alexa fluor 647-conjugated goat anti-mouse igg antibody Thermo Fisher Search Results


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  • 99
    Thermo Fisher goat anti mouse igg h l cross adsorbed secondary antibody
    Goat Anti Mouse Igg H L Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 14005 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 647 conjugated goat anti mouse igg2a
    Binding of IAV to pAEC and ipAEC. Primary pAECs (A) or immortalized pAECs (B) were incubated with H1N1 IL/08 (red), pH1N1 CA/09 (green) or mock virus preparation (black) at an MOI of 50 for 90 min on ice. Cells were washed either with cold DMEM (solid lines) or acid glycine buffer (dotted lines). Surface bound virus was analyzed by flowcytometry using anti-NP monoclonal antibody followed by <t>Alexa</t> <t>Fluor</t> 647 conjugated goat anti-mouse <t>IgG2a.</t> Data are representative of three independent experiments.
    Alexa Fluor 647 Conjugated Goat Anti Mouse Igg2a, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti mouse igg h l highly cross adsorbed secondary antibody
    Binding of IAV to pAEC and ipAEC. Primary pAECs (A) or immortalized pAECs (B) were incubated with H1N1 IL/08 (red), pH1N1 CA/09 (green) or mock virus preparation (black) at an MOI of 50 for 90 min on ice. Cells were washed either with cold DMEM (solid lines) or acid glycine buffer (dotted lines). Surface bound virus was analyzed by flowcytometry using anti-NP monoclonal antibody followed by <t>Alexa</t> <t>Fluor</t> 647 conjugated goat anti-mouse <t>IgG2a.</t> Data are representative of three independent experiments.
    Goat Anti Mouse Igg H L Highly Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9004 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti mouse igg1 cross adsorbed secondary antibody
    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated <t>IgG</t> (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.
    Goat Anti Mouse Igg1 Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1214 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher goat anti mouse igg2b alexa fluor 647 conjugate
    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated <t>IgG</t> (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.
    Goat Anti Mouse Igg2b Alexa Fluor 647 Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti mouse igg h l superclonal secondary antibody
    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated <t>IgG</t> (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.
    Goat Anti Mouse Igg H L Superclonal Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 411 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor conjugated secondary antibodies
    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated <t>IgG</t> (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.
    Alexa Fluor Conjugated Secondary Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9115 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti mouse igg1 af647
    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated <t>IgG</t> (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.
    Goat Anti Mouse Igg1 Af647, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti mouse igg
    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated <t>IgG</t> (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.
    Goat Anti Mouse Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 9641 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Binding of IAV to pAEC and ipAEC. Primary pAECs (A) or immortalized pAECs (B) were incubated with H1N1 IL/08 (red), pH1N1 CA/09 (green) or mock virus preparation (black) at an MOI of 50 for 90 min on ice. Cells were washed either with cold DMEM (solid lines) or acid glycine buffer (dotted lines). Surface bound virus was analyzed by flowcytometry using anti-NP monoclonal antibody followed by Alexa Fluor 647 conjugated goat anti-mouse IgG2a. Data are representative of three independent experiments.

    Journal: PLoS ONE

    Article Title: Differential Induction of Type I and Type III Interferons by Swine and Human Origin H1N1 Influenza A Viruses in Porcine Airway Epithelial Cells

    doi: 10.1371/journal.pone.0138704

    Figure Lengend Snippet: Binding of IAV to pAEC and ipAEC. Primary pAECs (A) or immortalized pAECs (B) were incubated with H1N1 IL/08 (red), pH1N1 CA/09 (green) or mock virus preparation (black) at an MOI of 50 for 90 min on ice. Cells were washed either with cold DMEM (solid lines) or acid glycine buffer (dotted lines). Surface bound virus was analyzed by flowcytometry using anti-NP monoclonal antibody followed by Alexa Fluor 647 conjugated goat anti-mouse IgG2a. Data are representative of three independent experiments.

    Article Snippet: To detect bound virus, cells were incubated with monoclonal antibody to influenza A nucleoprotein (NP) (MAB8800; EMD Millipore corporation, Temecula, CA) for 30 min. followed by Alexa Fluor 647 conjugated goat anti-mouse IgG2a (Molecular probes Inc, Eugene, OR) for 30 min at 4o C. The MAB detects NP from all IAV strains.

