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  • 99
    ATCC vero cells
    Correlation between <t>qPCR</t> - MN and plaque - reduction neutralization ( PRN). Neutralization assays were performed in the ( A ) absence or ( B ) presence of 5% guinea pig complement with RSV-A2 using a panel of human serum samples (n = 30). PRN was performed using HEp-2 cells (50% inhibition endpoint). qPCR-MN (90% inhibition endpoint; geometric mean titers calculated from two experimental replicates) was performed using <t>Vero</t> cells (500 TCID 50 per well of virus input; assessment at 24 hours post-infection).
    Vero Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 11997 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher l glutamine
    Correlation between <t>qPCR</t> - MN and plaque - reduction neutralization ( PRN). Neutralization assays were performed in the ( A ) absence or ( B ) presence of 5% guinea pig complement with RSV-A2 using a panel of human serum samples (n = 30). PRN was performed using HEp-2 cells (50% inhibition endpoint). qPCR-MN (90% inhibition endpoint; geometric mean titers calculated from two experimental replicates) was performed using <t>Vero</t> cells (500 TCID 50 per well of virus input; assessment at 24 hours post-infection).
    L Glutamine, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 146399 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC candida parapsilosis atcc 22019
    Phenotype of Quambalaria cyanescens 11PU348 on Sabouraud dextrose agar ( Figure 2a to 2f ) and CHROMagar Candida ( Figure 2g and 2h ). Incubation conditions: 2a and 2g, 28°C, 48 h; 2b, 28°C, 72 h; 2c, 28°C, 2 weeks; 2d and 2h, 37°C, 48 h; 2e, 37°C, 72 h; 2f, 37°C, 2 weeks. Strains used in Figure 2g and 2h: (i) Q. cyanescens 11PU348; (ii) C. glabrata sensu stricto 10H1043; (iii) C. albicans ATCC 90028; (iv) C. <t>parapsilosis</t> sensu stricto ATCC 22019; (v) C. krusei ATCC 6258; (iv) C. tropicalis 10H1048. C. glabrata sensu stricto 10H1043 and C. tropicalis 10H1048 were selected from CHIF-NET study [15] .
    Candida Parapsilosis Atcc 22019, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1004 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC a549 cells
    RSV NS1 interacts with KLF6. <t>A549</t> cells were transfected with 1.5 μg pEGFPC1-NS1 plasmid for 24 h in a 24-well plate and then transferred to chamber slides. Cells were allowed to adhere overnight, fixed, and stained for GFP expression using an anti-GFP antibody (green) and KLF6 (red). Nuclei were stained with DAPI (1 μg ml − 1 ). Confocal images were captured using a Zeiss LSM 710 inverted confocal microscope using an oil immersion lens at × 63. Images are representative of three fields. (a) DAPI alone, (b) GFP alone, (c) KLF6 alone, (d) merged, and (e) orthogonal projection of the optical section showing co-localization of NS1 and KLF6. Bar, 10 μm.
    A549 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 9092 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    ATCC rsv strains a2
    Fabs CB017.5 and CB002.5 bind with high affinity to <t>RSV</t> G and a G peptide. Surface plasmon resonance (SPR) response curves of Fab CB002.5 (top) and Fab CB017.5 (bottom) binding to wild-type RSV sG from strain A2 (A) and a subtype A RSV G peptide encompassing the central conserved region (B). The raw data are plotted in black, and the calculated best fit to a 1:1 binding model is plotted in red. The equilibrium dissociation constant ( K D ) for each interaction is displayed above the respective SPR curve. (C) Sequence alignment of the 45-residue G peptide and the corresponding region of RSV G from <t>strains</t> A2 and B1. The strictly conserved residues, the cystine noose, and CX3C motif are labeled.
    Rsv Strains A2, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC candida krusei atcc 6258
    Fabs CB017.5 and CB002.5 bind with high affinity to <t>RSV</t> G and a G peptide. Surface plasmon resonance (SPR) response curves of Fab CB002.5 (top) and Fab CB017.5 (bottom) binding to wild-type RSV sG from strain A2 (A) and a subtype A RSV G peptide encompassing the central conserved region (B). The raw data are plotted in black, and the calculated best fit to a 1:1 binding model is plotted in red. The equilibrium dissociation constant ( K D ) for each interaction is displayed above the respective SPR curve. (C) Sequence alignment of the 45-residue G peptide and the corresponding region of RSV G from <t>strains</t> A2 and B1. The strictly conserved residues, the cystine noose, and CX3C motif are labeled.
    Candida Krusei Atcc 6258, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 833 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC e coli atcc 25922
    Time-killing curve of A2 . (A) At time zero, samples of a growing culture of S. aureus ATCC 29213 were incubated with concentrations of A2 equivalent to 1 × (red), 2 × (green), or 4 × (blue) the MIC. (B) Samples of a growing culture of E. coli <t>ATCC</t> 25922 were incubated with concentrations of A2 equivalent to 1 × (red), 2 × (green), or 4 × (blue) the MIC. Vehicle (1% DMSO; black) was included. Samples were removed at the time intervals indicated for the determination of viable cell counts.
    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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    99
    Thermo Fisher rpmi 1640 medium
    Specific T cells induced by MTA1 (1–283) secrete IFN- γ and lyse target cells. PBMCs from healthy HLA-A ∗ 02 + donors were isolated and stimulated with protein MTA1 (1–283) (at final concentrations of 0, 1, 5, 10, 30, and 50 μ g/ml) in <t>RPMI</t> 1640 medium supplemented with 50 U/ml interleukin-2 and 10% FCS once a week for 21 days. On day 21, the induced T cells were collected; (a) IFN- γ secretion was assessed by the ELISPOT assay; ∗ P
    Rpmi 1640 Medium, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 105682 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    ATCC c parapsilosis
    Specific T cells induced by MTA1 (1–283) secrete IFN- γ and lyse target cells. PBMCs from healthy HLA-A ∗ 02 + donors were isolated and stimulated with protein MTA1 (1–283) (at final concentrations of 0, 1, 5, 10, 30, and 50 μ g/ml) in <t>RPMI</t> 1640 medium supplemented with 50 U/ml interleukin-2 and 10% FCS once a week for 21 days. On day 21, the induced T cells were collected; (a) IFN- γ secretion was assessed by the ELISPOT assay; ∗ P
    C Parapsilosis, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 674 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher fetal bovine serum
    Specific T cells induced by MTA1 (1–283) secrete IFN- γ and lyse target cells. PBMCs from healthy HLA-A ∗ 02 + donors were isolated and stimulated with protein MTA1 (1–283) (at final concentrations of 0, 1, 5, 10, 30, and 50 μ g/ml) in <t>RPMI</t> 1640 medium supplemented with 50 U/ml interleukin-2 and 10% FCS once a week for 21 days. On day 21, the induced T cells were collected; (a) IFN- γ secretion was assessed by the ELISPOT assay; ∗ P
    Fetal Bovine Serum, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 225914 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC arpe 19 cells
    In vitro assays of NaIO 3 (SI). ( A ) SI at indicated concentrations was incubated with <t>ARPE-19</t> cells that had not or had accumulated A2E ( bars outlined in orange ) and were exposed or not exposed to 430-nm (±30 nm) ( blue bars ) light for 20 minutes. Viability was determined by MTT absorbance (570 nm). Mean ± SEM of six replicates. P values determined by 1-way ANOVA and Tukey's multiple comparison test. ( B ) In a cell-free assay, SI at indicated concentrations was combined with A2E (50 μM; bars outlined in orange ) and was or was not (control) exposed to 430-nm light (60 seconds; blue bars ). A2E photooxidation was assayed by UPLC measurement of A2E loss. SI does not potentiate the photooxidation of A2E. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test. ( C ) In a cell-free assay, incubation of A2E (50 μM; bars outlined in orange ) with SI at indicated concentrations for 4 hours does not result in oxidative loss of A2E measured by UPLC. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test.
    Arpe 19 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1379 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare fetal bovine serum
    In vitro assays of NaIO 3 (SI). ( A ) SI at indicated concentrations was incubated with <t>ARPE-19</t> cells that had not or had accumulated A2E ( bars outlined in orange ) and were exposed or not exposed to 430-nm (±30 nm) ( blue bars ) light for 20 minutes. Viability was determined by MTT absorbance (570 nm). Mean ± SEM of six replicates. P values determined by 1-way ANOVA and Tukey's multiple comparison test. ( B ) In a cell-free assay, SI at indicated concentrations was combined with A2E (50 μM; bars outlined in orange ) and was or was not (control) exposed to 430-nm light (60 seconds; blue bars ). A2E photooxidation was assayed by UPLC measurement of A2E loss. SI does not potentiate the photooxidation of A2E. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test. ( C ) In a cell-free assay, incubation of A2E (50 μM; bars outlined in orange ) with SI at indicated concentrations for 4 hours does not result in oxidative loss of A2E measured by UPLC. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test.
