anti ha  (Sino Biological)


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  • 93
    Name:
    Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA Antibody Rabbit PAb Antigen Affinity Purified
    Description:
    Produced in rabbits immunized with purified recombinant Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA Catalog 11062 V08H1 AAT73273 1 Met1 Gln531 Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA specific IgG was purified by Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA affinity chromatography
    Catalog Number:
    11062-T54
    Price:
    None
    Category:
    Primary Antibody
    Reactivity:
    H5N1
    Applications:
    WB,ELISA
    Immunogen:
    Recombinant Influenza A H5N1 (A/Vietnam/1194/2004) Hemagglutinin / HA Protein (Catalog#11062-V08H1)
    Antibody Type:
    PAb
    Host:
    Rabbit
    Isotype:
    Rabbit IgG
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    Structured Review

    Sino Biological anti ha
    Produced in rabbits immunized with purified recombinant Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA Catalog 11062 V08H1 AAT73273 1 Met1 Gln531 Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA specific IgG was purified by Influenza A H5N1 A Vietnam 1194 2004 Hemagglutinin HA affinity chromatography
    https://www.bioz.com/result/anti ha/product/Sino Biological
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti ha - by Bioz Stars, 2021-04
    93/100 stars

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    Article Title: A single dose of a vesicular stomatitis virus-based influenza vaccine confers rapid protection against H5 viruses from different clades
    Article Snippet: Protein detection was performed using the following rabbit or mouse primary antibodies: anti-HA 1:1000 (cat. #11062-T54-100, Sino Biological Inc.), anti-EBOV GP (ZGP 12/1.1, 1 μg/ml; kindly provided by Ayato Takada, Hokkaido University, Sapporo, Japan), and anti-VSV M (23H12, 1:1000; Kerafast Inc.).

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  • 92
    Sino Biological rabbit anti ha polyclonal antibody
    M2 interacts with TRAPPC6A and TRAPPC6AΔ in mammalian cells. (A to C) Plasmids expressing TRAPPC6A-Myc and Flag-SC09M2 (A), TRAPPC6A-Myc and Flag-AH05M2 (B), or TRAPPC6A-Myc and Flag-WSNM2 (C) were transfected individually or in combination, as indicated, in HEK293T cells. Forty-eight hours after transfection, cell lysates were immunoprecipitated with a mouse anti-Flag MAb or a mouse anti-Myc MAb and were subjected to Western blotting with a rabbit anti-Flag <t>polyclonal</t> antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively. (D) Western blotting of proteins bound to GST alone or to GST-TRAPPC6A. HEK293T cells transfected with pCAGGS-SC09M2 or with the pCAGGS vector were lysed with IP buffer, and the lysate was incubated with purified GST or GST-TRAPPC6A and then subjected to a pulldown assay. Equal volumes of proteins bound to the beads and the original cell lysates (5% of the input) were examined by Western blotting using a mouse anti-M2 MAb or a mouse anti-actin MAb, respectively. The GST-tagged proteins in the eluates were detected by Coomassie blue (CB) staining. (E) Confocal analysis of the distribution of M2 and TRAPPC6A proteins in A549 cells. pCAGGS-TRAPPC6A-myc and pCAGGS-Flag-SC09M2 were transfected individually or in combination into A549 cells and assessed by immunofluorescence staining. IAV M2 was detected with a mouse anti-Flag MAb and visualized with Alexa Fluor 488 (green). TRAPPC6A was detected with a rabbit anti-Myc polyclonal antibody and visualized with Alexa Fluor 546 (red). Yellow indicates colocalization of Alexa Fluor 546 and 488 in the merged image. (F) pCAGGS-TRAPPC6A-myc was cotransfected with pEGFP-C1 or pEGFP-C1-BM2 into HEK293T cells for 48 h before the cells were lysed. Following immunoprecipitation of the cell lysates with a mouse anti-GFP MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-GFP polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of BM2 and TRAPPC6A, respectively. (G) Co-IP of M2 and TRAPPC6AΔ. pCAGGS-Flag-SC09M2 was cotransfected with pCAGGS-TRAPPC6A-myc or pCAGGS-TRAPPC6AΔ-myc into HEK293T cells. Forty-eight hours after transfection, cell lysates were immunoprecipitated with a mouse anti-Myc MAb and subjected to Western blotting with a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A or TRAPPC6AΔ, respectively.
    Rabbit Anti Ha Polyclonal Antibody, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti ha polyclonal antibody/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti ha polyclonal antibody - by Bioz Stars, 2021-04
    92/100 stars
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    94
    Sino Biological influenza a virus hemagglutinin ha antibody rabbit mab
    Effect of λ-CGN on <t>influenza</t> A infection in vivo . BALB/c mice were mock-infected (black) or intranasally infected with maPR8 at 5 MLD50 (red). As test groups, the virus was preincubated at room temperature for 30 min with λ-CGN at a lower dose (1 mg/kg/d, bright green) or a higher dose (5 mg/kg/d, dark green), followed by intranasal administration. Control mice received oral OSV-P twice a day (10 mg/kg/d) at 8-h intervals, starting at 4 h before viral infection (blue). Body weight (A) and mortality (B) of mice were measured every day from Days 0 to 14 post-infection. Data are expressed as the mean ± SEM from five mice
    Influenza A Virus Hemagglutinin Ha Antibody Rabbit Mab, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/influenza a virus hemagglutinin ha antibody rabbit mab/product/Sino Biological
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    influenza a virus hemagglutinin ha antibody rabbit mab - by Bioz Stars, 2021-04
    94/100 stars
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    93
    Sino Biological ha specific igg1 amounts
    PD-1 co-expression results in a more balanced HA-specific antibody response. Antibody subtype patterns of HA-immunized mice three weeks after priming and two (week 6) and 14 weeks (week 18) after the booster immunization. The ring size represents the overall antibody response. Shown are mean percentages of 18 animals from three independent experiments. Each subtype was analyzed by ELISA with identical amounts of HRP-conjugated anti-mouse <t>IgG1</t> (blue), IgG2a (red), IgG2b (gray), and IgG3 (black) antibodies.
    Ha Specific Igg1 Amounts, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ha specific igg1 amounts/product/Sino Biological
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ha specific igg1 amounts - by Bioz Stars, 2021-04
    93/100 stars
      Buy from Supplier