    Techniques: Binding Assay, Incubation

    Staurosporine treatment results in the redistribution of SSA/Ro52 to surface blebs of apoptotic cells. A representative confocal microcopy image of RAW264.7 cells treated with 1 µM staurosporine for 6 h. The distribution of the SSA/Ro52 autoantigen was visualized through confocal microscopy using a rabbit polyclonal anti-SSA/Ro52 and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary (Panel A). Nuclei were counterstained with propidium iodide (Panel B). Apoptotic nuclei are indicated by arrows. The plasma membrane was visualized with Alexa Fluor 647 cholera toxin subunit B conjugate (Panel C). Panel D shows the merged image with an arrow indicating apoptotic cell surface blebs enriched in SSA/Ro52.

    Journal: Toxicology

    Article Title: Autoantibodies from mice exposed to Libby amphibole asbestos bind SSA/Ro52 - enriched apoptotic blebs of murine macrophages

    doi: 10.1016/j.tox.2008.01.008

    Figure Lengend Snippet: Staurosporine treatment results in the redistribution of SSA/Ro52 to surface blebs of apoptotic cells. A representative confocal microcopy image of RAW264.7 cells treated with 1 µM staurosporine for 6 h. The distribution of the SSA/Ro52 autoantigen was visualized through confocal microscopy using a rabbit polyclonal anti-SSA/Ro52 and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary (Panel A). Nuclei were counterstained with propidium iodide (Panel B). Apoptotic nuclei are indicated by arrows. The plasma membrane was visualized with Alexa Fluor 647 cholera toxin subunit B conjugate (Panel C). Panel D shows the merged image with an arrow indicating apoptotic cell surface blebs enriched in SSA/Ro52.

    Article Snippet: Bound autoantibodies from asbestos exposed mice were detected using an Alexa Fluor 647-conjugated goat anti-mouse IgG antibody (Molecular Probes).

    Techniques: Confocal Microscopy

    Libby 6-mix exposure results in the redistribution of SSA/Ro52 to surface blebs of apoptotic cells. Representative confocal microcopy images of RAW264.7 cells untreated (Panels A–D) or exposed to Libby asbestos for 48 h (Panels E–L). The distribution of the SSA/Ro52 autoantigen was visualized through confocal microscopy using a rabbit polyclonal anti-SSA/Ro52 and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary (Green in panels A, E and I). Nuclei were counterstained with propidium iodide (Red in panels B, F and J). Apoptotic nuclei are indicated by arrows. The plasma membrane was visualized with Alexa Fluor 647 cholera toxin subunit B conjugate (Magenta in panels C, G and K). Right panels (D, H and L) show merged images with arrows indicating apoptotic cell surface blebs enriched in SSA/Ro52.

    Journal: Toxicology

    Article Title: Autoantibodies from mice exposed to Libby amphibole asbestos bind SSA/Ro52 - enriched apoptotic blebs of murine macrophages

    doi: 10.1016/j.tox.2008.01.008

    Figure Lengend Snippet: Libby 6-mix exposure results in the redistribution of SSA/Ro52 to surface blebs of apoptotic cells. Representative confocal microcopy images of RAW264.7 cells untreated (Panels A–D) or exposed to Libby asbestos for 48 h (Panels E–L). The distribution of the SSA/Ro52 autoantigen was visualized through confocal microscopy using a rabbit polyclonal anti-SSA/Ro52 and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary (Green in panels A, E and I). Nuclei were counterstained with propidium iodide (Red in panels B, F and J). Apoptotic nuclei are indicated by arrows. The plasma membrane was visualized with Alexa Fluor 647 cholera toxin subunit B conjugate (Magenta in panels C, G and K). Right panels (D, H and L) show merged images with arrows indicating apoptotic cell surface blebs enriched in SSA/Ro52.

    Article Snippet: Bound autoantibodies from asbestos exposed mice were detected using an Alexa Fluor 647-conjugated goat anti-mouse IgG antibody (Molecular Probes).