    Fetal Bovine Serum, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 65507 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC cyanothece sp
    ( a ) Comparison of amino-acid lengths of ortholog genes in UCYN-A1, UCYN-A2 and <t>Cyanothece</t> sp. 51142. ( b ) The range of percent gene length of the UCYN-A1 and UCYN-A2 orthologs compared with the Cyanothece sp. 51142 orthologs.
    Cyanothece Sp, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1623 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    k562  (ATCC)
    99
    ATCC k562
    Expanded lymphocytes are specific against melanoma antigens. In (A left panel), lymphocytes from a melanoma patient were stimulated with peptide pulsed DC in the presence of IL-2 (dashed lines) or IL-15 plus IL-21 (solid lines) for 10 days, and expanded with αCD3 and IL-2 for another 5 days. Cytotoxic activity against A375 melanoma cell line (filled symbols) or an irrelevant SKOv3 ovarian carcinoma (open symbols) cell line was measured with a 4 h Cr 51 release assay. Values represent triplicates at different E:T ratio. In (A, right panel) IL-2 (dashed lines) or IL15/21 (solid lines) expanded cultures were incubated with peptide pulsed or not T2 cells in the presence of cold <t>K562,</t> and cyototoxic activity was measured with a 4 h Cr 51 release assay. Values represent triplicates at different E:T ratio. Data shown is representative of 2 independent experiments. In (B) we stimulated lymphocytes with IL-2 (left) or IL-15/21 (right) and then performed an IFN-γ ELISPOT against T2 cells (black columns) or peptide pulsed T2 (white columns). Columns represent the average of triplicate wells +/- SD. (C) Lymphocytes from a melanoma patient were cultured for 7 days with DC pulsed with the indicated individual peptides plus IL-2 and then we performed an IFN-γ ELISPOT against non pulsed DC (white columns), peptide pulsed DC (black columns) or melanoma A375 cell line tumor lysate (grey columns). Data representative of two different melanoma patients.
    K562, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 2705 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bb7 2  (ATCC)
    94
    ATCC bb7 2
    HIV-1 Nef-DsRed fusion protein causes reduction of cell surface MHC-I antigens, and colocalizes with MHC-I in the perinuclear area. (A and B) Nef-DsRed fusion protein downmodulates MHC-I. HeLa cells stably expressing HLA-A2 (HeLa-A2) were transiently transfected with plasmids encoding either DsRed (A) or a Nef-DsRed fusion protein (B). At 48 h posttransfection, HLA-A2 cell surface expression and DsRed protein expression were analyzed simultaneously by two-color flow cytometry. Crosshairs denote maximum fluorescence of negative controls for HLA-A2 staining (HeLa parental cells) and DsRed protein expression (mock-transfected HeLa-A2 cells). Results shown are representative of three independent experiments. (C through K) Nef-DsRed and MHC-I colocalize in the perinuclear region of cells. HeLa cells (C through E) or HeLa-A2 cells (F through K) were grown on glass slides and transiently transfected with plasmids encoding DsRed (I through K) or Nef-DsRed (C through H). At 24 h posttransfection, DsRed protein was detected by direct immunofluorescence (C, F, and I), and HLA-A2 was detected by indirect immunofluorescence using the HLA-A2-specific monoclonal antibody <t>BB7.2</t> (D, G, and J). Enlargements of boxed regions are displayed as insets in the lower left corners of panels F through H. Images were collected using a Zeiss LSM 510 confocal laser scanning microscope, and single Z sections are displayed. Overlays and insets of DsRed and HLA-A2 images were generated using Adobe Photoshop imaging software. Results shown are representative of three independent experiments.
    Bb7 2, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 58 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC a flavus atcc 204304
    HIV-1 Nef-DsRed fusion protein causes reduction of cell surface MHC-I antigens, and colocalizes with MHC-I in the perinuclear area. (A and B) Nef-DsRed fusion protein downmodulates MHC-I. HeLa cells stably expressing HLA-A2 (HeLa-A2) were transiently transfected with plasmids encoding either DsRed (A) or a Nef-DsRed fusion protein (B). At 48 h posttransfection, HLA-A2 cell surface expression and DsRed protein expression were analyzed simultaneously by two-color flow cytometry. Crosshairs denote maximum fluorescence of negative controls for HLA-A2 staining (HeLa parental cells) and DsRed protein expression (mock-transfected HeLa-A2 cells). Results shown are representative of three independent experiments. (C through K) Nef-DsRed and MHC-I colocalize in the perinuclear region of cells. HeLa cells (C through E) or HeLa-A2 cells (F through K) were grown on glass slides and transiently transfected with plasmids encoding DsRed (I through K) or Nef-DsRed (C through H). At 24 h posttransfection, DsRed protein was detected by direct immunofluorescence (C, F, and I), and HLA-A2 was detected by indirect immunofluorescence using the HLA-A2-specific monoclonal antibody <t>BB7.2</t> (D, G, and J). Enlargements of boxed regions are displayed as insets in the lower left corners of panels F through H. Images were collected using a Zeiss LSM 510 confocal laser scanning microscope, and single Z sections are displayed. Overlays and insets of DsRed and HLA-A2 images were generated using Adobe Photoshop imaging software. Results shown are representative of three independent experiments.
    A Flavus Atcc 204304, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 104 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC a teichomyceticus atcc 31121
    Production of teicoplanin in TM1 to which L -valine and crude oils were added . Fermentation of A. <t>teichomyceticus</t> <t>ATCC</t> 31121 was run in TM1 to which 2.5 g/L corn oil ( A ) or 2.5 g/L olive oil was added ( B ) and different concentrations of L -valine. T-A 2 production in control conditions (without oil and L -valine addition) was set as 100%.
    A Teichomyceticus Atcc 31121, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC s aureus atcc 29213
    TLC separation of in vitro PG biosynthesis reaction mixtures. Cell membranes were prepared from  S. aureus  ATCC 29213, solubilized, and supplied with UDP-[ 14 C]GlcNAc and an appropriate UDP-MurNAc precursor. Where indicated, the samples were treated with ramoplanin prior to the addition of UDP-[ 14 C]GlcNAc. Following incubation and inactivation by boiling, 2-μl aliquots of samples were separated by TLC on silica gel plates and the plates were dried and autoradiographed. The band of unknown nature (indicated by an asterisk) that is detected regardless of the presence (+) or absence (−) of UDP-MurNAc-peptide precursors might result from previously described translocation of [ 14 C] N -acetylglucosamine-1-phosphate from UDP-[ 14 C]GlcNAc to C 55 ).
    S Aureus Atcc 29213, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 4800 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    ATCC bovine viral diarrhoea virus bvdv
    TLC separation of in vitro PG biosynthesis reaction mixtures. Cell membranes were prepared from  S. aureus  ATCC 29213, solubilized, and supplied with UDP-[ 14 C]GlcNAc and an appropriate UDP-MurNAc precursor. Where indicated, the samples were treated with ramoplanin prior to the addition of UDP-[ 14 C]GlcNAc. Following incubation and inactivation by boiling, 2-μl aliquots of samples were separated by TLC on silica gel plates and the plates were dried and autoradiographed. The band of unknown nature (indicated by an asterisk) that is detected regardless of the presence (+) or absence (−) of UDP-MurNAc-peptide precursors might result from previously described translocation of [ 14 C] N -acetylglucosamine-1-phosphate from UDP-[ 14 C]GlcNAc to C 55 ).
    Bovine Viral Diarrhoea Virus Bvdv, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Correlation between qPCR - MN and plaque - reduction neutralization ( PRN). Neutralization assays were performed in the ( A ) absence or ( B ) presence of 5% guinea pig complement with RSV-A2 using a panel of human serum samples (n = 30). PRN was performed using HEp-2 cells (50% inhibition endpoint). qPCR-MN (90% inhibition endpoint; geometric mean titers calculated from two experimental replicates) was performed using Vero cells (500 TCID 50 per well of virus input; assessment at 24 hours post-infection).