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    M2 interacts with TRAPPC6A and TRAPPC6AΔ in mammalian cells. (A to C) Plasmids expressing TRAPPC6A-Myc and Flag-SC09M2 (A), TRAPPC6A-Myc and Flag-AH05M2 (B), or TRAPPC6A-Myc and Flag-WSNM2 (C) were transfected individually or in combination, as indicated, in HEK293T cells. Forty-eight hours after transfection, cell lysates were immunoprecipitated with a mouse anti-Flag MAb or a mouse anti-Myc MAb and were subjected to Western blotting with a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively. (D) Western blotting of proteins bound to GST alone or to GST-TRAPPC6A. HEK293T cells transfected with pCAGGS-SC09M2 or with the pCAGGS vector were lysed with IP buffer, and the lysate was incubated with purified GST or GST-TRAPPC6A and then subjected to a pulldown assay. Equal volumes of proteins bound to the beads and the original cell lysates (5% of the input) were examined by Western blotting using a mouse anti-M2 MAb or a mouse anti-actin MAb, respectively. The GST-tagged proteins in the eluates were detected by Coomassie blue (CB) staining. (E) Confocal analysis of the distribution of M2 and TRAPPC6A proteins in A549 cells. pCAGGS-TRAPPC6A-myc and pCAGGS-Flag-SC09M2 were transfected individually or in combination into A549 cells and assessed by immunofluorescence staining. IAV M2 was detected with a mouse anti-Flag MAb and visualized with Alexa Fluor 488 (green). TRAPPC6A was detected with a rabbit anti-Myc polyclonal antibody and visualized with Alexa Fluor 546 (red). Yellow indicates colocalization of Alexa Fluor 546 and 488 in the merged image. (F) pCAGGS-TRAPPC6A-myc was cotransfected with pEGFP-C1 or pEGFP-C1-BM2 into HEK293T cells for 48 h before the cells were lysed. Following immunoprecipitation of the cell lysates with a mouse anti-GFP MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-GFP polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of BM2 and TRAPPC6A, respectively. (G) Co-IP of M2 and TRAPPC6AΔ. pCAGGS-Flag-SC09M2 was cotransfected with pCAGGS-TRAPPC6A-myc or pCAGGS-TRAPPC6AΔ-myc into HEK293T cells. Forty-eight hours after transfection, cell lysates were immunoprecipitated with a mouse anti-Myc MAb and subjected to Western blotting with a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A or TRAPPC6AΔ, respectively.

