immunoblotting using a specific antiserum directed against an epitope in the cytosolic tail of CDV F.
    Figure Legend Snippet: CDV F-ODP but not CDV F-Lederle is triggered by MV H. A, microphotographs of Vero-dogSLAM cells co-transfected with equal amounts of plasmid DNA encoding MV or CDV glycoproteins as specified. The cells were photographed at a magnification of 200× after incubation at 37 °C for seven to 11 h. Mock infected cells expressed only the H protein. B, quantification of cell-to-cell fusion activity using a firefly luciferase reporter-based fusion assay. The values reflect the average luciferase activities of at least three independent experiments ± S.D. per glycoprotein combination and are expressed as the percentages of activity measured for MV F and the respective H. C, CDV F glycoprotein variants show different strengths of interaction with MV H. Co-immunoprecipitation of CDVF-ODP and Lederle with MV H. The lysates of co-transfected cells were subjected to immunoprecipitation using specific antibodies directed against an epitope in the MV H ectodomain. Co-precipitated F (upper panel) was detected in comparison with F present in the lysates prior to precipitation (lower panel) by immunoblotting using a specific antiserum directed against an epitope in the cytosolic tail of CDV F.

    Techniques Used: Transfection, Plasmid Preparation, Incubation, Infection, Activity Assay, Luciferase, Single Vesicle Fusion Assay, Immunoprecipitation, Western Blot

    Identification of a minimal domain responsible for productive interaction of CDV F variants with MV H. A, quantification of cell-to-cell fusion activity of reciprocal chimeras between CDV F-ODP and Lederle upon co-transfection with MV H (black bars) or CDV H (gray bars) using the luciferase reporter-based fusion assay as outlined in Fig. 1B. The values were normalized for fusion activity observed upon co-transfection of cells with unmodified F-ODP and MV H or CDV H, respectively. The mean values ± S.D. of three independent experiments are shown, and the extent of differential triggering (based on the percentage of homotypic activity/percentage of heterotypic activity) is specified (see text for details). F constructs are schematized below the graph. The black boxes represent regions derived from F-Lederle, and the gray boxes represent F-ODP. The location of characteristic F protein domains, the site of the disulfide bridge linking the F1 and F2 subunits (black line), and the position of natural (BlpI, PvuII, EcoRV, and SmaI) and engineered (BglII and KpnI, in gray) restriction sites used for chimera generation are shown on the left. PS, N-terminal precursor sequence of CDV F; FP, fusion peptide; HR-A, N-terminal heptad repeat; HR-B, C-terminal heptad repeat; TM, transmembrane domain; CT, cytosolic tail. B, focused chimeras based on engineered restriction sites identify a domain in the N-terminal part of F-ODP (between restriction sites KpnI and EcoRV, construct XIII) to determine productive interaction of F-ODP with MV H. Quantification of fusion activity, calculation of differential triggering and color coding as described in A.
    Figure Legend Snippet: Identification of a minimal domain responsible for productive interaction of CDV F variants with MV H. A, quantification of cell-to-cell fusion activity of reciprocal chimeras between CDV F-ODP and Lederle upon co-transfection with MV H (black bars) or CDV H (gray bars) using the luciferase reporter-based fusion assay as outlined in Fig. 1B. The values were normalized for fusion activity observed upon co-transfection of cells with unmodified F-ODP and MV H or CDV H, respectively. The mean values ± S.D. of three independent experiments are shown, and the extent of differential triggering (based on the percentage of homotypic activity/percentage of heterotypic activity) is specified (see text for details). F constructs are schematized below the graph. The black boxes represent regions derived from F-Lederle, and the gray boxes represent F-ODP. The location of characteristic F protein domains, the site of the disulfide bridge linking the F1 and F2 subunits (black line), and the position of natural (BlpI, PvuII, EcoRV, and SmaI) and engineered (BglII and KpnI, in gray) restriction sites used for chimera generation are shown on the left. PS, N-terminal precursor sequence of CDV F; FP, fusion peptide; HR-A, N-terminal heptad repeat; HR-B, C-terminal heptad repeat; TM, transmembrane domain; CT, cytosolic tail. B, focused chimeras based on engineered restriction sites identify a domain in the N-terminal part of F-ODP (between restriction sites KpnI and EcoRV, construct XIII) to determine productive interaction of F-ODP with MV H. Quantification of fusion activity, calculation of differential triggering and color coding as described in A.