    Techniques: Confocal Microscopy

    Autoantibodies from asbestos-exposed mice recognize apoptotic blebs enriched with the SSA/Ro52 autoantigen. Representative confocal microcopy images of RAW264.7 cells exposed to Libby asbestos for 48 h. The SSA/Ro52 autoantigen was visualized through confocal microscopy using a rabbit polyclonal anti-SSA/Ro52 antibody and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary (Green in panels A, E and I). Nuclei were counterstained with propidium iodide (Cyan in panels B, F and J). Apoptotic nuclei are indicated by arrows. Binding of mouse autoantibodies were visualized with an Alexa Fluor 647 conjugated goat anti-mouse IgG secondary (Red in panels C, G and K). Panels C and G include AA staining from a mouse exposed to tremolite asbestos. Panel K includes AA staining from a mouse exposed to wollastonite fibers. Right panels (D, H and L) show merged images. Colocalization of SSA/Ro52 and autoantigens recognized by asbestos-induced mouse AAs is visualized in yellow in merged images and indicated by arrows. Colocalization was confirmed through Image J analysis.

    Journal: Toxicology

    Article Title: Autoantibodies from mice exposed to Libby amphibole asbestos bind SSA/Ro52 - enriched apoptotic blebs of murine macrophages

    doi: 10.1016/j.tox.2008.01.008

    Figure Lengend Snippet: Autoantibodies from asbestos-exposed mice recognize apoptotic blebs enriched with the SSA/Ro52 autoantigen. Representative confocal microcopy images of RAW264.7 cells exposed to Libby asbestos for 48 h. The SSA/Ro52 autoantigen was visualized through confocal microscopy using a rabbit polyclonal anti-SSA/Ro52 antibody and an Alexa Fluor 488 conjugated goat anti-rabbit IgG secondary (Green in panels A, E and I). Nuclei were counterstained with propidium iodide (Cyan in panels B, F and J). Apoptotic nuclei are indicated by arrows. Binding of mouse autoantibodies were visualized with an Alexa Fluor 647 conjugated goat anti-mouse IgG secondary (Red in panels C, G and K). Panels C and G include AA staining from a mouse exposed to tremolite asbestos. Panel K includes AA staining from a mouse exposed to wollastonite fibers. Right panels (D, H and L) show merged images. Colocalization of SSA/Ro52 and autoantigens recognized by asbestos-induced mouse AAs is visualized in yellow in merged images and indicated by arrows. Colocalization was confirmed through Image J analysis.

    Article Snippet: Bound autoantibodies from asbestos exposed mice were detected using an Alexa Fluor 647-conjugated goat anti-mouse IgG antibody (Molecular Probes).

    Techniques: Mouse Assay, Confocal Microscopy, Binding Assay, Staining, Atomic Absorption Spectroscopy

    Role of CCR5 dimerization in HIV-1 entry into T-cells. A Fusion kinetics of BlaM-vpr-containing virus #25 or 34 with CD4+ A3.01 T-cells expressing FLAG/SNAP-tagged WT-CCR5 or L196K-CCR5. Data points represent means ± SEM of 2 independent determinations (out of 5). B Gating strategy of A3.01 cells expressing WT-CCR5 (red) or L196K-CCR5 (blue) at a low (GMFI = 111 and 123 for WT-CCR5 and L196K-CCR5, respectively), intermediate (599 and 533) or high level (2903 and 2382). Shown are representative flow cytometry plots of cell side scatter vs receptor expression level revealed with the AlexaFluor 647-conjugated anti-FLAG mAb M2. On the whole cell populations, both receptors were expressed at similar expression levels (GMFI = 362 and 312 for WT-CCR5 and L196K-CCR5, respectively). Comparable results were obtained using the unconjugated M2 revealed by an AlexaFluor 647-conjugated goat anti-mouse IgG (GAM) (GMFI = 5871 and 3342) C , D and E The virus-cell fusion experiments shown in A were analyzed with A3.01 T-cells expressing low ( C ), intermediate ( D ) or high ( E ) cell surface level of either WT- or L196K-CCR5. F Levels of fusion at 3 h for the indicated viruses were measured with A3.01 T-cells expressing low (L) or high (H) level of either WT- (red bars) or L196K-CCR5 (blue bars). Results are means ± SEM of 3 independent determinations (except for the non-M and M-tropic viruses JR-CSF and JR-FL where n = 1). In panels A , C , D , E and F , results are expressed as percents of fusion relative to the maximum extent of fusion (F max ) of virus #34 with L196K-CCR5-expressing cells. This F max value, expressed as the percentage of cells containing BlaM-vpr, ranged between 40–60% and did not vary with the receptor expression level.