    Journal: Virology Journal

    Article Title: A neutralization assay for respiratory syncytial virus using a quantitative PCR-based endpoint assessment

    doi: 10.1186/1743-422X-10-195

    Figure Lengend Snippet: Correlation between qPCR - MN and plaque - reduction neutralization ( PRN). Neutralization assays were performed in the ( A ) absence or ( B ) presence of 5% guinea pig complement with RSV-A2 using a panel of human serum samples (n = 30). PRN was performed using HEp-2 cells (50% inhibition endpoint). qPCR-MN (90% inhibition endpoint; geometric mean titers calculated from two experimental replicates) was performed using Vero cells (500 TCID 50 per well of virus input; assessment at 24 hours post-infection).

    Article Snippet: For qPCR-MN, 96-well culture plates were seeded with Vero cells (15,000 cells per well).

    Techniques: Real-time Polymerase Chain Reaction, Neutralization, Inhibition, Infection

    qPCR signal vs. input virus dose. Vero cells were seeded in 96-well culture plates (15,000 cells per well). On the following day, each well was infected with an inoculum from a two-fold dilution series: 40,000 to 78 TCID 50 per well for ( A ) RSV-A2, and 250,000 to 490 TCID 50 per well for ( B ) RSV-B1. At 24 hours post-infection, cell lysates were prepared using Bio-Rad SPR and subjected to qRT-PCR analysis. RNA copy numbers were normalized to the mean value obtained with the most dilute virus input. Each point represents the mean with corresponding range (n = 4).

    Journal: Virology Journal

    Article Title: A neutralization assay for respiratory syncytial virus using a quantitative PCR-based endpoint assessment

    doi: 10.1186/1743-422X-10-195

    Figure Lengend Snippet: qPCR signal vs. input virus dose. Vero cells were seeded in 96-well culture plates (15,000 cells per well). On the following day, each well was infected with an inoculum from a two-fold dilution series: 40,000 to 78 TCID 50 per well for ( A ) RSV-A2, and 250,000 to 490 TCID 50 per well for ( B ) RSV-B1. At 24 hours post-infection, cell lysates were prepared using Bio-Rad SPR and subjected to qRT-PCR analysis. RNA copy numbers were normalized to the mean value obtained with the most dilute virus input. Each point represents the mean with corresponding range (n = 4).

    Article Snippet: For qPCR-MN, 96-well culture plates were seeded with Vero cells (15,000 cells per well).

    Techniques: Real-time Polymerase Chain Reaction, Infection, SPR Assay, Quantitative RT-PCR

    qRT - PCR - based microneutralization of RSV ( qPCR- MN). Vero cells were seeded in 96-well culture plates (15,000 cells per well). On the following day, a two-fold dilution series was prepared from a pooled human immunoglobulin reference standard (designated as RSV-Lot 1) starting from an initial concentration of 1%. The virus inoculum (500 TCID 50 per well of RSV-A2 or RSV-B1) was mixed with an equal volume of RSV-Lot 1 dilution and incubated for 1 hour at 37°C. After incubation, the mixture was transferred to the plate of seeded Vero cells. At 24 or 48 hours post-infection, cell lysates were prepared using Bio-Rad SPR and subjected to qRT-PCR analysis. RNA copy numbers were normalized to the mean value obtained from virus-infected control wells in the absence of neutralizing immunoglobulin. The neutralization titer was defined as the reciprocal of the highest dilution factor of RSV-Lot 1 necessary to inhibit the PCR signal by 90% (or below the threshold of 10% of the virus control wells indicated by the dotted line). ( A ) RSV-A2 neutralization assessed at 24 or 48 hours post-infection (each point represents the mean; n = 3). ( B ) RSV-B1 neutralization assessed at 24 or 48 hours post-infection (each point represents the mean; n = 3). The individual experimental replicates assessed independently (n = 3) are shown for neutralization experiments with ( C ) RSV-A2 and ( D ) RSV-B1. Additional neutralization experiments ( E ) with RSV-A2 assessed at 24 hours post-infection were also performed with a monoclonal antibody with known specificity to the RSV F protein (1200) as well as rabbit sera generated pre- and post-immunization with RSV-A2 (each point represents the mean with corresponding range; n = 3).

    Journal: Virology Journal

    Article Title: A neutralization assay for respiratory syncytial virus using a quantitative PCR-based endpoint assessment

    doi: 10.1186/1743-422X-10-195

    Figure Lengend Snippet: qRT - PCR - based microneutralization of RSV ( qPCR- MN). Vero cells were seeded in 96-well culture plates (15,000 cells per well). On the following day, a two-fold dilution series was prepared from a pooled human immunoglobulin reference standard (designated as RSV-Lot 1) starting from an initial concentration of 1%. The virus inoculum (500 TCID 50 per well of RSV-A2 or RSV-B1) was mixed with an equal volume of RSV-Lot 1 dilution and incubated for 1 hour at 37°C. After incubation, the mixture was transferred to the plate of seeded Vero cells. At 24 or 48 hours post-infection, cell lysates were prepared using Bio-Rad SPR and subjected to qRT-PCR analysis. RNA copy numbers were normalized to the mean value obtained from virus-infected control wells in the absence of neutralizing immunoglobulin. The neutralization titer was defined as the reciprocal of the highest dilution factor of RSV-Lot 1 necessary to inhibit the PCR signal by 90% (or below the threshold of 10% of the virus control wells indicated by the dotted line). ( A ) RSV-A2 neutralization assessed at 24 or 48 hours post-infection (each point represents the mean; n = 3). ( B ) RSV-B1 neutralization assessed at 24 or 48 hours post-infection (each point represents the mean; n = 3). The individual experimental replicates assessed independently (n = 3) are shown for neutralization experiments with ( C ) RSV-A2 and ( D ) RSV-B1. Additional neutralization experiments ( E ) with RSV-A2 assessed at 24 hours post-infection were also performed with a monoclonal antibody with known specificity to the RSV F protein (1200) as well as rabbit sera generated pre- and post-immunization with RSV-A2 (each point represents the mean with corresponding range; n = 3).

    Article Snippet: For qPCR-MN, 96-well culture plates were seeded with Vero cells (15,000 cells per well).