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: M2 interacts with TRAPPC6A and TRAPPC6AΔ in mammalian cells. (A to C) Plasmids expressing TRAPPC6A-Myc and Flag-SC09M2 (A), TRAPPC6A-Myc and Flag-AH05M2 (B), or TRAPPC6A-Myc and Flag-WSNM2 (C) were transfected individually or in combination, as indicated, in HEK293T cells. Forty-eight hours after transfection, cell lysates were immunoprecipitated with a mouse anti-Flag MAb or a mouse anti-Myc MAb and were subjected to Western blotting with a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively. (D) Western blotting of proteins bound to GST alone or to GST-TRAPPC6A. HEK293T cells transfected with pCAGGS-SC09M2 or with the pCAGGS vector were lysed with IP buffer, and the lysate was incubated with purified GST or GST-TRAPPC6A and then subjected to a pulldown assay. Equal volumes of proteins bound to the beads and the original cell lysates (5% of the input) were examined by Western blotting using a mouse anti-M2 MAb or a mouse anti-actin MAb, respectively. The GST-tagged proteins in the eluates were detected by Coomassie blue (CB) staining. (E) Confocal analysis of the distribution of M2 and TRAPPC6A proteins in A549 cells. pCAGGS-TRAPPC6A-myc and pCAGGS-Flag-SC09M2 were transfected individually or in combination into A549 cells and assessed by immunofluorescence staining. IAV M2 was detected with a mouse anti-Flag MAb and visualized with Alexa Fluor 488 (green). TRAPPC6A was detected with a rabbit anti-Myc polyclonal antibody and visualized with Alexa Fluor 546 (red). Yellow indicates colocalization of Alexa Fluor 546 and 488 in the merged image. (F) pCAGGS-TRAPPC6A-myc was cotransfected with pEGFP-C1 or pEGFP-C1-BM2 into HEK293T cells for 48 h before the cells were lysed. Following immunoprecipitation of the cell lysates with a mouse anti-GFP MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-GFP polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of BM2 and TRAPPC6A, respectively. (G) Co-IP of M2 and TRAPPC6AΔ. pCAGGS-Flag-SC09M2 was cotransfected with pCAGGS-TRAPPC6A-myc or pCAGGS-TRAPPC6AΔ-myc into HEK293T cells. Forty-eight hours after transfection, cell lysates were immunoprecipitated with a mouse anti-Myc MAb and subjected to Western blotting with a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A or TRAPPC6AΔ, respectively.

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Expressing, Transfection, Immunoprecipitation, Western Blot, Plasmid Preparation, Incubation, Purification, Staining, Immunofluorescence, Co-Immunoprecipitation Assay

    A leucine residue at position 96 of M2 is required for the TRAPPC6A interaction. (A) pCAGGS-TRAPPC6A-myc was cotransfected with pEGFP-C1, pEGFP-C1-SC09 M2, pEGFP-C1-SC09 M2EDTM, or pEGFP-C1-SC09 M2CT into HEK293T cells for 48 h before preparation for cell lysates. Following immunoprecipitation with a mouse anti-GFP MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-GFP polyclonal antibody and a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively. (B and C) Plasmids expressing TRAPPC6A-myc and Flag-SC09M2 or Flag-SC09M2 with different amino acid deletions in the C terminus were cotransfected into HEK293T cells for 48 h before the preparation of cell lysates. Following immunoprecipitation with a mouse anti-Flag MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively.

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: A leucine residue at position 96 of M2 is required for the TRAPPC6A interaction. (A) pCAGGS-TRAPPC6A-myc was cotransfected with pEGFP-C1, pEGFP-C1-SC09 M2, pEGFP-C1-SC09 M2EDTM, or pEGFP-C1-SC09 M2CT into HEK293T cells for 48 h before preparation for cell lysates. Following immunoprecipitation with a mouse anti-GFP MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-GFP polyclonal antibody and a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively. (B and C) Plasmids expressing TRAPPC6A-myc and Flag-SC09M2 or Flag-SC09M2 with different amino acid deletions in the C terminus were cotransfected into HEK293T cells for 48 h before the preparation of cell lysates. Following immunoprecipitation with a mouse anti-Flag MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively.

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Immunoprecipitation, Western Blot, Expressing

    Dynamics of the interaction of M2 and TRAPPC6AΔ in wt and mutant WSN virus-infected cells. A549 cells were infected with wt influenza virus WSN (A), or one of the M2 deletion mutants WSN M2Del1 (B) and WSN M2Del2 (C), at an MOI of 5. At 4, 6, 8, 10, and 14 h p.i., the infected cells were fixed and stained with mouse anti-M2 MAb 14C2 and rabbit anti-TRAPPC6A polyclonal antibody, followed by incubation with Alexa Fluor 488 donkey anti-mouse IgG(H+L) (green) and Alexa Fluor 546 donkey anti-rabbit IgG(H+L) (red). Nuclei were stained with DAPI.

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: Dynamics of the interaction of M2 and TRAPPC6AΔ in wt and mutant WSN virus-infected cells. A549 cells were infected with wt influenza virus WSN (A), or one of the M2 deletion mutants WSN M2Del1 (B) and WSN M2Del2 (C), at an MOI of 5. At 4, 6, 8, 10, and 14 h p.i., the infected cells were fixed and stained with mouse anti-M2 MAb 14C2 and rabbit anti-TRAPPC6A polyclonal antibody, followed by incubation with Alexa Fluor 488 donkey anti-mouse IgG(H+L) (green) and Alexa Fluor 546 donkey anti-rabbit IgG(H+L) (red). Nuclei were stained with DAPI.

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Mutagenesis, Infection, Staining, Incubation

    Mutation at position 96 of M2 affects its interaction with TRAPPC6A. (A) Sequence analysis of IAV M2 at position 96. All of the IAV M2 sequences deposited in GenBank by 6 July 2014 were downloaded. The identity of the amino acids at position 96 was statistically analyzed. (B) Plasmids expressing TRAPPC6A-Myc and Flag-WSNM2 or Flag-WSNM2 with different mutations at position 96 were cotransfected into HEK293T cells for 48 h before the preparation of cell lysates. Following immunoprecipitation with a mouse anti-Flag MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively.