    Journal: PLoS Pathogens

    Article Title: CCR5 structural plasticity shapes HIV-1 phenotypic properties

    doi: 10.1371/journal.ppat.1007432

    Figure Lengend Snippet: Role of CCR5 dimerization in HIV-1 entry into T-cells. A Fusion kinetics of BlaM-vpr-containing virus #25 or 34 with CD4+ A3.01 T-cells expressing FLAG/SNAP-tagged WT-CCR5 or L196K-CCR5. Data points represent means ± SEM of 2 independent determinations (out of 5). B Gating strategy of A3.01 cells expressing WT-CCR5 (red) or L196K-CCR5 (blue) at a low (GMFI = 111 and 123 for WT-CCR5 and L196K-CCR5, respectively), intermediate (599 and 533) or high level (2903 and 2382). Shown are representative flow cytometry plots of cell side scatter vs receptor expression level revealed with the AlexaFluor 647-conjugated anti-FLAG mAb M2. On the whole cell populations, both receptors were expressed at similar expression levels (GMFI = 362 and 312 for WT-CCR5 and L196K-CCR5, respectively). Comparable results were obtained using the unconjugated M2 revealed by an AlexaFluor 647-conjugated goat anti-mouse IgG (GAM) (GMFI = 5871 and 3342) C , D and E The virus-cell fusion experiments shown in A were analyzed with A3.01 T-cells expressing low ( C ), intermediate ( D ) or high ( E ) cell surface level of either WT- or L196K-CCR5. F Levels of fusion at 3 h for the indicated viruses were measured with A3.01 T-cells expressing low (L) or high (H) level of either WT- (red bars) or L196K-CCR5 (blue bars). Results are means ± SEM of 3 independent determinations (except for the non-M and M-tropic viruses JR-CSF and JR-FL where n = 1). In panels A , C , D , E and F , results are expressed as percents of fusion relative to the maximum extent of fusion (F max ) of virus #34 with L196K-CCR5-expressing cells. This F max value, expressed as the percentage of cells containing BlaM-vpr, ranged between 40–60% and did not vary with the receptor expression level.

    Article Snippet: After two washing steps in ice-cold FACS buffer, cells were incubated at 4°C for 30 min in 0.1 ml FACS buffer containing AlexaFluor 647-conjugated goat anti-mouse IgG (Life Technologies) at a 1:500 dilution.