    Techniques: Quantitative RT-PCR, Real-time Polymerase Chain Reaction, Concentration Assay, Incubation, Infection, SPR Assay, Neutralization, Polymerase Chain Reaction, Generated

    Phenotype of Quambalaria cyanescens 11PU348 on Sabouraud dextrose agar ( Figure 2a to 2f ) and CHROMagar Candida ( Figure 2g and 2h ). Incubation conditions: 2a and 2g, 28°C, 48 h; 2b, 28°C, 72 h; 2c, 28°C, 2 weeks; 2d and 2h, 37°C, 48 h; 2e, 37°C, 72 h; 2f, 37°C, 2 weeks. Strains used in Figure 2g and 2h: (i) Q. cyanescens 11PU348; (ii) C. glabrata sensu stricto 10H1043; (iii) C. albicans ATCC 90028; (iv) C. parapsilosis sensu stricto ATCC 22019; (v) C. krusei ATCC 6258; (iv) C. tropicalis 10H1048. C. glabrata sensu stricto 10H1043 and C. tropicalis 10H1048 were selected from CHIF-NET study [15] .

    Journal: PLoS ONE

    Article Title: A Rare Fungal Species, Quambalaria cyanescens, Isolated from a Patient after Augmentation Mammoplasty – Environmental Contaminant or Pathogen?

    doi: 10.1371/journal.pone.0106949

    Figure Lengend Snippet: Phenotype of Quambalaria cyanescens 11PU348 on Sabouraud dextrose agar ( Figure 2a to 2f ) and CHROMagar Candida ( Figure 2g and 2h ). Incubation conditions: 2a and 2g, 28°C, 48 h; 2b, 28°C, 72 h; 2c, 28°C, 2 weeks; 2d and 2h, 37°C, 48 h; 2e, 37°C, 72 h; 2f, 37°C, 2 weeks. Strains used in Figure 2g and 2h: (i) Q. cyanescens 11PU348; (ii) C. glabrata sensu stricto 10H1043; (iii) C. albicans ATCC 90028; (iv) C. parapsilosis sensu stricto ATCC 22019; (v) C. krusei ATCC 6258; (iv) C. tropicalis 10H1048. C. glabrata sensu stricto 10H1043 and C. tropicalis 10H1048 were selected from CHIF-NET study [15] .

    Article Snippet: Candida parapsilosis ATCC 22019 and Candida krusei ATCC 6258 were used as the quality control strains for the test .

    Techniques: Incubation

    RSV NS1 interacts with KLF6. A549 cells were transfected with 1.5 μg pEGFPC1-NS1 plasmid for 24 h in a 24-well plate and then transferred to chamber slides. Cells were allowed to adhere overnight, fixed, and stained for GFP expression using an anti-GFP antibody (green) and KLF6 (red). Nuclei were stained with DAPI (1 μg ml − 1 ). Confocal images were captured using a Zeiss LSM 710 inverted confocal microscope using an oil immersion lens at × 63. Images are representative of three fields. (a) DAPI alone, (b) GFP alone, (c) KLF6 alone, (d) merged, and (e) orthogonal projection of the optical section showing co-localization of NS1 and KLF6. Bar, 10 μm.

    Journal: The Journal of General Virology

    Article Title: Human respiratory syncytial virus non-structural protein NS1 modifies miR-24 expression via transforming growth factor-β

    doi: 10.1099/jgv.0.000261

    Figure Lengend Snippet: RSV NS1 interacts with KLF6. A549 cells were transfected with 1.5 μg pEGFPC1-NS1 plasmid for 24 h in a 24-well plate and then transferred to chamber slides. Cells were allowed to adhere overnight, fixed, and stained for GFP expression using an anti-GFP antibody (green) and KLF6 (red). Nuclei were stained with DAPI (1 μg ml − 1 ). Confocal images were captured using a Zeiss LSM 710 inverted confocal microscope using an oil immersion lens at × 63. Images are representative of three fields. (a) DAPI alone, (b) GFP alone, (c) KLF6 alone, (d) merged, and (e) orthogonal projection of the optical section showing co-localization of NS1 and KLF6. Bar, 10 μm.

    Article Snippet: A549 cells (ATCC CCL-185) were cultured in Dulbecco's modified Eagle's medium (DMEM) (HyClone) containing 5 % heat-inactivated FBS (Hyclone) ( ; ).

    Techniques: Transfection, Plasmid Preparation, Staining, Expressing, Microscopy

    miR-24 regulates multiple cellular pathways. (a) Work flow used to shortlist miR-24 target genes. Top target predictions were compared to public microarray data on RSV infection. (b, c) Subsets of genes (b) identified were validated using miR-24 inhibition experiments (c). A549 cells (2 × 10 5 ) were transfected with miR-24 inhibitor (25 nM) or mock or non-targeting control (NTC) for 24 h followed by analysis of gene expression using target-specific primers. Expression was calculated relative to 18S rRNA and non-targeting control from two or three independent experiments.

    Journal: The Journal of General Virology

    Article Title: Human respiratory syncytial virus non-structural protein NS1 modifies miR-24 expression via transforming growth factor-β

    doi: 10.1099/jgv.0.000261

    Figure Lengend Snippet: miR-24 regulates multiple cellular pathways. (a) Work flow used to shortlist miR-24 target genes. Top target predictions were compared to public microarray data on RSV infection. (b, c) Subsets of genes (b) identified were validated using miR-24 inhibition experiments (c). A549 cells (2 × 10 5 ) were transfected with miR-24 inhibitor (25 nM) or mock or non-targeting control (NTC) for 24 h followed by analysis of gene expression using target-specific primers. Expression was calculated relative to 18S rRNA and non-targeting control from two or three independent experiments.

    Article Snippet: A549 cells (ATCC CCL-185) were cultured in Dulbecco's modified Eagle's medium (DMEM) (HyClone) containing 5 % heat-inactivated FBS (Hyclone) ( ; ).

    Techniques: Flow Cytometry, Microarray, Infection, Inhibition, Transfection, Expressing

    APOER2 interacts with respiratory syncytial virus (RSV) P protein . ( a ) APOER2 forms a complex with RSV P protein. A549 cells in six-well plate were transfected with 2 µg/well plasmids encoding Flag-tagged APOER2 or it control vectors. At 30 hours

    Journal: Molecular Therapy

    Article Title: Respiratory Syncytial Virus Utilizes a tRNA Fragment to Suppress Antiviral Responses Through a Novel Targeting Mechanism

    doi: 10.1038/mt.2015.124

    Figure Lengend Snippet: APOER2 interacts with respiratory syncytial virus (RSV) P protein . ( a ) APOER2 forms a complex with RSV P protein. A549 cells in six-well plate were transfected with 2 µg/well plasmids encoding Flag-tagged APOER2 or it control vectors. At 30 hours

    Article Snippet: HEp-2, HEK-293, and A549, human alveolar type II-like epithelial cells (all from ATCC, Manassas, VA) were maintained as we previously described., RSV A2 strain was grown in HEp-2 cells and purified by sucrose gradient as described., Viral titer was determined by immunostaining in HEp-2 cells using polyclonal biotin-conjugated goat anti-RSV antibody (Ad Direct, Barberton, OH) and streptavidin peroxidase polymer (Sigma-Aldrich, St Louis, MO) sequentially, as described., RNA pull-down.

    Techniques: Transfection

    Antiviral effect of APOER2 . ( a–c ) The effect of APOER2 silencing on RSV replication. A549 cells were transfected with 100 nmol/l siRNA against APOER2 (si-APOER2) or si-ctrl using Lipofectamine 2000. At 48 hours post-transfection, cells were mock-infected

    Journal: Molecular Therapy

    Article Title: Respiratory Syncytial Virus Utilizes a tRNA Fragment to Suppress Antiviral Responses Through a Novel Targeting Mechanism

    doi: 10.1038/mt.2015.124

    Figure Lengend Snippet: Antiviral effect of APOER2 . ( a–c ) The effect of APOER2 silencing on RSV replication. A549 cells were transfected with 100 nmol/l siRNA against APOER2 (si-APOER2) or si-ctrl using Lipofectamine 2000. At 48 hours post-transfection, cells were mock-infected

    Article Snippet: HEp-2, HEK-293, and A549, human alveolar type II-like epithelial cells (all from ATCC, Manassas, VA) were maintained as we previously described., RSV A2 strain was grown in HEp-2 cells and purified by sucrose gradient as described., Viral titer was determined by immunostaining in HEp-2 cells using polyclonal biotin-conjugated goat anti-RSV antibody (Ad Direct, Barberton, OH) and streptavidin peroxidase polymer (Sigma-Aldrich, St Louis, MO) sequentially, as described., RNA pull-down.