    Techniques Used: Activity Assay, Cotransfection, Luciferase, Single Vesicle Fusion Assay, Construct, Derivative Assay, Sequencing

    Four point mutations disrupt productive interaction of CDV F-ODP with MV H. A, amino acid sequence alignment of the identified fragment between the KpnI and EcoRV sites of F-Lederle and ODP. The black letters indicate residues that differ between the strains. The fusion peptide (red) and the relative position of the PvuII site are shown. A vertical line marks the furin cleavage site. B, quantitative comparison of fusion activity of individual F-ODP point mutants. The values are expressed as percentages of fusion activity observed upon co-transfection with unmodified F-ODP and either MV or CDV H. The averages of four experiments ± S.D. and the extent of differential triggering are shown. C, visualization of the identified residues in a structural model of the prefusion CDV F-ODP trimer. In the left panel, all four residues (164, 219, 233, and 317) are highlighted in red. Residues 164, 219, and 233 are predicted to be surface-exposed; residue 317 is predicted to be completely buried in the trimer (visible only in the ribbon models; center panel, side view; right panel, top view). For clarity, residues 164, 219, and 233 are not highlighted in the ribbon models. D, co-immunoprecipitation of selected F-ODP mutant constructs with MV H reveals a limited reduction in co-precipitation efficiency as compared with unmodified F-ODP. The experimental conditions were the same as described for Fig. 1C. The values below the blot represent averages of densitometric quantification of co-precipitated F1 material from two independent experiments. They are corrected for the amount of F1 material present in cell lysates prior to precipitation, which serves as internal standard (lower panel), and are expressed as percentage of co-precipitated CDV F1-ODP.
    Figure Legend Snippet: Four point mutations disrupt productive interaction of CDV F-ODP with MV H. A, amino acid sequence alignment of the identified fragment between the KpnI and EcoRV sites of F-Lederle and ODP. The black letters indicate residues that differ between the strains. The fusion peptide (red) and the relative position of the PvuII site are shown. A vertical line marks the furin cleavage site. B, quantitative comparison of fusion activity of individual F-ODP point mutants. The values are expressed as percentages of fusion activity observed upon co-transfection with unmodified F-ODP and either MV or CDV H. The averages of four experiments ± S.D. and the extent of differential triggering are shown. C, visualization of the identified residues in a structural model of the prefusion CDV F-ODP trimer. In the left panel, all four residues (164, 219, 233, and 317) are highlighted in red. Residues 164, 219, and 233 are predicted to be surface-exposed; residue 317 is predicted to be completely buried in the trimer (visible only in the ribbon models; center panel, side view; right panel, top view). For clarity, residues 164, 219, and 233 are not highlighted in the ribbon models. D, co-immunoprecipitation of selected F-ODP mutant constructs with MV H reveals a limited reduction in co-precipitation efficiency as compared with unmodified F-ODP. The experimental conditions were the same as described for Fig. 1C. The values below the blot represent averages of densitometric quantification of co-precipitated F1 material from two independent experiments. They are corrected for the amount of F1 material present in cell lysates prior to precipitation, which serves as internal standard (lower panel), and are expressed as percentage of co-precipitated CDV F1-ODP.

    Techniques Used: Sequencing, Activity Assay, Cotransfection, Immunoprecipitation, Mutagenesis, Construct

    Residues in an MV H N-terminal domain are determinants for F specificity. A, quantification of fusion activity upon activation of CDV F-Lederle or MV F with CDV H, MV H, or an MV/CDV H chimera specified in the schematic below the graph. The activity was determined as outlined before (Fig. 1A), and the values are expressed as a percentage of activity observed for either CDV F-Lederle or MV F co-expressed with CDV H. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. Stalk, membrane-proximal part of the H ectodomain (up to residue 139); TM, transmembrane domain; CT, cytosolic tail. B, microphotographs of Vero-dogSLAM cells co-transfected with the constructs outlined in A. The pictures were taken 9.5 h post-transfection at a magnification of 200×. Mock transfected cells received only F-encoding plasmid.
    Figure Legend Snippet: Residues in an MV H N-terminal domain are determinants for F specificity. A, quantification of fusion activity upon activation of CDV F-Lederle or MV F with CDV H, MV H, or an MV/CDV H chimera specified in the schematic below the graph. The activity was determined as outlined before (Fig. 1A), and the values are expressed as a percentage of activity observed for either CDV F-Lederle or MV F co-expressed with CDV H. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. Stalk, membrane-proximal part of the H ectodomain (up to residue 139); TM, transmembrane domain; CT, cytosolic tail. B, microphotographs of Vero-dogSLAM cells co-transfected with the constructs outlined in A. The pictures were taken 9.5 h post-transfection at a magnification of 200×. Mock transfected cells received only F-encoding plasmid.