    Techniques: Expressing, Flow Cytometry, Cytometry

    Blood-derived HIV-1 isolates depend on CCR5 plasticity for infection of MDMs. A MDMs from 6 different healthy donors were infected by virus clones pseudotyped with gp160 #1, #10, #25, #34, #50 or #58, the M-tropic or the non-M-tropic HIV-1 strain JR-FL or JR-CSF, respectively, or recombinant viral populations generated from plasma (P) or cerebrospinal fluid (CSF) of two patients with HIV-1-associated encephalitis (P#B and P#J). Virus quantities that produced comparable levels of infectivity in T-cells isolated from the same donors ( i . e . 10 5 RLU) were used. Of note, similar results were obtained after normalizing the virus quantities to the p24 content. Results represent infectivities of the viruses in MDMs, determined in duplicate, and normalized to infectivity of JR-FL (arbitrarily set at 100%). B Sensitivity of viruses to sCD4. Some of the previous viruses were tested for their sensitivity to inhibition by increasing concentrations of sCD4 in infection experiments of PHA/IL-2- activated CD4 T-cells. The virus amounts were selected in such a way that infectivities in the absence of sCD4 were similar ( i . e . 10 5 RLU of luciferase activity). The data points shown are from one representative experiment performed in duplicate, out of three experiments performed independently. The independent experiments were carried out with the lymphocytes from different healthy donors. Infectivity of the viruses was expressed as percentage of that measured in the absence of sCD4 (100%). Inhibition curves were fitted according to a sigmoidal dose-response model with a variable slope. C The panel shows sCD4 IC 50 values that were deduced from inhibition curves with GraphPad Prism 6. Results are means ± SD of 3 independent determinations. D Dose-response inhibitions of infection of activated CD4 T-cells by increasing concentrations (ranging between 10 −12 and 3x10 -8 nM) of the anti-CD4 mAb Q4120 were carried out with the indicated viruses. Then, IC 50 values for inhibition of infection by Q4120 were calculated with GraphPad Prism 6. The data shown here represent means ± SEM of two independent experiments performed in duplicate. E Infection assays of Affinofile cells expressing CCR5 at a high level (≈ 10 5 receptors/cell, stimulated by 2 μM ponasterone A) and increasing amounts of CD4 stimulated by 7 different concentrations of minocycline ranging between 0.08 and 2.5 ng/ml (see “ Materials and methods ” for further details). Data points represent infectivities of viruses that were normalized to infectivity in Affinofile cells expressing the highest levels of CCR5 and CD4 (CD4 high /CCR5 high Affinofile cells), arbitrarily taken as 100%. One representative experiment out of three independent experiments performed in duplicate is shown. In those experiments, the quantities of the different viruses were adjusted in such a way that they generated similar RLU in CD4 high /CCR5 high Affinofile cells (10 5 ). However, similar results were also obtained when normalizing the quantities of viruses to the p24 content. F Infectivities of the indicated pseudotyped viruses in CD4 low /CCR5 high affinofile cells (cells that have not been stimulated by minocycline, and where the CD4 expression level is minimal, i . e . in the range of 4000 receptors/cell), expressed as percentage of the infectivity in CD4 high /CCR5 high Affinofile cells). G Receptor expression levels at the surface of untransduced (grey line) or transduced MDMs with pTRIP ΔU3-expressing FLAG-tagged WT-CCR5 (blue line) or L196K-CCR5 (magenta line). Results were obtained using the anti-Flag mAb M2 (left panel) or the anti-CCR5 mAb 2D7 (right panel) revealed by an AlexaFluor 647-conjugated goat anti-mouse IgG (GAM) and flow cytometry analysis. With the mAb M2, GMFI values equal to 7836 and 2010 were found for WT-CCR5 and L196K-CCR5. Background signal of untransduced MDMs labeled with GAM alone is represented as red lines. H Levels of fusion of BlaM-vpr-containing virus #25, virus #34, JR-CSF or JR-FL to untransduced or transduced MDMs. Fusion was measured by flow cytometry analysis 3 h post-inoculation, as described in the “Materials and Methods” section. Each data point represents the level of fusion of the indicated virus clone with MDMs from one donor, expressed as a percentage of MDMs where CCF2 is cleaved by BlaM. On the whole, four independent experiments with MDMs from four healthy individuals were done. The panel displays the means +/- SD of the results obtained from these 4 experiments.