    Techniques: Transfection, Infection

    Fabs CB017.5 and CB002.5 bind with high affinity to RSV G and a G peptide. Surface plasmon resonance (SPR) response curves of Fab CB002.5 (top) and Fab CB017.5 (bottom) binding to wild-type RSV sG from strain A2 (A) and a subtype A RSV G peptide encompassing the central conserved region (B). The raw data are plotted in black, and the calculated best fit to a 1:1 binding model is plotted in red. The equilibrium dissociation constant ( K D ) for each interaction is displayed above the respective SPR curve. (C) Sequence alignment of the 45-residue G peptide and the corresponding region of RSV G from strains A2 and B1. The strictly conserved residues, the cystine noose, and CX3C motif are labeled.

    Journal: PLoS Pathogens

    Article Title: Structural basis for recognition of the central conserved region of RSV G by neutralizing human antibodies

    doi: 10.1371/journal.ppat.1006935

    Figure Lengend Snippet: Fabs CB017.5 and CB002.5 bind with high affinity to RSV G and a G peptide. Surface plasmon resonance (SPR) response curves of Fab CB002.5 (top) and Fab CB017.5 (bottom) binding to wild-type RSV sG from strain A2 (A) and a subtype A RSV G peptide encompassing the central conserved region (B). The raw data are plotted in black, and the calculated best fit to a 1:1 binding model is plotted in red. The equilibrium dissociation constant ( K D ) for each interaction is displayed above the respective SPR curve. (C) Sequence alignment of the 45-residue G peptide and the corresponding region of RSV G from strains A2 and B1. The strictly conserved residues, the cystine noose, and CX3C motif are labeled.

    Article Snippet: RSV strains A2 (ATCC VR-1540) or B1 (ATCC VR-1580) were diluted to 75 PFU/well in 150 μL total volume per well in Eagle’s Minimum Essential Medium (EMEM, ATCC) containing 10% baby rabbit complement (AbD Serotec).

    Techniques: SPR Assay, Binding Assay, Sequencing, Labeling

    Immunization with PR8/NA-F 85–93 virus reduces RSV replication in challenged mice. BALB/c mice were infected with the indicated viruses or with PBS and then challenged intranasally with 1 × 10 6 PFU of RSV-A2. (A) Spleens were isolated 10

    Journal: Journal of Virology

    Article Title: Recombinant Influenza Virus Carrying the Respiratory Syncytial Virus (RSV) F85-93 CTL Epitope Reduces RSV Replication in Mice

    doi: 10.1128/JVI.03019-12

    Figure Lengend Snippet: Immunization with PR8/NA-F 85–93 virus reduces RSV replication in challenged mice. BALB/c mice were infected with the indicated viruses or with PBS and then challenged intranasally with 1 × 10 6 PFU of RSV-A2. (A) Spleens were isolated 10

    Article Snippet: RSV-A2 (ATCC VR-1540) was propagated on HEp-2 cells and quantified by plaque titration on Vero cells.

    Techniques: Mouse Assay, Infection, Isolation

    Time-killing curve of A2 . (A) At time zero, samples of a growing culture of S. aureus ATCC 29213 were incubated with concentrations of A2 equivalent to 1 × (red), 2 × (green), or 4 × (blue) the MIC. (B) Samples of a growing culture of E. coli ATCC 25922 were incubated with concentrations of A2 equivalent to 1 × (red), 2 × (green), or 4 × (blue) the MIC. Vehicle (1% DMSO; black) was included. Samples were removed at the time intervals indicated for the determination of viable cell counts.

    Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

    Article Title: Antibacterial activity of 3-methylbenzo[d]thiazol-methylquinolinium derivatives and study of their action mechanism

    doi: 10.1080/14756366.2018.1465055

    Figure Lengend Snippet: Time-killing curve of A2 . (A) At time zero, samples of a growing culture of S. aureus ATCC 29213 were incubated with concentrations of A2 equivalent to 1 × (red), 2 × (green), or 4 × (blue) the MIC. (B) Samples of a growing culture of E. coli ATCC 25922 were incubated with concentrations of A2 equivalent to 1 × (red), 2 × (green), or 4 × (blue) the MIC. Vehicle (1% DMSO; black) was included. Samples were removed at the time intervals indicated for the determination of viable cell counts.

    Article Snippet: Time killing curves resulting from A2 against S. aureus ATCC 29213 and E. coli ATCC 25922 are presented in .

    Techniques: Incubation

    Specific T cells induced by MTA1 (1–283) secrete IFN- γ and lyse target cells. PBMCs from healthy HLA-A ∗ 02 + donors were isolated and stimulated with protein MTA1 (1–283) (at final concentrations of 0, 1, 5, 10, 30, and 50 μ g/ml) in RPMI 1640 medium supplemented with 50 U/ml interleukin-2 and 10% FCS once a week for 21 days. On day 21, the induced T cells were collected; (a) IFN- γ secretion was assessed by the ELISPOT assay; ∗ P

    Journal: Journal of Immunology Research

    Article Title: HLA-A2-Restricted Epitopes Identified from MTA1 Could Elicit Antigen-Specific Cytotoxic T Lymphocyte Response

    doi: 10.1155/2018/2942679

    Figure Lengend Snippet: Specific T cells induced by MTA1 (1–283) secrete IFN- γ and lyse target cells. PBMCs from healthy HLA-A ∗ 02 + donors were isolated and stimulated with protein MTA1 (1–283) (at final concentrations of 0, 1, 5, 10, 30, and 50 μ g/ml) in RPMI 1640 medium supplemented with 50 U/ml interleukin-2 and 10% FCS once a week for 21 days. On day 21, the induced T cells were collected; (a) IFN- γ secretion was assessed by the ELISPOT assay; ∗ P

    Article Snippet: All cells were cultured in RPMI 1640 medium (Invitrogen, Grand Island, USA) at 37°C in a humidified atmosphere of 5% CO2 and 95% air, supplemented with 10% fetal bovine serum (FBS, BI, Israel), 2 mM L-glutamine, 100 units/ml penicillin, and 100 μ g/ml streptomycin.

    Techniques: Isolation, Enzyme-linked Immunospot

    IFN- γ release and lyse target cell ability of peptide-induced CTLs. PBMCs from six HLA-A ∗ 02 + healthy donors were collected and induced by the indicated peptides (10 μ g/ml) three times in RPMI 1640 medium supplemented with 3 μ g/ml β 2-M (once at each stimulation), interleukin-2 (50 U/ml, on day 3 and 1 day after each stimulation), and 10% FCS for 21 days. CTLs induced by COX-2 321–329 were used as positive controls. On day 21, the CTLs were collected, and the IFN- γ secretion and cytotoxic activity of the CTLs were measured. (a) CTL secretion of IFN- γ was detected by the ELISPOT assay ( n = 6). T2 cells loaded with/without peptide (50 μ g/ml) for 4 h were used as the stimulating cells. LDH cytotoxicity assays were performed ( n = 3) using the following target cell lines: (b) SW620 (HLA-A2 + , MTA1 + ), (c) MDA-MB-231 (HLA-A2 + , MTA1 + ), (d) SW620 incubated with an anti-human HLA-A2 antibody (HLA-A2 − , MTA1 + ), (e) HT-29 (HLA-A2 − , MTA1 + ), (f) MCF-7 (HLA-A2 + , MTA1 + ), (g) HUVEC (HLA-A2 + , MTA1 low ), and (h) Het-1A (HLA-A2 + , MTA1 low ). CTLs induced by PBS were used as the negative control. Data represent means ± standard deviation (SD), ∗ P