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: Mutation at position 96 of M2 affects its interaction with TRAPPC6A. (A) Sequence analysis of IAV M2 at position 96. All of the IAV M2 sequences deposited in GenBank by 6 July 2014 were downloaded. The identity of the amino acids at position 96 was statistically analyzed. (B) Plasmids expressing TRAPPC6A-Myc and Flag-WSNM2 or Flag-WSNM2 with different mutations at position 96 were cotransfected into HEK293T cells for 48 h before the preparation of cell lysates. Following immunoprecipitation with a mouse anti-Flag MAb, the immunoprecipitates were analyzed by Western blotting using a rabbit anti-Flag polyclonal antibody or a rabbit anti-Myc polyclonal antibody to reveal the presence of M2 and TRAPPC6A, respectively.

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Mutagenesis, Sequencing, Expressing, Immunoprecipitation, Western Blot

    Effect of modulation of TRAPPC6AΔ expression on the cell surface expression of viral and cellular proteins. (A) A549 cells were transfected with siRNA targeting TRAPPC6AΔ or with nontargeting siRNA for 48 h and were then infected with the WSN virus at an MOI of 3. Cell lysates were processed at 8 and 10 h p.i. and subjected to Western blotting using a mouse anti-M2 MAb to detect the expression level of M2. (B) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. Cells were fixed at 8 and 10 h p.i., left nonpermeabilized, and stained with the mouse anti-M2 MAb and Alexa Fluor 488-conjugated donkey anti-mouse IgG(H+L) for M2 surface expression analysis by flow cytometry. The graph shows the fluorescence intensity of M2 surface expression. (C) The TRAPPC6AΔ-overexpressing A549 cell line or the A549 control cell line transduced with an empty retrovirus was infected with the WSN virus at an MOI of 3. Cell lysates were processed at 8 and 10 h p.i. and subjected to Western blotting using a mouse anti-M2 MAb to detect the expression level of M2. (D) The TRAPPC6AΔ-overexpressing A549 cell line or the A549 control cell line transduced with an empty retrovirus was infected with the WSN virus at an MOI of 3. The cell surface expression of M2 was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B. (E) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. The cell surface expression of HA was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B by using the rabbit anti-HA polyclonal antibody and Alexa Fluor 488-conjugated goat anti-rabbit IgG(H+L). (F) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. The cell surface expression of FGF2 was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B by using the rabbit anti-FGF2 MAb and Alexa Fluor 488-conjugated goat anti-rabbit IgG(H+L). (G) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. At 2 h p.i., the culture medium was replaced with medium supplemented with 25 μM amantadine. The cell surface expression of M2 was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B.

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: Effect of modulation of TRAPPC6AΔ expression on the cell surface expression of viral and cellular proteins. (A) A549 cells were transfected with siRNA targeting TRAPPC6AΔ or with nontargeting siRNA for 48 h and were then infected with the WSN virus at an MOI of 3. Cell lysates were processed at 8 and 10 h p.i. and subjected to Western blotting using a mouse anti-M2 MAb to detect the expression level of M2. (B) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. Cells were fixed at 8 and 10 h p.i., left nonpermeabilized, and stained with the mouse anti-M2 MAb and Alexa Fluor 488-conjugated donkey anti-mouse IgG(H+L) for M2 surface expression analysis by flow cytometry. The graph shows the fluorescence intensity of M2 surface expression. (C) The TRAPPC6AΔ-overexpressing A549 cell line or the A549 control cell line transduced with an empty retrovirus was infected with the WSN virus at an MOI of 3. Cell lysates were processed at 8 and 10 h p.i. and subjected to Western blotting using a mouse anti-M2 MAb to detect the expression level of M2. (D) The TRAPPC6AΔ-overexpressing A549 cell line or the A549 control cell line transduced with an empty retrovirus was infected with the WSN virus at an MOI of 3. The cell surface expression of M2 was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B. (E) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. The cell surface expression of HA was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B by using the rabbit anti-HA polyclonal antibody and Alexa Fluor 488-conjugated goat anti-rabbit IgG(H+L). (F) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. The cell surface expression of FGF2 was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B by using the rabbit anti-FGF2 MAb and Alexa Fluor 488-conjugated goat anti-rabbit IgG(H+L). (G) A549 cells were treated with siRNA and infected with the WSN virus as described above for panel A. At 2 h p.i., the culture medium was replaced with medium supplemented with 25 μM amantadine. The cell surface expression of M2 was analyzed by flow cytometry at 8 and 10 h p.i. as described above for panel B.

