h7n9  (Sino Biological)


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    Sino Biological h7n9
    Antibody response induced by NDV-vectored <t>H7N9</t> vaccine in chickens. (A) HI titers against NDV vector. (B) HI titers against H7N9 virus. The dotted lines in (A,B) indicate the cutoff value for positive reading in HI assay (4 log 2 ). (C) VN antibody titers against H7N9 virus. (D) IgG titers determined by ELISA. Serum samples from individual chicken were pooled for measurement of VN and IgG titers. The dotted lines in (C,D) stand for the lower detection limit for VN test and ELISA.
    H7n9, supplied by Sino Biological, used in various techniques. Bioz Stars score: 88/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/h7n9/product/Sino Biological
    Average 88 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    h7n9 - by Bioz Stars, 2022-11
    88/100 stars

    Images

    1) Product Images from "Hemagglutinin-Specific Non-neutralizing Antibody Is Essential for Protection Provided by Inactivated and Viral-Vectored H7N9 Avian Influenza Vaccines in Chickens"

    Article Title: Hemagglutinin-Specific Non-neutralizing Antibody Is Essential for Protection Provided by Inactivated and Viral-Vectored H7N9 Avian Influenza Vaccines in Chickens

    Journal: Frontiers in Veterinary Science

    doi: 10.3389/fvets.2019.00482

    Antibody response induced by NDV-vectored H7N9 vaccine in chickens. (A) HI titers against NDV vector. (B) HI titers against H7N9 virus. The dotted lines in (A,B) indicate the cutoff value for positive reading in HI assay (4 log 2 ). (C) VN antibody titers against H7N9 virus. (D) IgG titers determined by ELISA. Serum samples from individual chicken were pooled for measurement of VN and IgG titers. The dotted lines in (C,D) stand for the lower detection limit for VN test and ELISA.
    Figure Legend Snippet: Antibody response induced by NDV-vectored H7N9 vaccine in chickens. (A) HI titers against NDV vector. (B) HI titers against H7N9 virus. The dotted lines in (A,B) indicate the cutoff value for positive reading in HI assay (4 log 2 ). (C) VN antibody titers against H7N9 virus. (D) IgG titers determined by ELISA. Serum samples from individual chicken were pooled for measurement of VN and IgG titers. The dotted lines in (C,D) stand for the lower detection limit for VN test and ELISA.

    Techniques Used: Plasmid Preparation, HI Assay, Enzyme-linked Immunosorbent Assay

    Passive transfer challenge study of non-neutralizing sera. (A) Schematic illustration for the serum transfer experiment. (B) Clinical scoring and (C) survival of chickens after H7N9 virus infection. “ns” in (C) indicates non-significant difference.
    Figure Legend Snippet: Passive transfer challenge study of non-neutralizing sera. (A) Schematic illustration for the serum transfer experiment. (B) Clinical scoring and (C) survival of chickens after H7N9 virus infection. “ns” in (C) indicates non-significant difference.

    Techniques Used: Infection

    Antibody response induced by inactivated H7N9 vaccine in chickens. (A) HI, (B) VN, and (C) IgG titers induced by the vaccine. (D) Correlation analysis between VN and HI antibody titers. (E) Correlation analysis between IgG and HI antibody titers. (F) Correlation analysis between IgG and VN antibody titers. The dotted line in (A) indicates the cutoff value for positive reading in HI assay (4 log 2 ) and the lines in (B,C) stand for the lower detection limit for serological assays. GMT in (D–F) stands for geometry mean titer.
    Figure Legend Snippet: Antibody response induced by inactivated H7N9 vaccine in chickens. (A) HI, (B) VN, and (C) IgG titers induced by the vaccine. (D) Correlation analysis between VN and HI antibody titers. (E) Correlation analysis between IgG and HI antibody titers. (F) Correlation analysis between IgG and VN antibody titers. The dotted line in (A) indicates the cutoff value for positive reading in HI assay (4 log 2 ) and the lines in (B,C) stand for the lower detection limit for serological assays. GMT in (D–F) stands for geometry mean titer.

    Techniques Used: HI Assay

    Clinical scoring and survival of animals after H7N9 challenge. (A) Clinical scoring and (B) survival of chickens immunized with the rGD15 vaccine. (C) Clinical scoring and (D) survival of chickens immunized with the NDV-H7N9 vaccine.
    Figure Legend Snippet: Clinical scoring and survival of animals after H7N9 challenge. (A) Clinical scoring and (B) survival of chickens immunized with the rGD15 vaccine. (C) Clinical scoring and (D) survival of chickens immunized with the NDV-H7N9 vaccine.