    Journal: Journal of Immunology Research

    Article Title: HLA-A2-Restricted Epitopes Identified from MTA1 Could Elicit Antigen-Specific Cytotoxic T Lymphocyte Response

    doi: 10.1155/2018/2942679

    Figure Lengend Snippet: IFN- γ release and lyse target cell ability of peptide-induced CTLs. PBMCs from six HLA-A ∗ 02 + healthy donors were collected and induced by the indicated peptides (10 μ g/ml) three times in RPMI 1640 medium supplemented with 3 μ g/ml β 2-M (once at each stimulation), interleukin-2 (50 U/ml, on day 3 and 1 day after each stimulation), and 10% FCS for 21 days. CTLs induced by COX-2 321–329 were used as positive controls. On day 21, the CTLs were collected, and the IFN- γ secretion and cytotoxic activity of the CTLs were measured. (a) CTL secretion of IFN- γ was detected by the ELISPOT assay ( n = 6). T2 cells loaded with/without peptide (50 μ g/ml) for 4 h were used as the stimulating cells. LDH cytotoxicity assays were performed ( n = 3) using the following target cell lines: (b) SW620 (HLA-A2 + , MTA1 + ), (c) MDA-MB-231 (HLA-A2 + , MTA1 + ), (d) SW620 incubated with an anti-human HLA-A2 antibody (HLA-A2 − , MTA1 + ), (e) HT-29 (HLA-A2 − , MTA1 + ), (f) MCF-7 (HLA-A2 + , MTA1 + ), (g) HUVEC (HLA-A2 + , MTA1 low ), and (h) Het-1A (HLA-A2 + , MTA1 low ). CTLs induced by PBS were used as the negative control. Data represent means ± standard deviation (SD), ∗ P

    Article Snippet: All cells were cultured in RPMI 1640 medium (Invitrogen, Grand Island, USA) at 37°C in a humidified atmosphere of 5% CO2 and 95% air, supplemented with 10% fetal bovine serum (FBS, BI, Israel), 2 mM L-glutamine, 100 units/ml penicillin, and 100 μ g/ml streptomycin.

    Techniques: Activity Assay, CTL Assay, Enzyme-linked Immunospot, Multiple Displacement Amplification, Incubation, Negative Control, Standard Deviation

    In vitro assays of NaIO 3 (SI). ( A ) SI at indicated concentrations was incubated with ARPE-19 cells that had not or had accumulated A2E ( bars outlined in orange ) and were exposed or not exposed to 430-nm (±30 nm) ( blue bars ) light for 20 minutes. Viability was determined by MTT absorbance (570 nm). Mean ± SEM of six replicates. P values determined by 1-way ANOVA and Tukey's multiple comparison test. ( B ) In a cell-free assay, SI at indicated concentrations was combined with A2E (50 μM; bars outlined in orange ) and was or was not (control) exposed to 430-nm light (60 seconds; blue bars ). A2E photooxidation was assayed by UPLC measurement of A2E loss. SI does not potentiate the photooxidation of A2E. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test. ( C ) In a cell-free assay, incubation of A2E (50 μM; bars outlined in orange ) with SI at indicated concentrations for 4 hours does not result in oxidative loss of A2E measured by UPLC. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test.

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Multimodal Fundus Imaging of Sodium Iodate-Treated Mice Informs RPE Susceptibility and Origins of Increased Fundus Autofluorescence

    doi: 10.1167/iovs.17-21557

    Figure Lengend Snippet: In vitro assays of NaIO 3 (SI). ( A ) SI at indicated concentrations was incubated with ARPE-19 cells that had not or had accumulated A2E ( bars outlined in orange ) and were exposed or not exposed to 430-nm (±30 nm) ( blue bars ) light for 20 minutes. Viability was determined by MTT absorbance (570 nm). Mean ± SEM of six replicates. P values determined by 1-way ANOVA and Tukey's multiple comparison test. ( B ) In a cell-free assay, SI at indicated concentrations was combined with A2E (50 μM; bars outlined in orange ) and was or was not (control) exposed to 430-nm light (60 seconds; blue bars ). A2E photooxidation was assayed by UPLC measurement of A2E loss. SI does not potentiate the photooxidation of A2E. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test. ( C ) In a cell-free assay, incubation of A2E (50 μM; bars outlined in orange ) with SI at indicated concentrations for 4 hours does not result in oxidative loss of A2E measured by UPLC. Mean ± SEM of two replicates. P > 0.05, 1-way ANOVA, and Tukey's multiple comparison test.

    Article Snippet: To test for direct effects of NaIO3 on cultured RPE, ARPE-19 cells (American Type Culture Collection, Manassas, VA, USA) deficient in endogenous lipofuscin were grown to confluence in 96-well plates as described.

    Techniques: In Vitro, Incubation, MTT Assay, Cell-Free Assay

    ( a ) Comparison of amino-acid lengths of ortholog genes in UCYN-A1, UCYN-A2 and Cyanothece sp. 51142. ( b ) The range of percent gene length of the UCYN-A1 and UCYN-A2 orthologs compared with the Cyanothece sp. 51142 orthologs.

    Journal: The ISME Journal

    Article Title: Comparative genomics reveals surprising divergence of two closely related strains of uncultivated UCYN-A cyanobacteria

    doi: 10.1038/ismej.2014.167

    Figure Lengend Snippet: ( a ) Comparison of amino-acid lengths of ortholog genes in UCYN-A1, UCYN-A2 and Cyanothece sp. 51142. ( b ) The range of percent gene length of the UCYN-A1 and UCYN-A2 orthologs compared with the Cyanothece sp. 51142 orthologs.

    Article Snippet: Maximum likelihood analyses confirmed that both UCYN-A strains belong to a well-supported monophyletic group of marine planktonic cyanobacteria containing Crocosphaera sp., Cyanothece sp. and other unicellular N2 fixing cyanobacteria ( ).

    Techniques:

    Expanded lymphocytes are specific against melanoma antigens. In (A left panel), lymphocytes from a melanoma patient were stimulated with peptide pulsed DC in the presence of IL-2 (dashed lines) or IL-15 plus IL-21 (solid lines) for 10 days, and expanded with αCD3 and IL-2 for another 5 days. Cytotoxic activity against A375 melanoma cell line (filled symbols) or an irrelevant SKOv3 ovarian carcinoma (open symbols) cell line was measured with a 4 h Cr 51 release assay. Values represent triplicates at different E:T ratio. In (A, right panel) IL-2 (dashed lines) or IL15/21 (solid lines) expanded cultures were incubated with peptide pulsed or not T2 cells in the presence of cold K562, and cyototoxic activity was measured with a 4 h Cr 51 release assay. Values represent triplicates at different E:T ratio. Data shown is representative of 2 independent experiments. In (B) we stimulated lymphocytes with IL-2 (left) or IL-15/21 (right) and then performed an IFN-γ ELISPOT against T2 cells (black columns) or peptide pulsed T2 (white columns). Columns represent the average of triplicate wells +/- SD. (C) Lymphocytes from a melanoma patient were cultured for 7 days with DC pulsed with the indicated individual peptides plus IL-2 and then we performed an IFN-γ ELISPOT against non pulsed DC (white columns), peptide pulsed DC (black columns) or melanoma A375 cell line tumor lysate (grey columns). Data representative of two different melanoma patients.