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Expressing, Transfection, Infection, Western Blot, Staining, Flow Cytometry, Cytometry, Fluorescence, Transduction

    TRAPPC6AΔ positively modulates influenza virus infection. (A) Endogenous expression of TRAPPC6AΔ in A549 cells. Whole lysates of A549 cells grown in 12-well plates were subjected to Western blotting with a rabbit anti-TRAPPC6A polyclonal antibody. HEK293T cell lysates transiently transfected with pCAGGS-TRAPPC6A or pCAGGS-TRAPPC6AΔ were used as a control. (B) siRNA knockdown of TRAPPC6AΔ in A549 cells. A549 cells were transfected with siRNA targeting TRAPPC6AΔ or nontargeting siRNA for 48 h. Whole-cell lysates were then collected and analyzed by Western blotting with a rabbit anti-TRAPPC6A polyclonal antibody. (C) Cell viability of siRNA-treated A549 cells measured by using the CellTiter-Glo assay. A549 cells were transfected with siRNA as described above for panel B. The data are presented as means ± standard deviations for triplicate transfections. (D) Virus replication in siRNA-treated A549 cells. Cells transfected with siRNA as described above for panel B were infected with WSN virus. At 24 and 48 h p.i., supernatants were collected and titrated for infectious virus by plaque assays in MDCK cells. Three independent experiments were performed, and data are shown as means ± standard deviations for triplicates from a representative experiment. **, P

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: TRAPPC6AΔ positively modulates influenza virus infection. (A) Endogenous expression of TRAPPC6AΔ in A549 cells. Whole lysates of A549 cells grown in 12-well plates were subjected to Western blotting with a rabbit anti-TRAPPC6A polyclonal antibody. HEK293T cell lysates transiently transfected with pCAGGS-TRAPPC6A or pCAGGS-TRAPPC6AΔ were used as a control. (B) siRNA knockdown of TRAPPC6AΔ in A549 cells. A549 cells were transfected with siRNA targeting TRAPPC6AΔ or nontargeting siRNA for 48 h. Whole-cell lysates were then collected and analyzed by Western blotting with a rabbit anti-TRAPPC6A polyclonal antibody. (C) Cell viability of siRNA-treated A549 cells measured by using the CellTiter-Glo assay. A549 cells were transfected with siRNA as described above for panel B. The data are presented as means ± standard deviations for triplicate transfections. (D) Virus replication in siRNA-treated A549 cells. Cells transfected with siRNA as described above for panel B were infected with WSN virus. At 24 and 48 h p.i., supernatants were collected and titrated for infectious virus by plaque assays in MDCK cells. Three independent experiments were performed, and data are shown as means ± standard deviations for triplicates from a representative experiment. **, P

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Infection, Expressing, Western Blot, Transfection, Glo Assay

    Confocal microscopy of WSN virus-infected cells stained for the Golgi apparatus or lysosomes. A549 cells were infected with the wt WSN virus at an MOI of 5. At the indicated time points, infected cells were fixed and stained with mouse anti-Giantin MAb and rabbit anti-M2 polyclonal antibody (A), mouse anti-LAMP1 MAb and rabbit anti-M2 polyclonal antibody (B), or mouse anti-LAMP1 MAb and rabbit anti-TRAPPC6A polyclonal antibody (C), followed by incubation with Alexa Fluor 488 donkey anti-mouse IgG(H+L) (green) and Alexa Fluor 546 donkey anti-rabbit IgG(H+L) (red). Nuclei were stained with DAPI.

    Journal: Journal of Virology

    Article Title: Host Cellular Protein TRAPPC6AΔ Interacts with Influenza A Virus M2 Protein and Regulates Viral Propagation by Modulating M2 Trafficking

    doi: 10.1128/JVI.01757-16

    Figure Lengend Snippet: Confocal microscopy of WSN virus-infected cells stained for the Golgi apparatus or lysosomes. A549 cells were infected with the wt WSN virus at an MOI of 5. At the indicated time points, infected cells were fixed and stained with mouse anti-Giantin MAb and rabbit anti-M2 polyclonal antibody (A), mouse anti-LAMP1 MAb and rabbit anti-M2 polyclonal antibody (B), or mouse anti-LAMP1 MAb and rabbit anti-TRAPPC6A polyclonal antibody (C), followed by incubation with Alexa Fluor 488 donkey anti-mouse IgG(H+L) (green) and Alexa Fluor 546 donkey anti-rabbit IgG(H+L) (red). Nuclei were stained with DAPI.

    Article Snippet: The following primary antibodies were obtained from commercial sources: rabbit anti-Flag polyclonal antibody (F7425; Sigma-Aldrich), mouse anti-Flag monoclonal antibody (F3165; Sigma-Aldrich), rabbit anti-Myc polyclonal antibody (C3965; Sigma-Aldrich), mouse anti-Myc monoclonal antibody (M4439; Sigma-Aldrich), mouse anti-actin monoclonal antibody (sc-47778; Santa Cruz, Dallas, TX), rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) polyclonal antibody (10494-1-AP; Proteintech, Chicago, IL), rabbit anti-GFP polyclonal antibody (AG279; Beyotime Biotech, Shanghai, China), mouse anti-GFP monoclonal antibody (ab1218; Abcam, Cambridge, MA), mouse anti-M2 monoclonal antibody (ab5416; Abcam), rabbit anti-M2 polyclonal antibody (GTX125951; GeneTex, Irvine, CA), rabbit anti-HA polyclonal antibody (11692-T54; Sino Biological Inc., Beijing, China), rabbit anti-FGF2 monoclonal antibody (ab92337; Abcam), mouse anti-LAMP1 monoclonal antibody (ab25630; Abcam), and mouse anti-Giantin monoclonal antibody (ab37266; Abcam).