    Techniques Used:

    2) Product Images from "Simultaneous and automated detection of influenza A virus hemagglutinin H7 and H9 based on magnetism and size mediated microfluidic chip"

    Article Title: Simultaneous and automated detection of influenza A virus hemagglutinin H7 and H9 based on magnetism and size mediated microfluidic chip

    Journal: Sensors and Actuators. B, Chemical

    doi: 10.1016/j.snb.2020.127675

    (A–F) Fluorescence microscopic images of different concentrations of samples (0, 10.0, 20, 50.0, 100.0, and 500.0 ng/mL, respectively). (G) Fluorescence intensity for H7N9 HA in 5−500 ng/mL. (H) Linear response for H7N9 HA with the concentration range of 5.0–100.0 ng/mL. (I) Fluorescence intensity for H9N2 HA in 5−500 ng/mL. (H) Linear response for H9N2 HA with the concentration range of 5.0–100.0 ng/mL. Error bars indicate the standard deviation of three experiments. The scale bar is 10 μm.
    Figure Legend Snippet: (A–F) Fluorescence microscopic images of different concentrations of samples (0, 10.0, 20, 50.0, 100.0, and 500.0 ng/mL, respectively). (G) Fluorescence intensity for H7N9 HA in 5−500 ng/mL. (H) Linear response for H7N9 HA with the concentration range of 5.0–100.0 ng/mL. (I) Fluorescence intensity for H9N2 HA in 5−500 ng/mL. (H) Linear response for H9N2 HA with the concentration range of 5.0–100.0 ng/mL. Error bars indicate the standard deviation of three experiments. The scale bar is 10 μm.

    Techniques Used: Fluorescence, Concentration Assay, Standard Deviation

    Microscopic images of IMBs (bright field, fluorescence field, and merge, respectively). (A–C) Microscopic images of H7N9 antibody modified magnetic beads. (D–F) Microscopic images of H7N9 antibody unmodified magnetic beads. The scale bar is 50 μm.
    Figure Legend Snippet: Microscopic images of IMBs (bright field, fluorescence field, and merge, respectively). (A–C) Microscopic images of H7N9 antibody modified magnetic beads. (D–F) Microscopic images of H7N9 antibody unmodified magnetic beads. The scale bar is 50 μm.

    Techniques Used: Fluorescence, Modification, Magnetic Beads

    (A). Histograms of the specificity of H7N9 HA. (B) Histograms of the specificity of H9N2 HA. (C) Histogram of H7N9 fluorescence intensity in different samples. (D) Histogram of H9N2 fluorescence intensity in different samples. Error bars indicate the standard deviation of three experiments.
    Figure Legend Snippet: (A). Histograms of the specificity of H7N9 HA. (B) Histograms of the specificity of H9N2 HA. (C) Histogram of H7N9 fluorescence intensity in different samples. (D) Histogram of H9N2 fluorescence intensity in different samples. Error bars indicate the standard deviation of three experiments.

    Techniques Used: Fluorescence, Standard Deviation

    3) Product Images from "A potent germline-like human monoclonal antibody targets a pH-sensitive epitope on H7N9 influenza hemagglutinin"

    Article Title: A potent germline-like human monoclonal antibody targets a pH-sensitive epitope on H7N9 influenza hemagglutinin

    Journal: Cell host & microbe

    doi: 10.1016/j.chom.2017.08.011

    The schematic biopanning process and the characterization of H7 HA-specific mAb from the antibody library. (A) The biopanning strategy of H7 HA1-specific mAbs from the naïve antibody phage display library. (B) Polyclonal phage ELISA showing the binding of the first to fifth rounds (Rd 1 to Rd 5) of phages to HA and HA1. Bound phages were detected with anti-M13-HRP conjugate. (C) Binding of Fab m826 to 4 different subtypes of influenza virus HA. (D) Immunogenetic analysis of the heavy and light chain variable regions of m826 using the IMGT tool. (E) Germline-rooted circular phylogenetic tree of m826-like antibody sequences found in IgM libraries derived from healthy human adults, neonates and H7N9-infected patients. The sequences of m826 and the clone identical to m826 were shown in red. Sequence ID started with CB represents sequences derived from the neonates, started with HH represents sequences derived from the healthy adults, and started with H7N9 represents that from the H7N9-infected patients. The phylogenetic tree was constructed by the Neighbor-Joining method.
    Figure Legend Snippet: The schematic biopanning process and the characterization of H7 HA-specific mAb from the antibody library. (A) The biopanning strategy of H7 HA1-specific mAbs from the naïve antibody phage display library. (B) Polyclonal phage ELISA showing the binding of the first to fifth rounds (Rd 1 to Rd 5) of phages to HA and HA1. Bound phages were detected with anti-M13-HRP conjugate. (C) Binding of Fab m826 to 4 different subtypes of influenza virus HA. (D) Immunogenetic analysis of the heavy and light chain variable regions of m826 using the IMGT tool. (E) Germline-rooted circular phylogenetic tree of m826-like antibody sequences found in IgM libraries derived from healthy human adults, neonates and H7N9-infected patients. The sequences of m826 and the clone identical to m826 were shown in red. Sequence ID started with CB represents sequences derived from the neonates, started with HH represents sequences derived from the healthy adults, and started with H7N9 represents that from the H7N9-infected patients. The phylogenetic tree was constructed by the Neighbor-Joining method.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Binding Assay, Derivative Assay, Infection, Sequencing, Construct