    Journal: Cancer letters

    Article Title: Ex vivo expansion of tumor specific lymphocytes with IL-15 and IL-21 for adoptive immunotherapy in melanoma

    doi: 10.1016/j.canlet.2009.05.003

    Figure Lengend Snippet: Expanded lymphocytes are specific against melanoma antigens. In (A left panel), lymphocytes from a melanoma patient were stimulated with peptide pulsed DC in the presence of IL-2 (dashed lines) or IL-15 plus IL-21 (solid lines) for 10 days, and expanded with αCD3 and IL-2 for another 5 days. Cytotoxic activity against A375 melanoma cell line (filled symbols) or an irrelevant SKOv3 ovarian carcinoma (open symbols) cell line was measured with a 4 h Cr 51 release assay. Values represent triplicates at different E:T ratio. In (A, right panel) IL-2 (dashed lines) or IL15/21 (solid lines) expanded cultures were incubated with peptide pulsed or not T2 cells in the presence of cold K562, and cyototoxic activity was measured with a 4 h Cr 51 release assay. Values represent triplicates at different E:T ratio. Data shown is representative of 2 independent experiments. In (B) we stimulated lymphocytes with IL-2 (left) or IL-15/21 (right) and then performed an IFN-γ ELISPOT against T2 cells (black columns) or peptide pulsed T2 (white columns). Columns represent the average of triplicate wells +/- SD. (C) Lymphocytes from a melanoma patient were cultured for 7 days with DC pulsed with the indicated individual peptides plus IL-2 and then we performed an IFN-γ ELISPOT against non pulsed DC (white columns), peptide pulsed DC (black columns) or melanoma A375 cell line tumor lysate (grey columns). Data representative of two different melanoma patients.

    Article Snippet: HLA-A2+ cell lines A375 (melanoma), SKOv3 (ovarian carcinoma), and the cell lines T2 and K562 were obtained from the American Type Culture Collection (ATCC) (Rockville, MD) and cultured following ATCC guidelines.

    Techniques: Activity Assay, Release Assay, Incubation, Enzyme-linked Immunospot, Cell Culture

    HIV-1 Nef-DsRed fusion protein causes reduction of cell surface MHC-I antigens, and colocalizes with MHC-I in the perinuclear area. (A and B) Nef-DsRed fusion protein downmodulates MHC-I. HeLa cells stably expressing HLA-A2 (HeLa-A2) were transiently transfected with plasmids encoding either DsRed (A) or a Nef-DsRed fusion protein (B). At 48 h posttransfection, HLA-A2 cell surface expression and DsRed protein expression were analyzed simultaneously by two-color flow cytometry. Crosshairs denote maximum fluorescence of negative controls for HLA-A2 staining (HeLa parental cells) and DsRed protein expression (mock-transfected HeLa-A2 cells). Results shown are representative of three independent experiments. (C through K) Nef-DsRed and MHC-I colocalize in the perinuclear region of cells. HeLa cells (C through E) or HeLa-A2 cells (F through K) were grown on glass slides and transiently transfected with plasmids encoding DsRed (I through K) or Nef-DsRed (C through H). At 24 h posttransfection, DsRed protein was detected by direct immunofluorescence (C, F, and I), and HLA-A2 was detected by indirect immunofluorescence using the HLA-A2-specific monoclonal antibody BB7.2 (D, G, and J). Enlargements of boxed regions are displayed as insets in the lower left corners of panels F through H. Images were collected using a Zeiss LSM 510 confocal laser scanning microscope, and single Z sections are displayed. Overlays and insets of DsRed and HLA-A2 images were generated using Adobe Photoshop imaging software. Results shown are representative of three independent experiments.

    Journal: Journal of Virology

    Article Title: Direct Binding of Human Immunodeficiency Virus Type 1 Nef to the Major Histocompatibility Complex Class I (MHC-I) Cytoplasmic Tail Disrupts MHC-I Trafficking

    doi: 10.1128/JVI.76.23.12173-12184.2002

    Figure Lengend Snippet: HIV-1 Nef-DsRed fusion protein causes reduction of cell surface MHC-I antigens, and colocalizes with MHC-I in the perinuclear area. (A and B) Nef-DsRed fusion protein downmodulates MHC-I. HeLa cells stably expressing HLA-A2 (HeLa-A2) were transiently transfected with plasmids encoding either DsRed (A) or a Nef-DsRed fusion protein (B). At 48 h posttransfection, HLA-A2 cell surface expression and DsRed protein expression were analyzed simultaneously by two-color flow cytometry. Crosshairs denote maximum fluorescence of negative controls for HLA-A2 staining (HeLa parental cells) and DsRed protein expression (mock-transfected HeLa-A2 cells). Results shown are representative of three independent experiments. (C through K) Nef-DsRed and MHC-I colocalize in the perinuclear region of cells. HeLa cells (C through E) or HeLa-A2 cells (F through K) were grown on glass slides and transiently transfected with plasmids encoding DsRed (I through K) or Nef-DsRed (C through H). At 24 h posttransfection, DsRed protein was detected by direct immunofluorescence (C, F, and I), and HLA-A2 was detected by indirect immunofluorescence using the HLA-A2-specific monoclonal antibody BB7.2 (D, G, and J). Enlargements of boxed regions are displayed as insets in the lower left corners of panels F through H. Images were collected using a Zeiss LSM 510 confocal laser scanning microscope, and single Z sections are displayed. Overlays and insets of DsRed and HLA-A2 images were generated using Adobe Photoshop imaging software. Results shown are representative of three independent experiments.

    Article Snippet: For fluorescence microscopy, BB7.2 (ATCC) was used.

    Techniques: Stable Transfection, Expressing, Transfection, Flow Cytometry, Cytometry, Fluorescence, Staining, Immunofluorescence, Laser-Scanning Microscopy, Generated, Imaging, Software

    Production of teicoplanin in TM1 to which L -valine and crude oils were added . Fermentation of A. teichomyceticus ATCC 31121 was run in TM1 to which 2.5 g/L corn oil ( A ) or 2.5 g/L olive oil was added ( B ) and different concentrations of L -valine. T-A 2 production in control conditions (without oil and L -valine addition) was set as 100%.

    Journal: Microbial Cell Factories

    Article Title: Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin

    doi: 10.1186/1475-2859-10-82

    Figure Lengend Snippet: Production of teicoplanin in TM1 to which L -valine and crude oils were added . Fermentation of A. teichomyceticus ATCC 31121 was run in TM1 to which 2.5 g/L corn oil ( A ) or 2.5 g/L olive oil was added ( B ) and different concentrations of L -valine. T-A 2 production in control conditions (without oil and L -valine addition) was set as 100%.

    Article Snippet: Components of TE/20 medium (carbon sources, nitrogen sources, and CaCO3 ) were examined individually to determine their contribution toward the production of T-A2 in A. teichomyceticus ATCC 31121 (single-factor experiments).

    Techniques:

    Teicoplanin profile in TM1 to which L -valine was added . HPLC profile of sample harvested at 120 hours from the fermentation of A. teichomyceticus ATCC 31121 in TM1 to which 2 g/ L -valine was added. T-A 2-1 , T-A 2-2 , T-A 2-3 , T-A 2-4 , and T-A 2-5 represent 7.3, 73.4, 10.5, 2.0, and 6.8% of the total T-A 2 .

    Journal: Microbial Cell Factories

    Article Title: Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin

    doi: 10.1186/1475-2859-10-82

    Figure Lengend Snippet: Teicoplanin profile in TM1 to which L -valine was added . HPLC profile of sample harvested at 120 hours from the fermentation of A. teichomyceticus ATCC 31121 in TM1 to which 2 g/ L -valine was added. T-A 2-1 , T-A 2-2 , T-A 2-3 , T-A 2-4 , and T-A 2-5 represent 7.3, 73.4, 10.5, 2.0, and 6.8% of the total T-A 2 .

    Article Snippet: Components of TE/20 medium (carbon sources, nitrogen sources, and CaCO3 ) were examined individually to determine their contribution toward the production of T-A2 in A. teichomyceticus ATCC 31121 (single-factor experiments).