    Journal: PLoS Pathogens

    Article Title: CCR5 structural plasticity shapes HIV-1 phenotypic properties

    doi: 10.1371/journal.ppat.1007432

    Figure Lengend Snippet: Blood-derived HIV-1 isolates depend on CCR5 plasticity for infection of MDMs. A MDMs from 6 different healthy donors were infected by virus clones pseudotyped with gp160 #1, #10, #25, #34, #50 or #58, the M-tropic or the non-M-tropic HIV-1 strain JR-FL or JR-CSF, respectively, or recombinant viral populations generated from plasma (P) or cerebrospinal fluid (CSF) of two patients with HIV-1-associated encephalitis (P#B and P#J). Virus quantities that produced comparable levels of infectivity in T-cells isolated from the same donors ( i . e . 10 5 RLU) were used. Of note, similar results were obtained after normalizing the virus quantities to the p24 content. Results represent infectivities of the viruses in MDMs, determined in duplicate, and normalized to infectivity of JR-FL (arbitrarily set at 100%). B Sensitivity of viruses to sCD4. Some of the previous viruses were tested for their sensitivity to inhibition by increasing concentrations of sCD4 in infection experiments of PHA/IL-2- activated CD4 T-cells. The virus amounts were selected in such a way that infectivities in the absence of sCD4 were similar ( i . e . 10 5 RLU of luciferase activity). The data points shown are from one representative experiment performed in duplicate, out of three experiments performed independently. The independent experiments were carried out with the lymphocytes from different healthy donors. Infectivity of the viruses was expressed as percentage of that measured in the absence of sCD4 (100%). Inhibition curves were fitted according to a sigmoidal dose-response model with a variable slope. C The panel shows sCD4 IC 50 values that were deduced from inhibition curves with GraphPad Prism 6. Results are means ± SD of 3 independent determinations. D Dose-response inhibitions of infection of activated CD4 T-cells by increasing concentrations (ranging between 10 −12 and 3x10 -8 nM) of the anti-CD4 mAb Q4120 were carried out with the indicated viruses. Then, IC 50 values for inhibition of infection by Q4120 were calculated with GraphPad Prism 6. The data shown here represent means ± SEM of two independent experiments performed in duplicate. E Infection assays of Affinofile cells expressing CCR5 at a high level (≈ 10 5 receptors/cell, stimulated by 2 μM ponasterone A) and increasing amounts of CD4 stimulated by 7 different concentrations of minocycline ranging between 0.08 and 2.5 ng/ml (see “ Materials and methods ” for further details). Data points represent infectivities of viruses that were normalized to infectivity in Affinofile cells expressing the highest levels of CCR5 and CD4 (CD4 high /CCR5 high Affinofile cells), arbitrarily taken as 100%. One representative experiment out of three independent experiments performed in duplicate is shown. In those experiments, the quantities of the different viruses were adjusted in such a way that they generated similar RLU in CD4 high /CCR5 high Affinofile cells (10 5 ). However, similar results were also obtained when normalizing the quantities of viruses to the p24 content. F Infectivities of the indicated pseudotyped viruses in CD4 low /CCR5 high affinofile cells (cells that have not been stimulated by minocycline, and where the CD4 expression level is minimal, i . e . in the range of 4000 receptors/cell), expressed as percentage of the infectivity in CD4 high /CCR5 high Affinofile cells). G Receptor expression levels at the surface of untransduced (grey line) or transduced MDMs with pTRIP ΔU3-expressing FLAG-tagged WT-CCR5 (blue line) or L196K-CCR5 (magenta line). Results were obtained using the anti-Flag mAb M2 (left panel) or the anti-CCR5 mAb 2D7 (right panel) revealed by an AlexaFluor 647-conjugated goat anti-mouse IgG (GAM) and flow cytometry analysis. With the mAb M2, GMFI values equal to 7836 and 2010 were found for WT-CCR5 and L196K-CCR5. Background signal of untransduced MDMs labeled with GAM alone is represented as red lines. H Levels of fusion of BlaM-vpr-containing virus #25, virus #34, JR-CSF or JR-FL to untransduced or transduced MDMs. Fusion was measured by flow cytometry analysis 3 h post-inoculation, as described in the “Materials and Methods” section. Each data point represents the level of fusion of the indicated virus clone with MDMs from one donor, expressed as a percentage of MDMs where CCF2 is cleaved by BlaM. On the whole, four independent experiments with MDMs from four healthy individuals were done. The panel displays the means +/- SD of the results obtained from these 4 experiments.

    Article Snippet: After two washing steps in ice-cold FACS buffer, cells were incubated at 4°C for 30 min in 0.1 ml FACS buffer containing AlexaFluor 647-conjugated goat anti-mouse IgG (Life Technologies) at a 1:500 dilution.

    Techniques: Derivative Assay, Infection, Clone Assay, Recombinant, Generated, Produced, Isolation, Inhibition, Luciferase, Activity Assay, Expressing, Flow Cytometry, Cytometry, Labeling

    HIV-1 Gag failed to localize to VCCs upon 5ptaseIV overexpression. (A) MDMs were infected with pseudotyped HIV-1 encoding Gag-YFP along with 5ptaseIV (FL) or 5ptaseIV Δ1. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594 (a PM marker), fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. (B) Pearson's correlation coefficients for colocalization of Gag-YFP with CD81 are shown as means and standard errors of the means (SEM). Twenty to 30 cells were analyzed per condition. **, P

    Journal: Journal of Virology

    Article Title: Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages

    doi: 10.1128/JVI.01004-16

    Figure Lengend Snippet: HIV-1 Gag failed to localize to VCCs upon 5ptaseIV overexpression. (A) MDMs were infected with pseudotyped HIV-1 encoding Gag-YFP along with 5ptaseIV (FL) or 5ptaseIV Δ1. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594 (a PM marker), fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. (B) Pearson's correlation coefficients for colocalization of Gag-YFP with CD81 are shown as means and standard errors of the means (SEM). Twenty to 30 cells were analyzed per condition. **, P

    Article Snippet: The cells were immunostained with anti-CD81 antibody (BD Biosciences Pharmingen, San Diego, CA) for 1 h at room temperature, washed twice with PBS, and stained with goat anti-mouse IgG conjugated to Alexa Fluor 647 (Invitrogen).