    m826 mAb recognizes a unique epitope on H7 HA. (A ) Docking of the m826-HA1 complex onto the crystal structure of monomeric H7 HA. The epitope of m826 is distinct from the RBS. (B) Superposition of the antibody epitope which was partially buried in the trimeric HA structure. (C) Sequence alignment of HA1 from the H7N9, H7N7, and H7N4 and highlighting of structurally defined influenza antibody epitopes. The conventional antigenic sites (Sa, Sb, Ca1, Ca2, and Cb) are shaded in blue, the epitope of m826 is shaded in red, and RBS is shown in the black box.
    Figure Legend Snippet: m826 mAb recognizes a unique epitope on H7 HA. (A ) Docking of the m826-HA1 complex onto the crystal structure of monomeric H7 HA. The epitope of m826 is distinct from the RBS. (B) Superposition of the antibody epitope which was partially buried in the trimeric HA structure. (C) Sequence alignment of HA1 from the H7N9, H7N7, and H7N4 and highlighting of structurally defined influenza antibody epitopes. The conventional antigenic sites (Sa, Sb, Ca1, Ca2, and Cb) are shaded in blue, the epitope of m826 is shaded in red, and RBS is shown in the black box.

    Techniques Used: Sequencing

    m826 mAb does not neutralize H7 virus but mediates potent ADCC. (A) The immunostaining-based neutralization assay for m826 mAb against H7N4 virus. Immunostaining was conducted using influenza NP-specific mAbs to detect virus-infected cells. H7N4-specfic Ab was used as positive control. (B) Confocal images of pCMV3-H7N9-HA-GFP transfected 293T cells stained with 100 nM m826 IgG or an unrelated anti-HBV human IgG G12 as the control. Green signal: GFP. Red signal: detecting with Alexa Fluor 647 conjugated goat anti-human IgG. Scale bar = 25 μm. (C) ADCC-related signaling in Jurkat T cells engineered to express human FcγRIIIa triggered by m826 and CR9114 IgG in the presence of H7N9 HA expressing-293 T cells. An unrelated anti-MERS-CoV IgG m336 was used as negative control. (D) ADCC activity of m826 and CR9114 IgG against H7N9 HA expressing-293 T cells mediated by freshly prepared human PBMCs. The percentage (%) of specific lysis was calculated as described in the Materials and Methods. All error bars reflect standard deviation (s.d.).
    Figure Legend Snippet: m826 mAb does not neutralize H7 virus but mediates potent ADCC. (A) The immunostaining-based neutralization assay for m826 mAb against H7N4 virus. Immunostaining was conducted using influenza NP-specific mAbs to detect virus-infected cells. H7N4-specfic Ab was used as positive control. (B) Confocal images of pCMV3-H7N9-HA-GFP transfected 293T cells stained with 100 nM m826 IgG or an unrelated anti-HBV human IgG G12 as the control. Green signal: GFP. Red signal: detecting with Alexa Fluor 647 conjugated goat anti-human IgG. Scale bar = 25 μm. (C) ADCC-related signaling in Jurkat T cells engineered to express human FcγRIIIa triggered by m826 and CR9114 IgG in the presence of H7N9 HA expressing-293 T cells. An unrelated anti-MERS-CoV IgG m336 was used as negative control. (D) ADCC activity of m826 and CR9114 IgG against H7N9 HA expressing-293 T cells mediated by freshly prepared human PBMCs. The percentage (%) of specific lysis was calculated as described in the Materials and Methods. All error bars reflect standard deviation (s.d.).