    Techniques: Confocal Microscopy, Infection, Staining, Incubation

    Effect of λ-CGN on influenza A infection in vivo . BALB/c mice were mock-infected (black) or intranasally infected with maPR8 at 5 MLD50 (red). As test groups, the virus was preincubated at room temperature for 30 min with λ-CGN at a lower dose (1 mg/kg/d, bright green) or a higher dose (5 mg/kg/d, dark green), followed by intranasal administration. Control mice received oral OSV-P twice a day (10 mg/kg/d) at 8-h intervals, starting at 4 h before viral infection (blue). Body weight (A) and mortality (B) of mice were measured every day from Days 0 to 14 post-infection. Data are expressed as the mean ± SEM from five mice

    Journal: bioRxiv

    Article Title: Antiviral activity of lambda-carrageenan against influenza viruses in mice and severe acute respiratory syndrome coronavirus 2 in vitro

    doi: 10.1101/2020.08.23.255364

    Figure Lengend Snippet: Effect of λ-CGN on influenza A infection in vivo . BALB/c mice were mock-infected (black) or intranasally infected with maPR8 at 5 MLD50 (red). As test groups, the virus was preincubated at room temperature for 30 min with λ-CGN at a lower dose (1 mg/kg/d, bright green) or a higher dose (5 mg/kg/d, dark green), followed by intranasal administration. Control mice received oral OSV-P twice a day (10 mg/kg/d) at 8-h intervals, starting at 4 h before viral infection (blue). Body weight (A) and mortality (B) of mice were measured every day from Days 0 to 14 post-infection. Data are expressed as the mean ± SEM from five mice

    Article Snippet: Viral NP and HA proteins were detected using mouse anti-NP (catalog no. 11675-MM03; Sino Biological, Beijing, China) and rabbit anti-HA2 (catalog no. 86001-RM01; Sino Biological) antibodies, respectively, according to our previous report .

    Techniques: Infection, In Vivo, Mouse Assay

    Effect of λ-CGN on the intracellular entry of influenza A virus. MDCK cells were infected with PR8 (MOI, 5) and subsequently mock-treated or treated either with λ-CGN or with p-KG03 at a concentration of 10 μg/ml. At 4 h p.i. in the absence of CHX (A) or at 2.5 h in the presence of 10 μg/ml CHX (B), viral NP was detected with an anti-NP antibody and an Alex Fluor 488-conjugated goat anti-mouse secondary antibody (green). Cell nuclei were counterstained with DAPI (blue). Original magnification, 400×.

    Journal: bioRxiv

    Article Title: Antiviral activity of lambda-carrageenan against influenza viruses in mice and severe acute respiratory syndrome coronavirus 2 in vitro

    doi: 10.1101/2020.08.23.255364

    Figure Lengend Snippet: Effect of λ-CGN on the intracellular entry of influenza A virus. MDCK cells were infected with PR8 (MOI, 5) and subsequently mock-treated or treated either with λ-CGN or with p-KG03 at a concentration of 10 μg/ml. At 4 h p.i. in the absence of CHX (A) or at 2.5 h in the presence of 10 μg/ml CHX (B), viral NP was detected with an anti-NP antibody and an Alex Fluor 488-conjugated goat anti-mouse secondary antibody (green). Cell nuclei were counterstained with DAPI (blue). Original magnification, 400×.

    Article Snippet: Viral NP and HA proteins were detected using mouse anti-NP (catalog no. 11675-MM03; Sino Biological, Beijing, China) and rabbit anti-HA2 (catalog no. 86001-RM01; Sino Biological) antibodies, respectively, according to our previous report .