    Techniques: High Performance Liquid Chromatography

    Optimization of teicoplanin production medium . Effect of different carbon ( A ) and nitrogen ( B ) sources on growth (PMV, empty bars) and T-A 2 production (mg/L, filled bars) by A. teichomyceticus ATCC 31121. Carbon sources were tested at 20 g/L replacing maltose in TE/20. Nitrogen sources were tested at 15 g/L replacing cottonseed meal in TE/20.

    Journal: Microbial Cell Factories

    Article Title: Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin

    doi: 10.1186/1475-2859-10-82

    Figure Lengend Snippet: Optimization of teicoplanin production medium . Effect of different carbon ( A ) and nitrogen ( B ) sources on growth (PMV, empty bars) and T-A 2 production (mg/L, filled bars) by A. teichomyceticus ATCC 31121. Carbon sources were tested at 20 g/L replacing maltose in TE/20. Nitrogen sources were tested at 15 g/L replacing cottonseed meal in TE/20.

    Article Snippet: Components of TE/20 medium (carbon sources, nitrogen sources, and CaCO3 ) were examined individually to determine their contribution toward the production of T-A2 in A. teichomyceticus ATCC 31121 (single-factor experiments).

    Techniques:

    Fermentation of A. teichomyceticus ATCC 31121 at flask scale in TM1 medium . In ( A ), time courses of pH (□, dashed line), glucose (▲, dashed line), growth curve measured as PMV (○, solid line), and T-A 2 production (●, solid line). In ( B ), HPLC profile of 144-hour sample showing the following complex composition: T-A 2-1 , T-A 2-2 , T-A 2-3 , T-A 2-4 , and T-A 2-5 represent 7.3, 60.2, 13.1, 9.1, and 10.3% of the total T-A 2 .

    Journal: Microbial Cell Factories

    Article Title: Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin

    doi: 10.1186/1475-2859-10-82

    Figure Lengend Snippet: Fermentation of A. teichomyceticus ATCC 31121 at flask scale in TM1 medium . In ( A ), time courses of pH (□, dashed line), glucose (▲, dashed line), growth curve measured as PMV (○, solid line), and T-A 2 production (●, solid line). In ( B ), HPLC profile of 144-hour sample showing the following complex composition: T-A 2-1 , T-A 2-2 , T-A 2-3 , T-A 2-4 , and T-A 2-5 represent 7.3, 60.2, 13.1, 9.1, and 10.3% of the total T-A 2 .

    Article Snippet: Components of TE/20 medium (carbon sources, nitrogen sources, and CaCO3 ) were examined individually to determine their contribution toward the production of T-A2 in A. teichomyceticus ATCC 31121 (single-factor experiments).

    Techniques: High Performance Liquid Chromatography

    Growth and teicoplanin production in 3-L batch fermentations of A. teichomyceticus ATCC 31121 in TM1 . The pH value was naturally self-regulated ( i.e ., it was not controlled by adding acid/base during the fermentation), whereas the pO 2 was controlled over the 20% of saturation by adjusting agitation speed. In ( A) , time courses of pH (●, solid line), pO 2 (□, dashed line), glucose (▲, solid line), and growth curve measured as dry weight (Δ, dashed line) and PMV (■, solid line). In ( B ), production of T-A 2 measured by HPLC analysis as mg/L (filled bars).

    Journal: Microbial Cell Factories

    Article Title: Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin

    doi: 10.1186/1475-2859-10-82

    Figure Lengend Snippet: Growth and teicoplanin production in 3-L batch fermentations of A. teichomyceticus ATCC 31121 in TM1 . The pH value was naturally self-regulated ( i.e ., it was not controlled by adding acid/base during the fermentation), whereas the pO 2 was controlled over the 20% of saturation by adjusting agitation speed. In ( A) , time courses of pH (●, solid line), pO 2 (□, dashed line), glucose (▲, solid line), and growth curve measured as dry weight (Δ, dashed line) and PMV (■, solid line). In ( B ), production of T-A 2 measured by HPLC analysis as mg/L (filled bars).

    Article Snippet: Components of TE/20 medium (carbon sources, nitrogen sources, and CaCO3 ) were examined individually to determine their contribution toward the production of T-A2 in A. teichomyceticus ATCC 31121 (single-factor experiments).

    Techniques: High Performance Liquid Chromatography

    Growth and teicoplanin production in 3-L batch fermentations of A. teichomyceticus ATCC 31121 in TM1 to which L -valine was added . L -valine (2 g/L) was added at the time of inoculation. The pH value was naturally self-regulated, whereas the pO 2 was controlled over the 20% of saturation by adjusting agitation speed. In ( A ), time courses time course of pH (●, solid line), pO 2 (□, dashed line), glucose (▲, solid line), growth curve measured as dry weight (Δ, dashed line), and PMV (■, solid line). In ( B ), production of T-A 2 measured by HPLC analysis as mg/L (filled bars).

    Journal: Microbial Cell Factories

    Article Title: Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin

    doi: 10.1186/1475-2859-10-82

    Figure Lengend Snippet: Growth and teicoplanin production in 3-L batch fermentations of A. teichomyceticus ATCC 31121 in TM1 to which L -valine was added . L -valine (2 g/L) was added at the time of inoculation. The pH value was naturally self-regulated, whereas the pO 2 was controlled over the 20% of saturation by adjusting agitation speed. In ( A ), time courses time course of pH (●, solid line), pO 2 (□, dashed line), glucose (▲, solid line), growth curve measured as dry weight (Δ, dashed line), and PMV (■, solid line). In ( B ), production of T-A 2 measured by HPLC analysis as mg/L (filled bars).

    Article Snippet: Components of TE/20 medium (carbon sources, nitrogen sources, and CaCO3 ) were examined individually to determine their contribution toward the production of T-A2 in A. teichomyceticus ATCC 31121 (single-factor experiments).

    Techniques: High Performance Liquid Chromatography

    TLC separation of in vitro PG biosynthesis reaction mixtures. Cell membranes were prepared from  S. aureus  ATCC 29213, solubilized, and supplied with UDP-[ 14 C]GlcNAc and an appropriate UDP-MurNAc precursor. Where indicated, the samples were treated with ramoplanin prior to the addition of UDP-[ 14 C]GlcNAc. Following incubation and inactivation by boiling, 2-μl aliquots of samples were separated by TLC on silica gel plates and the plates were dried and autoradiographed. The band of unknown nature (indicated by an asterisk) that is detected regardless of the presence (+) or absence (−) of UDP-MurNAc-peptide precursors might result from previously described translocation of [ 14 C] N -acetylglucosamine-1-phosphate from UDP-[ 14 C]GlcNAc to C 55 ).

    Journal: Journal of Bacteriology

    Article Title: Further Evidence that a Cell Wall Precursor [C55-MurNAc-(Peptide)-GlcNAc] Serves as an Acceptor in a Sorting Reaction

    doi: 10.1128/JB.184.8.2141-2147.2002

    Figure Lengend Snippet: TLC separation of in vitro PG biosynthesis reaction mixtures. Cell membranes were prepared from S. aureus ATCC 29213, solubilized, and supplied with UDP-[ 14 C]GlcNAc and an appropriate UDP-MurNAc precursor. Where indicated, the samples were treated with ramoplanin prior to the addition of UDP-[ 14 C]GlcNAc. Following incubation and inactivation by boiling, 2-μl aliquots of samples were separated by TLC on silica gel plates and the plates were dried and autoradiographed. The band of unknown nature (indicated by an asterisk) that is detected regardless of the presence (+) or absence (−) of UDP-MurNAc-peptide precursors might result from previously described translocation of [ 14 C] N -acetylglucosamine-1-phosphate from UDP-[ 14 C]GlcNAc to C 55 ).

    Article Snippet: The A2 pm-containing precursors were isolated from S. lividans as described above, and the Lys-containing precursor was isolated by a similar procedure from TCA extracts of S. aureus ATCC 29213.

    Techniques: Thin Layer Chromatography, In Vitro, Incubation, Translocation Assay