    Techniques Used: Immunostaining, Neutralization, Infection, Positive Control, Transfection, Staining, Expressing, Negative Control, Activity Assay, Lysis, Standard Deviation

    Binding profiles of m826 mAb to HA and HA1 measured by BLI in OctetRED96. The m826 mAb was immobilized on activated AR2G biosensors. The analytes consisted of serial dilution (between 100 nM and 1.2 nM) of trimeric H7N9 HA at pH 5.0 (A) or 7.4 (B) , H7N9 HA1 at pH 7.4 (C) , or 100 nM H1N1 (red curve) and H3N2 HA (blue curve) at pH 7.4 (D) . Binding kinetics was evaluated using a 1:1 Langmuir binding model by Fortebio Data Analysis 7.0 software.
    Figure Legend Snippet: Binding profiles of m826 mAb to HA and HA1 measured by BLI in OctetRED96. The m826 mAb was immobilized on activated AR2G biosensors. The analytes consisted of serial dilution (between 100 nM and 1.2 nM) of trimeric H7N9 HA at pH 5.0 (A) or 7.4 (B) , H7N9 HA1 at pH 7.4 (C) , or 100 nM H1N1 (red curve) and H3N2 HA (blue curve) at pH 7.4 (D) . Binding kinetics was evaluated using a 1:1 Langmuir binding model by Fortebio Data Analysis 7.0 software.

    Techniques Used: Binding Assay, Serial Dilution, Software

    Prophylactic and therapeutic efficacy of mAb m826 in protecting mice against lethal dose H7N9 challenge. For prophylactic efficacy study, mice were treated ( i.p. ) with m826 antibody 12 h before viral challenge ( i.n. ) with 10×LD 50 of H7N9 virus and were monitored daily for 14 days for the accumulated mortality (A) and weight loss (B) , expressed as percent (%) weight loss and survival, respectively (n = 5 per group). PBS was used for the control group. For therapeutic efficacy study, mice were treated ( i.p. ) with m826 antibody 12 h after viral challenge ( i.n. ) with 10×LD 50 of H7N9 virus and were monitored daily for 14 days for the accumulated mortality (C) and weight loss (D) . The weight loss of panels B and D represents mean change in body weight per group and standard deviation was also shown. (E) Evaluation of histopathological changes in the pulmonary tissues of uninfected mice and mice from therapeutic, prophylactic and control group. The black, yellow, blue arrows represented the H7N9 infection-induced inflammation of blood vessel, alveoli or capillary, respectively. ( F ) Evaluation of histopathological changes in the bronchial tissues. The black, yellow, blue and green arrows represented bronchial epithelial cell, bronchial alveoli, capillary and interstitial tissue, respectively.
    Figure Legend Snippet: Prophylactic and therapeutic efficacy of mAb m826 in protecting mice against lethal dose H7N9 challenge. For prophylactic efficacy study, mice were treated ( i.p. ) with m826 antibody 12 h before viral challenge ( i.n. ) with 10×LD 50 of H7N9 virus and were monitored daily for 14 days for the accumulated mortality (A) and weight loss (B) , expressed as percent (%) weight loss and survival, respectively (n = 5 per group). PBS was used for the control group. For therapeutic efficacy study, mice were treated ( i.p. ) with m826 antibody 12 h after viral challenge ( i.n. ) with 10×LD 50 of H7N9 virus and were monitored daily for 14 days for the accumulated mortality (C) and weight loss (D) . The weight loss of panels B and D represents mean change in body weight per group and standard deviation was also shown. (E) Evaluation of histopathological changes in the pulmonary tissues of uninfected mice and mice from therapeutic, prophylactic and control group. The black, yellow, blue arrows represented the H7N9 infection-induced inflammation of blood vessel, alveoli or capillary, respectively. ( F ) Evaluation of histopathological changes in the bronchial tissues. The black, yellow, blue and green arrows represented bronchial epithelial cell, bronchial alveoli, capillary and interstitial tissue, respectively.

    Techniques Used: Mouse Assay, Standard Deviation, Infection

    4) Product Images from "Improvement of a rapid diagnostic application of monoclonal antibodies against avian influenza H7 subtype virus using Europium nanoparticles"

    Article Title: Improvement of a rapid diagnostic application of monoclonal antibodies against avian influenza H7 subtype virus using Europium nanoparticles

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-08328-9

    Detection limit of FICT assay for target antigen. FICT employing Europium-conjugated antibodies were tested for the limit of detection (LOD) against H7N9 rHA1 ( A ). The data ( n = 3) are shown as mean ± SD. Linear regression is shown with the dotted line. The arrow indicates the antigen concentration of LOD. Raw fluorescence peaks from the test line (TL) and control line (CL) in FICT are shown in the bottom panel.
    Figure Legend Snippet: Detection limit of FICT assay for target antigen. FICT employing Europium-conjugated antibodies were tested for the limit of detection (LOD) against H7N9 rHA1 ( A ). The data ( n = 3) are shown as mean ± SD. Linear regression is shown with the dotted line. The arrow indicates the antigen concentration of LOD. Raw fluorescence peaks from the test line (TL) and control line (CL) in FICT are shown in the bottom panel.