    Techniques Used: Activity Assay, Activation Assay, Transfection, Construct, Plasmid Preparation

    Residues identified in F and H act interdependently. Quantitative (A) and qualitative (B) assessment of fusion activity of cells co-transfected with the CDV F-ODP (residues 164, 219, 233, and 317) variant introduced in Fig. 3B and CDV H, MV H, or chimeras derived thereof as specified. The quantification results are expressed as percentages of activity observed for cells co-expressing CDV F-ODP (residues 164, 219, 233, and 317) and homotypic CDV H. The averages of three independent experiments ± S.D. are shown. The microphotographs were taken 13 h post-transfection at a magnification of 200×.
    Figure Legend Snippet: Residues identified in F and H act interdependently. Quantitative (A) and qualitative (B) assessment of fusion activity of cells co-transfected with the CDV F-ODP (residues 164, 219, 233, and 317) variant introduced in Fig. 3B and CDV H, MV H, or chimeras derived thereof as specified. The quantification results are expressed as percentages of activity observed for cells co-expressing CDV F-ODP (residues 164, 219, 233, and 317) and homotypic CDV H. The averages of three independent experiments ± S.D. are shown. The microphotographs were taken 13 h post-transfection at a magnification of 200×.

    Techniques Used: Activity Assay, Transfection, Variant Assay, Derivative Assay, Expressing

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    ATCC canine distemper virus cdv strain lederle
    Canine Distemper Virus Cdv Strain Lederle, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    List of strains used as challenge organisms for biltong processing in this study.
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    List of strains used as challenge organisms for biltong processing in this study.
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    93
    ATCC chicken embryos
    MICs in iron-limited BM2 medium
    Chicken Embryos, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    ATCC cdv strain lederle
    Transferring a linear domain of five <t>CDV</t> residues into the H stalk renders MV H capable of activating <t>CDV</t> <t>F-Lederle.</t> A, amino acid sequence alignment of a 49 residue-stretch in the H stalk domain identified in B to mediate specificity of MV H for CDV F-Lederle. The bold letters indicate residues that differ between the H variants. B, a minimal CDV H-derived microdomain spanning residues 110–114 is required for CDV F-Lederle activation by MV H variants. Quantitative fusion assays of cells co-transfected with CDV F-Lederle or MV F and MV H variants as specified below the graph. The values are expressed as the percentages of activity upon co-transfection of CDV F-Lederle or MV F with chimeric MV H (1–138 CDV) covering the area under investigation. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. C, hemadsorption activity of selected H constructs. Roman numerals specify the H variants introduced in B. The values are averages of two independent experiments; the error bars represent the range observed.
    Cdv Strain Lederle, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    List of strains used as challenge organisms for biltong processing in this study.

    Journal: Microorganisms

    Article Title: Evaluation of Various Lactic Acid Bacteria and Generic E. coli as Potential Nonpathogenic Surrogates for In-Plant Validation of Biltong Dried Beef Processing

    doi: 10.3390/microorganisms10081648

    Figure Lengend Snippet: List of strains used as challenge organisms for biltong processing in this study.

    Article Snippet: Pediococcus acidilactici , ATCC 8042 , PMM 128 , GM, 10; RF, 5 , Muriana Culture Collection.