    Techniques: Infection, Concentration Assay

    Antiviral effect of λ-CGN against influenza A virus in vivo. BALB/c mice (6–7 weeks old female) were mock-infected (black) or intranasally infected with maPR8 at 5 MLD 50 (red). As test groups, the virus was preincubated at room temperature for 30 min with λ-CGN at a lower dose (1 mg/kg/d, purple) or a higher dose (5 mg/kg/d, green), followed by intranasal administration. Control mice received OSV-P orally twice a day (10 mg/kg/d) at 8-h intervals, starting at 4 h before viral infection (blue). Body weight ( A ) and mortality ( B ) of mice were measured every day from days 0 to 14 post-infection. Data are expressed as the mean ± S.D. from five mice. Survival statistics were calculated by Log-rank (Mantel–Cox) test. ** P

    Journal: Scientific Reports

    Article Title: Antiviral activity of lambda-carrageenan against influenza viruses and severe acute respiratory syndrome coronavirus 2

    doi: 10.1038/s41598-020-80896-9

    Figure Lengend Snippet: Antiviral effect of λ-CGN against influenza A virus in vivo. BALB/c mice (6–7 weeks old female) were mock-infected (black) or intranasally infected with maPR8 at 5 MLD 50 (red). As test groups, the virus was preincubated at room temperature for 30 min with λ-CGN at a lower dose (1 mg/kg/d, purple) or a higher dose (5 mg/kg/d, green), followed by intranasal administration. Control mice received OSV-P orally twice a day (10 mg/kg/d) at 8-h intervals, starting at 4 h before viral infection (blue). Body weight ( A ) and mortality ( B ) of mice were measured every day from days 0 to 14 post-infection. Data are expressed as the mean ± S.D. from five mice. Survival statistics were calculated by Log-rank (Mantel–Cox) test. ** P

    Article Snippet: Influenza viral NP and HA proteins were detected using mouse anti-NP (Cat. No., 11675-MM03; Sino Biological, Beijing, China) and rabbit anti-HA2 (Cat. No., 86001-RM01; Sino Biological) antibodies, respectively, according to our previous report .

    Techniques: In Vivo, Mouse Assay, Infection

    Effect of λ-CGN on the influenza A virus entry. ( A ) HA inhibition assay. Two-fold serially diluted PR8 (from 2 3 to 2 11 ) in PBS was incubated with an equal volume of PBS or twofold increasing concentrations of λ-CGN for 20 min. HA titer in each combination was determined at 30 min after addition of 0.5% chicken RBC. HA titers are marked on the right side of the panel. ( B , C ) Confocal microscopy. MDCK cells were infected with PR8 (MOI, 5) in the absence (Mock) or presence of either λ-CGN or p-KG03 at a concentration of 10 μg/ml. At 4 h post-infection in the absence of CHX ( B ) or at 2.5 h in the presence of 10 μg/ml CHX ( C ), viral NP was detected with an anti-NP antibody and an Alex Fluor 488-conjugated goat anti-mouse secondary antibody (green). Cell nuclei were counterstained with DAPI (blue). Original magnification, 400×. The images were analyzed using ZEN blue software 3.1 ( www.zeiss.com ).

    Journal: Scientific Reports

    Article Title: Antiviral activity of lambda-carrageenan against influenza viruses and severe acute respiratory syndrome coronavirus 2

    doi: 10.1038/s41598-020-80896-9

    Figure Lengend Snippet: Effect of λ-CGN on the influenza A virus entry. ( A ) HA inhibition assay. Two-fold serially diluted PR8 (from 2 3 to 2 11 ) in PBS was incubated with an equal volume of PBS or twofold increasing concentrations of λ-CGN for 20 min. HA titer in each combination was determined at 30 min after addition of 0.5% chicken RBC. HA titers are marked on the right side of the panel. ( B , C ) Confocal microscopy. MDCK cells were infected with PR8 (MOI, 5) in the absence (Mock) or presence of either λ-CGN or p-KG03 at a concentration of 10 μg/ml. At 4 h post-infection in the absence of CHX ( B ) or at 2.5 h in the presence of 10 μg/ml CHX ( C ), viral NP was detected with an anti-NP antibody and an Alex Fluor 488-conjugated goat anti-mouse secondary antibody (green). Cell nuclei were counterstained with DAPI (blue). Original magnification, 400×. The images were analyzed using ZEN blue software 3.1 ( www.zeiss.com ).

    Article Snippet: Influenza viral NP and HA proteins were detected using mouse anti-NP (Cat. No., 11675-MM03; Sino Biological, Beijing, China) and rabbit anti-HA2 (Cat. No., 86001-RM01; Sino Biological) antibodies, respectively, according to our previous report .

    Techniques: Inhibition, Incubation, Confocal Microscopy, Infection, Concentration Assay, Software

    Inhibition of infection by influenza A virus (H1N1) HA/NA- or SARS-CoV-2 spike-pseudotyped viruses. Lentiviral pseudotypes bearing influenza A virus (H1N1) HA and NA proteins (black bars) or SARS-CoV-2 spike protein (gray bars) were prepared, in which a firefly luciferase-expressing plasmid was incorporated. They were preincubated with mock or increasing concentrations of λ-CGN for 2 h at 37 °C and then infected into Vero E6 cells. On day 2, relative firefly luciferase activity (RLU) was determined by fixing the mock-treated sample at 100%. Data are expressed as the mean ± S.D. of three independent experiments. **** P