    Techniques: Over Expression, Infection, Staining, Labeling, Marker, Microscopy

    The myristate moiety but not the intact HIV-1 MA sequence is required for VCC localization. (A) MDMs were infected with pseudotyped HIV-1 encoding WT Gag-YFP or Gag-YFP derivatives containing the indicated MA substitutions. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594, fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. (B) Pearson's correlation coefficients for colocalization of Gag-YFP with CD81 are shown as means and SEM. Twenty to 30 cells were analyzed per condition. *, P

    Journal: Journal of Virology

    Article Title: Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages

    doi: 10.1128/JVI.01004-16

    Figure Lengend Snippet: The myristate moiety but not the intact HIV-1 MA sequence is required for VCC localization. (A) MDMs were infected with pseudotyped HIV-1 encoding WT Gag-YFP or Gag-YFP derivatives containing the indicated MA substitutions. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594, fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. (B) Pearson's correlation coefficients for colocalization of Gag-YFP with CD81 are shown as means and SEM. Twenty to 30 cells were analyzed per condition. *, P

    Article Snippet: The cells were immunostained with anti-CD81 antibody (BD Biosciences Pharmingen, San Diego, CA) for 1 h at room temperature, washed twice with PBS, and stained with goat anti-mouse IgG conjugated to Alexa Fluor 647 (Invitrogen).

    Techniques: Sequencing, Infection, Staining, Labeling, Microscopy

    Heterologous membrane binding sequences can replace HIV-1 MA without affecting VCC localization. (A) Schematic illustrations of WT, PH/ΔMA, Kmyr/ΔMA, and Fyn(10)/ΔMA Gag-YFP. (B) MDMs were infected with pseudotyped HIV-1 encoding WT Gag-YFP or Gag-YFP derivatives in which MA was replaced by a heterologous membrane binding sequence. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594, fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. (C) Pearson's correlation coefficients for colocalization of Gag-YFP with CD81 are shown as means and SEM. Twenty to 30 cells were analyzed per condition. n.s., not significant.

    Journal: Journal of Virology

    Article Title: Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages

    doi: 10.1128/JVI.01004-16

    Figure Lengend Snippet: Heterologous membrane binding sequences can replace HIV-1 MA without affecting VCC localization. (A) Schematic illustrations of WT, PH/ΔMA, Kmyr/ΔMA, and Fyn(10)/ΔMA Gag-YFP. (B) MDMs were infected with pseudotyped HIV-1 encoding WT Gag-YFP or Gag-YFP derivatives in which MA was replaced by a heterologous membrane binding sequence. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594, fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. (C) Pearson's correlation coefficients for colocalization of Gag-YFP with CD81 are shown as means and SEM. Twenty to 30 cells were analyzed per condition. n.s., not significant.

    Article Snippet: The cells were immunostained with anti-CD81 antibody (BD Biosciences Pharmingen, San Diego, CA) for 1 h at room temperature, washed twice with PBS, and stained with goat anti-mouse IgG conjugated to Alexa Fluor 647 (Invitrogen).

    Techniques: Binding Assay, Infection, Sequencing, Staining, Labeling, Microscopy

    HIV-1 Gag localization to VCCs requires higher-order multimerization. (A) Schematic illustrations of WT, EE75,76AA, delNC, LZ, and LZ4 Gag-YFP. LZ4 Gag-YFP contains the WM184,185AA CA mutation, which disrupts Gag dimerization, in addition to replacement of NC with a tetramer-forming LZ sequence. (B) MDMs were infected with pseudotyped HIV-1 encoding WT Gag-YFP or Gag-YFP derivatives containing the substitutions shown in panel A. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594, fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. Note that for cells expressing delNC Gag-YFP or LZ4 Gag-YFP, prominent YFP signals were found at the cell surface as detected by ConA (white arrowheads), whereas such surface YFP signals were nearly undetectable in WT Gag-YFP-expressing cells. (C) Pearson's correlation coefficients for colocalization of Gag-YFP with ConA are shown as means and SEM. Twenty to 40 cells were analyzed per condition. *, P