    Techniques: Isolation

    MICs in iron-limited BM2 medium

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Iron/Heme Metabolism-Targeted Gallium(III) Nanoparticles Are Active against Extracellular and Intracellular Pseudomonas aeruginosa and Acinetobacter baumannii

    doi: 10.1128/AAC.02643-18

    Figure Lengend Snippet: MICs in iron-limited BM2 medium

    Article Snippet: Thus, the susceptibility of A. baumannii to Ga(NO 3 ) 3 is more strain dependent, and resistance to Ga(NO 3 ) 3 is more common than for P. aeruginosa ( 22 ). table ft1 table-wrap mode="anchored" t5 TABLE 1 caption a7 Strain MIC (μg/ml) by compound a Ga(NO 3 ) 3 GaPP GaMP GaPC A. baumannii ATCC 19606 4 4 (>128) 4 (>128) >32 A. baumannii B189-17 b >128 8 8 — A. baumannii B220-17 b >128 4 4 — A. baumannii B1365-15 b 1 0.5 0.25 >128 A. baumannii B1457-15 b 16 4 4 — P. aeruginosa PA103 1 to 2 (>128) 8 to 16 ( 1 ) 8 to 16 ( 1 ) >32 P. aeruginosa B1384 b 2 16 to 32 ( 1 ) 32 >128 P. aeruginosa B1379 b 1 32 32 >128 P. aeruginosa B1413 b 2 32 32 >128 P. aeruginosa B1393 b 4 32 32 >128 P. aeruginosa B1416 b 2 32 c 32 c >128 Open in a separate window a Numbers in parentheses indicate MIC determined in RPMI 1640 medium supplemented with 10% FBS.

    Techniques:

    Transferring a linear domain of five CDV residues into the H stalk renders MV H capable of activating CDV F-Lederle. A, amino acid sequence alignment of a 49 residue-stretch in the H stalk domain identified in B to mediate specificity of MV H for CDV F-Lederle. The bold letters indicate residues that differ between the H variants. B, a minimal CDV H-derived microdomain spanning residues 110–114 is required for CDV F-Lederle activation by MV H variants. Quantitative fusion assays of cells co-transfected with CDV F-Lederle or MV F and MV H variants as specified below the graph. The values are expressed as the percentages of activity upon co-transfection of CDV F-Lederle or MV F with chimeric MV H (1–138 CDV) covering the area under investigation. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. C, hemadsorption activity of selected H constructs. Roman numerals specify the H variants introduced in B. The values are averages of two independent experiments; the error bars represent the range observed.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    doi: 10.1074/jbc.M801018200

    Figure Lengend Snippet: Transferring a linear domain of five CDV residues into the H stalk renders MV H capable of activating CDV F-Lederle. A, amino acid sequence alignment of a 49 residue-stretch in the H stalk domain identified in B to mediate specificity of MV H for CDV F-Lederle. The bold letters indicate residues that differ between the H variants. B, a minimal CDV H-derived microdomain spanning residues 110–114 is required for CDV F-Lederle activation by MV H variants. Quantitative fusion assays of cells co-transfected with CDV F-Lederle or MV F and MV H variants as specified below the graph. The values are expressed as the percentages of activity upon co-transfection of CDV F-Lederle or MV F with chimeric MV H (1–138 CDV) covering the area under investigation. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. C, hemadsorption activity of selected H constructs. Roman numerals specify the H variants introduced in B. The values are averages of two independent experiments; the error bars represent the range observed.

    Article Snippet: To prepare stocks of the CDV strain Onderstepoort (ODP; a kind gift of S. Niewiesk) or CDV strain Lederle (ATCC VR-128), Vero-dogSLAM cells were infected at a multiplicity of infection of 0.001 plaque-forming units/cell and incubated at 37 °C.

    Techniques: Transferring, Sequencing, Derivative Assay, Activation Assay, Transfection, Activity Assay, Cotransfection, Construct

    CDV F-ODP but not CDV F-Lederle is triggered by MV H. A, microphotographs of Vero-dogSLAM cells co-transfected with equal amounts of plasmid DNA encoding MV or CDV glycoproteins as specified. The cells were photographed at a magnification of 200× after incubation at 37 °C for seven to 11 h. Mock infected cells expressed only the H protein. B, quantification of cell-to-cell fusion activity using a firefly luciferase reporter-based fusion assay. The values reflect the average luciferase activities of at least three independent experiments ± S.D. per glycoprotein combination and are expressed as the percentages of activity measured for MV F and the respective H. C, CDV F glycoprotein variants show different strengths of interaction with MV H. Co-immunoprecipitation of CDVF-ODP and Lederle with MV H. The lysates of co-transfected cells were subjected to immunoprecipitation using specific antibodies directed against an epitope in the MV H ectodomain. Co-precipitated F (upper panel) was detected in comparison with F present in the lysates prior to precipitation (lower panel) by immunoblotting using a specific antiserum directed against an epitope in the cytosolic tail of CDV F.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    doi: 10.1074/jbc.M801018200