    Journal: Scientific Reports

    Article Title: Antiviral activity of lambda-carrageenan against influenza viruses and severe acute respiratory syndrome coronavirus 2

    doi: 10.1038/s41598-020-80896-9

    Figure Lengend Snippet: Inhibition of infection by influenza A virus (H1N1) HA/NA- or SARS-CoV-2 spike-pseudotyped viruses. Lentiviral pseudotypes bearing influenza A virus (H1N1) HA and NA proteins (black bars) or SARS-CoV-2 spike protein (gray bars) were prepared, in which a firefly luciferase-expressing plasmid was incorporated. They were preincubated with mock or increasing concentrations of λ-CGN for 2 h at 37 °C and then infected into Vero E6 cells. On day 2, relative firefly luciferase activity (RLU) was determined by fixing the mock-treated sample at 100%. Data are expressed as the mean ± S.D. of three independent experiments. **** P

    Article Snippet: Influenza viral NP and HA proteins were detected using mouse anti-NP (Cat. No., 11675-MM03; Sino Biological, Beijing, China) and rabbit anti-HA2 (Cat. No., 86001-RM01; Sino Biological) antibodies, respectively, according to our previous report .

    Techniques: Inhibition, Infection, Luciferase, Expressing, Plasmid Preparation, Activity Assay

    PD-1 co-expression results in a more balanced HA-specific antibody response. Antibody subtype patterns of HA-immunized mice three weeks after priming and two (week 6) and 14 weeks (week 18) after the booster immunization. The ring size represents the overall antibody response. Shown are mean percentages of 18 animals from three independent experiments. Each subtype was analyzed by ELISA with identical amounts of HRP-conjugated anti-mouse IgG1 (blue), IgG2a (red), IgG2b (gray), and IgG3 (black) antibodies.

    Journal: Vaccines

    Article Title: Genetic Co-Administration of Soluble PD-1 Ectodomains Modifies Immune Responses against Influenza A Virus Induced by DNA Vaccination

    doi: 10.3390/vaccines8040570

    Figure Lengend Snippet: PD-1 co-expression results in a more balanced HA-specific antibody response. Antibody subtype patterns of HA-immunized mice three weeks after priming and two (week 6) and 14 weeks (week 18) after the booster immunization. The ring size represents the overall antibody response. Shown are mean percentages of 18 animals from three independent experiments. Each subtype was analyzed by ELISA with identical amounts of HRP-conjugated anti-mouse IgG1 (blue), IgG2a (red), IgG2b (gray), and IgG3 (black) antibodies.

    Article Snippet: Quantitative analysis of the HA-specific IgG1 amounts was performed using a monoclonal anti-influenza Hemagglutinin antibody (2F1A7, IgG1, Sino Biological, Peking, China).

    Techniques: Expressing, Mouse Assay, Enzyme-linked Immunosorbent Assay

    Soluble checkpoint co-expression modulates HA-specific antibody responses. ( A ) Six-week old BALB/c mice were electroporated intramuscularly with expression plasmids encoding for HA and NP together either with an empty vector (mock) or plasmids encoding for sPD-1 or sPD-L1. Four weeks after priming, a booster immunization was administered Blood was drawn at weeks 3, 6 and 18 and antibody responses were analyzed by ELISA. NP-specific IgG ( B ), IgG1 ( C ) and IgG2a ( D ) antibody responses and HA-specific IgG ( E ), IgG1 ( F ) and IgG2a ( G ) antibody responses in the sera of BALB/c mice after i.m. electroporation over a time-period of 18 weeks. Shown are mean values with SEM ( n = 9–18) and significant differences between immunized groups (two-way ANOVA analyses followed by Tukey’s multiple comparison test, ( F ) * p

    Journal: Vaccines

    Article Title: Genetic Co-Administration of Soluble PD-1 Ectodomains Modifies Immune Responses against Influenza A Virus Induced by DNA Vaccination

    doi: 10.3390/vaccines8040570

    Figure Lengend Snippet: Soluble checkpoint co-expression modulates HA-specific antibody responses. ( A ) Six-week old BALB/c mice were electroporated intramuscularly with expression plasmids encoding for HA and NP together either with an empty vector (mock) or plasmids encoding for sPD-1 or sPD-L1. Four weeks after priming, a booster immunization was administered Blood was drawn at weeks 3, 6 and 18 and antibody responses were analyzed by ELISA. NP-specific IgG ( B ), IgG1 ( C ) and IgG2a ( D ) antibody responses and HA-specific IgG ( E ), IgG1 ( F ) and IgG2a ( G ) antibody responses in the sera of BALB/c mice after i.m. electroporation over a time-period of 18 weeks. Shown are mean values with SEM ( n = 9–18) and significant differences between immunized groups (two-way ANOVA analyses followed by Tukey’s multiple comparison test, ( F ) * p

    Article Snippet: Quantitative analysis of the HA-specific IgG1 amounts was performed using a monoclonal anti-influenza Hemagglutinin antibody (2F1A7, IgG1, Sino Biological, Peking, China).

    Techniques: Expressing, Mouse Assay, Plasmid Preparation, Enzyme-linked Immunosorbent Assay, Electroporation