    Journal: Journal of Virology

    Article Title: Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages

    doi: 10.1128/JVI.01004-16

    Figure Lengend Snippet: HIV-1 Gag localization to VCCs requires higher-order multimerization. (A) Schematic illustrations of WT, EE75,76AA, delNC, LZ, and LZ4 Gag-YFP. LZ4 Gag-YFP contains the WM184,185AA CA mutation, which disrupts Gag dimerization, in addition to replacement of NC with a tetramer-forming LZ sequence. (B) MDMs were infected with pseudotyped HIV-1 encoding WT Gag-YFP or Gag-YFP derivatives containing the substitutions shown in panel A. At 48 h postinfection, cells were stained with ConA labeled with Alexa Fluor 594, fixed, immunostained with a mouse monoclonal anti-CD81 antibody and anti-mouse IgG conjugated with Alexa Fluor 647, and analyzed using a confocal microscope. Note that for cells expressing delNC Gag-YFP or LZ4 Gag-YFP, prominent YFP signals were found at the cell surface as detected by ConA (white arrowheads), whereas such surface YFP signals were nearly undetectable in WT Gag-YFP-expressing cells. (C) Pearson's correlation coefficients for colocalization of Gag-YFP with ConA are shown as means and SEM. Twenty to 40 cells were analyzed per condition. *, P

    Article Snippet: The cells were immunostained with anti-CD81 antibody (BD Biosciences Pharmingen, San Diego, CA) for 1 h at room temperature, washed twice with PBS, and stained with goat anti-mouse IgG conjugated to Alexa Fluor 647 (Invitrogen).

    Techniques: Mutagenesis, Sequencing, Infection, Staining, Labeling, Microscopy, Expressing

    Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated IgG (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Herpes Simplex Virus 1-Induced Blood-Brain Barrier Damage Involves Apoptosis Associated With GM130-Mediated Golgi Stress

    doi: 10.3389/fnmol.2020.00002

    Figure Lengend Snippet: Golgi apparatus (GA) disruption and cleaved-caspase 3 activations in Bend.3 cells infected with HSV-1. Bend.3 cells were mock-infected (mock) or infected with HSV-1 (V) at an MOI of 3 and then harvested at 12 hours post-infection (hpi), 24 hpi, 36 hpi, and 48 hpi. (A) GA disruption and cleaved-caspase 3 activations were detected by immunofluorescence analysis. Mock-infected or HSV-1 infected cells were fixed, permeabilized, and incubated with antibodies to GM130 and cleaved-caspase 3, followed by incubation with Alexa Fluor 594-conjugated IgG (red channel) and Alexa Fluor 647-conjugated IgG (cyan channel). Infected cells expressed green fluorescent protein (GFP; green channel). DAPI was used to stain nuclei (blue channel). Merged channels generated the fifth image shown in each row. Scale bar, 10 μm. (B) GA disruption was determined by transmission electron microscopy. GA regions (red box) were captured at a magnification of 2,500× in mock-infected (upper) and HSV-1 infected (lower) cells. Scale bar, 2 μm. Highly ordered Golgi stacks are observed in mock-infected cells at a magnification of 5,000× (black arrowheads). The ultrastructure of the GA in HSV-1-infected cells gradually varied from organized stacks to discontinued stacks and dilated-elongated Golgi cisternae (red arrowheads). Representative images are shown from three independent experiments. The asterisk indicates the nucleus. Scale bar, 1 μm.

    Article Snippet: Subsequently, the cells were incubated with Alexa Fluor 488-conjugated (Molecular Probes Cat# A-21202 also A21202 Lot# RRID: AB_141607 ), Alexa Fluor 594-conjugated (Molecular Probes Cat# A-21207 also A21207 Lot# RRID: AB_141637 ), and Alexa Fluor 647-conjugated (Molecular Probes Cat# A-21240 also A21240 Lot# RRID: AB_141658 ) secondary antibodies.

    Techniques: Infection, Immunofluorescence, Incubation, Staining, Generated, Transmission Assay, Electron Microscopy