    Figure Lengend Snippet: CDV F-ODP but not CDV F-Lederle is triggered by MV H. A, microphotographs of Vero-dogSLAM cells co-transfected with equal amounts of plasmid DNA encoding MV or CDV glycoproteins as specified. The cells were photographed at a magnification of 200× after incubation at 37 °C for seven to 11 h. Mock infected cells expressed only the H protein. B, quantification of cell-to-cell fusion activity using a firefly luciferase reporter-based fusion assay. The values reflect the average luciferase activities of at least three independent experiments ± S.D. per glycoprotein combination and are expressed as the percentages of activity measured for MV F and the respective H. C, CDV F glycoprotein variants show different strengths of interaction with MV H. Co-immunoprecipitation of CDVF-ODP and Lederle with MV H. The lysates of co-transfected cells were subjected to immunoprecipitation using specific antibodies directed against an epitope in the MV H ectodomain. Co-precipitated F (upper panel) was detected in comparison with F present in the lysates prior to precipitation (lower panel) by immunoblotting using a specific antiserum directed against an epitope in the cytosolic tail of CDV F.

    Article Snippet: To prepare stocks of the CDV strain Onderstepoort (ODP; a kind gift of S. Niewiesk) or CDV strain Lederle (ATCC VR-128), Vero-dogSLAM cells were infected at a multiplicity of infection of 0.001 plaque-forming units/cell and incubated at 37 °C.

    Techniques: Transfection, Plasmid Preparation, Incubation, Infection, Activity Assay, Luciferase, Single Vesicle Fusion Assay, Immunoprecipitation, Western Blot

    Identification of a minimal domain responsible for productive interaction of CDV F variants with MV H. A, quantification of cell-to-cell fusion activity of reciprocal chimeras between CDV F-ODP and Lederle upon co-transfection with MV H (black bars) or CDV H (gray bars) using the luciferase reporter-based fusion assay as outlined in Fig. 1B. The values were normalized for fusion activity observed upon co-transfection of cells with unmodified F-ODP and MV H or CDV H, respectively. The mean values ± S.D. of three independent experiments are shown, and the extent of differential triggering (based on the percentage of homotypic activity/percentage of heterotypic activity) is specified (see text for details). F constructs are schematized below the graph. The black boxes represent regions derived from F-Lederle, and the gray boxes represent F-ODP. The location of characteristic F protein domains, the site of the disulfide bridge linking the F1 and F2 subunits (black line), and the position of natural (BlpI, PvuII, EcoRV, and SmaI) and engineered (BglII and KpnI, in gray) restriction sites used for chimera generation are shown on the left. PS, N-terminal precursor sequence of CDV F; FP, fusion peptide; HR-A, N-terminal heptad repeat; HR-B, C-terminal heptad repeat; TM, transmembrane domain; CT, cytosolic tail. B, focused chimeras based on engineered restriction sites identify a domain in the N-terminal part of F-ODP (between restriction sites KpnI and EcoRV, construct XIII) to determine productive interaction of F-ODP with MV H. Quantification of fusion activity, calculation of differential triggering and color coding as described in A.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    doi: 10.1074/jbc.M801018200

    Figure Lengend Snippet: Identification of a minimal domain responsible for productive interaction of CDV F variants with MV H. A, quantification of cell-to-cell fusion activity of reciprocal chimeras between CDV F-ODP and Lederle upon co-transfection with MV H (black bars) or CDV H (gray bars) using the luciferase reporter-based fusion assay as outlined in Fig. 1B. The values were normalized for fusion activity observed upon co-transfection of cells with unmodified F-ODP and MV H or CDV H, respectively. The mean values ± S.D. of three independent experiments are shown, and the extent of differential triggering (based on the percentage of homotypic activity/percentage of heterotypic activity) is specified (see text for details). F constructs are schematized below the graph. The black boxes represent regions derived from F-Lederle, and the gray boxes represent F-ODP. The location of characteristic F protein domains, the site of the disulfide bridge linking the F1 and F2 subunits (black line), and the position of natural (BlpI, PvuII, EcoRV, and SmaI) and engineered (BglII and KpnI, in gray) restriction sites used for chimera generation are shown on the left. PS, N-terminal precursor sequence of CDV F; FP, fusion peptide; HR-A, N-terminal heptad repeat; HR-B, C-terminal heptad repeat; TM, transmembrane domain; CT, cytosolic tail. B, focused chimeras based on engineered restriction sites identify a domain in the N-terminal part of F-ODP (between restriction sites KpnI and EcoRV, construct XIII) to determine productive interaction of F-ODP with MV H. Quantification of fusion activity, calculation of differential triggering and color coding as described in A.

    Article Snippet: To prepare stocks of the CDV strain Onderstepoort (ODP; a kind gift of S. Niewiesk) or CDV strain Lederle (ATCC VR-128), Vero-dogSLAM cells were infected at a multiplicity of infection of 0.001 plaque-forming units/cell and incubated at 37 °C.

    Techniques: Activity Assay, Cotransfection, Luciferase, Single Vesicle Fusion Assay, Construct, Derivative Assay, Sequencing

    Four point mutations disrupt productive interaction of CDV F-ODP with MV H. A, amino acid sequence alignment of the identified fragment between the KpnI and EcoRV sites of F-Lederle and ODP. The black letters indicate residues that differ between the strains. The fusion peptide (red) and the relative position of the PvuII site are shown. A vertical line marks the furin cleavage site. B, quantitative comparison of fusion activity of individual F-ODP point mutants. The values are expressed as percentages of fusion activity observed upon co-transfection with unmodified F-ODP and either MV or CDV H. The averages of four experiments ± S.D. and the extent of differential triggering are shown. C, visualization of the identified residues in a structural model of the prefusion CDV F-ODP trimer. In the left panel, all four residues (164, 219, 233, and 317) are highlighted in red. Residues 164, 219, and 233 are predicted to be surface-exposed; residue 317 is predicted to be completely buried in the trimer (visible only in the ribbon models; center panel, side view; right panel, top view). For clarity, residues 164, 219, and 233 are not highlighted in the ribbon models. D, co-immunoprecipitation of selected F-ODP mutant constructs with MV H reveals a limited reduction in co-precipitation efficiency as compared with unmodified F-ODP. The experimental conditions were the same as described for Fig. 1C. The values below the blot represent averages of densitometric quantification of co-precipitated F1 material from two independent experiments. They are corrected for the amount of F1 material present in cell lysates prior to precipitation, which serves as internal standard (lower panel), and are expressed as percentage of co-precipitated CDV F1-ODP.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    doi: 10.1074/jbc.M801018200

    Figure Lengend Snippet: Four point mutations disrupt productive interaction of CDV F-ODP with MV H. A, amino acid sequence alignment of the identified fragment between the KpnI and EcoRV sites of F-Lederle and ODP. The black letters indicate residues that differ between the strains. The fusion peptide (red) and the relative position of the PvuII site are shown. A vertical line marks the furin cleavage site. B, quantitative comparison of fusion activity of individual F-ODP point mutants. The values are expressed as percentages of fusion activity observed upon co-transfection with unmodified F-ODP and either MV or CDV H. The averages of four experiments ± S.D. and the extent of differential triggering are shown. C, visualization of the identified residues in a structural model of the prefusion CDV F-ODP trimer. In the left panel, all four residues (164, 219, 233, and 317) are highlighted in red. Residues 164, 219, and 233 are predicted to be surface-exposed; residue 317 is predicted to be completely buried in the trimer (visible only in the ribbon models; center panel, side view; right panel, top view). For clarity, residues 164, 219, and 233 are not highlighted in the ribbon models. D, co-immunoprecipitation of selected F-ODP mutant constructs with MV H reveals a limited reduction in co-precipitation efficiency as compared with unmodified F-ODP. The experimental conditions were the same as described for Fig. 1C. The values below the blot represent averages of densitometric quantification of co-precipitated F1 material from two independent experiments. They are corrected for the amount of F1 material present in cell lysates prior to precipitation, which serves as internal standard (lower panel), and are expressed as percentage of co-precipitated CDV F1-ODP.

    Article Snippet: To prepare stocks of the CDV strain Onderstepoort (ODP; a kind gift of S. Niewiesk) or CDV strain Lederle (ATCC VR-128), Vero-dogSLAM cells were infected at a multiplicity of infection of 0.001 plaque-forming units/cell and incubated at 37 °C.

    Techniques: Sequencing, Activity Assay, Cotransfection, Immunoprecipitation, Mutagenesis, Construct

    Residues in an MV H N-terminal domain are determinants for F specificity. A, quantification of fusion activity upon activation of CDV F-Lederle or MV F with CDV H, MV H, or an MV/CDV H chimera specified in the schematic below the graph. The activity was determined as outlined before (Fig. 1A), and the values are expressed as a percentage of activity observed for either CDV F-Lederle or MV F co-expressed with CDV H. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. Stalk, membrane-proximal part of the H ectodomain (up to residue 139); TM, transmembrane domain; CT, cytosolic tail. B, microphotographs of Vero-dogSLAM cells co-transfected with the constructs outlined in A. The pictures were taken 9.5 h post-transfection at a magnification of 200×. Mock transfected cells received only F-encoding plasmid.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    doi: 10.1074/jbc.M801018200

    Figure Lengend Snippet: Residues in an MV H N-terminal domain are determinants for F specificity. A, quantification of fusion activity upon activation of CDV F-Lederle or MV F with CDV H, MV H, or an MV/CDV H chimera specified in the schematic below the graph. The activity was determined as outlined before (Fig. 1A), and the values are expressed as a percentage of activity observed for either CDV F-Lederle or MV F co-expressed with CDV H. The averages of three independent experiments ± S.D. and the extent of differential triggering are shown. Stalk, membrane-proximal part of the H ectodomain (up to residue 139); TM, transmembrane domain; CT, cytosolic tail. B, microphotographs of Vero-dogSLAM cells co-transfected with the constructs outlined in A. The pictures were taken 9.5 h post-transfection at a magnification of 200×. Mock transfected cells received only F-encoding plasmid.

    Article Snippet: To prepare stocks of the CDV strain Onderstepoort (ODP; a kind gift of S. Niewiesk) or CDV strain Lederle (ATCC VR-128), Vero-dogSLAM cells were infected at a multiplicity of infection of 0.001 plaque-forming units/cell and incubated at 37 °C.

    Techniques: Activity Assay, Activation Assay, Transfection, Construct, Plasmid Preparation

    Residues identified in F and H act interdependently. Quantitative (A) and qualitative (B) assessment of fusion activity of cells co-transfected with the CDV F-ODP (residues 164, 219, 233, and 317) variant introduced in Fig. 3B and CDV H, MV H, or chimeras derived thereof as specified. The quantification results are expressed as percentages of activity observed for cells co-expressing CDV F-ODP (residues 164, 219, 233, and 317) and homotypic CDV H. The averages of three independent experiments ± S.D. are shown. The microphotographs were taken 13 h post-transfection at a magnification of 200×.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Interaction between Paramyxovirus Fusion and Attachment Proteins

    doi: 10.1074/jbc.M801018200

    Figure Lengend Snippet: Residues identified in F and H act interdependently. Quantitative (A) and qualitative (B) assessment of fusion activity of cells co-transfected with the CDV F-ODP (residues 164, 219, 233, and 317) variant introduced in Fig. 3B and CDV H, MV H, or chimeras derived thereof as specified. The quantification results are expressed as percentages of activity observed for cells co-expressing CDV F-ODP (residues 164, 219, 233, and 317) and homotypic CDV H. The averages of three independent experiments ± S.D. are shown. The microphotographs were taken 13 h post-transfection at a magnification of 200×.

    Article Snippet: To prepare stocks of the CDV strain Onderstepoort (ODP; a kind gift of S. Niewiesk) or CDV strain Lederle (ATCC VR-128), Vero-dogSLAM cells were infected at a multiplicity of infection of 0.001 plaque-forming units/cell and incubated at 37 °C.

    Techniques: Activity Assay, Transfection, Variant Assay, Derivative Assay, Expressing