    Techniques Used: Concentration Assay, Fluorescence

    Development of H7 subtype-specific antibodies. The fusions were performed using mouse spleen cells inoculated with H7N9 virus rHA1. Ten hybridomas were produced. The secreted antibodies from each hybridoma were tested for recombinant antigen (H7N9 HA1 ( A ) and different influenza subtype virus ( B ) by indirect ELISA. Pre-immune, serum from a healthy mouse; P.C., positive control antibody (anti-influenza A nucleoprotein antibody).
    Figure Legend Snippet: Development of H7 subtype-specific antibodies. The fusions were performed using mouse spleen cells inoculated with H7N9 virus rHA1. Ten hybridomas were produced. The secreted antibodies from each hybridoma were tested for recombinant antigen (H7N9 HA1 ( A ) and different influenza subtype virus ( B ) by indirect ELISA. Pre-immune, serum from a healthy mouse; P.C., positive control antibody (anti-influenza A nucleoprotein antibody).

    Techniques Used: Produced, Recombinant, Indirect ELISA, Positive Control

    5) Product Images from "Development of an Influenza A Master Virus for Generating High-Growth Reassortants for A/Anhui/1/2013(H7N9) Vaccine Production in Qualified MDCK Cells"

    Article Title: Development of an Influenza A Master Virus for Generating High-Growth Reassortants for A/Anhui/1/2013(H7N9) Vaccine Production in Qualified MDCK Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0160040

    Western blotting analysis of the purified viral proteins. Purified viral concentrates of NIIDRG-10C, -10.1C, -10 and -10.1 were analyzed by SDS-PAGE. HA proteins were detected using a rabbit polyclonal antibody against recombinant HA protein of H7N9 (A/Shanghai/1/2013) (Sino Biological Inc. Beijing, China) and a donkey anti-rabbit IgG horseradish peroxidase-conjugated secondary antibody by western blotting analysis. Purified viral proteins were treated (A) or untreated (B) with N-glycosidase F.
    Figure Legend Snippet: Western blotting analysis of the purified viral proteins. Purified viral concentrates of NIIDRG-10C, -10.1C, -10 and -10.1 were analyzed by SDS-PAGE. HA proteins were detected using a rabbit polyclonal antibody against recombinant HA protein of H7N9 (A/Shanghai/1/2013) (Sino Biological Inc. Beijing, China) and a donkey anti-rabbit IgG horseradish peroxidase-conjugated secondary antibody by western blotting analysis. Purified viral proteins were treated (A) or untreated (B) with N-glycosidase F.

    Techniques Used: Western Blot, Purification, SDS Page, Recombinant

    6) Product Images from "Cross-reactivity between avian influenza A (H7N9) virus and divergent H7 subtypic- and heterosubtypic influenza A viruses"

    Article Title: Cross-reactivity between avian influenza A (H7N9) virus and divergent H7 subtypic- and heterosubtypic influenza A viruses

    Journal: Scientific Reports

    doi: 10.1038/srep22045

    Cross-reactivity between H7N9 HA and antibodies against heterosubtypes of influenza A viruses. ( A,B ) Cross-reactivities in ELISA. ELISA tests were performed with H7N9 HA expressed in insect cells as coating antigen. Antisera against H1, H2, H3, H4, H5, and H8 ( A ), and H9, H10, H11, H12, H13, and H16 ( B ) were serially diluted starting at a dilution of 256 ng/ml to react with the coating antigens. Antisera against H7N9 HA were used as positive control. ( C ) Cross-reactivities in indirect immunofluorescence assays. MDCK cells infected with Anhui/1 at an MOI of 0.1 were fixed with 4% formaldehyde and probed with antisera against HA proteins of H1, H2, H3, H4, H5, H8, H9, H10, H11, H12, H13, and H16 with a concentration of 0.5 μg/ml. Antisera against H7N9 HA were used as positive control. ( D ) Cross-reactivities in Hemagglutination inhibition (HI) assays. The assays were carried out using the A/Anhui/1/2013 (H7N9) strain and antisera against whole virus of H1N1, H3N2, and H5N1 with antisera against H7N9-, H7N2-, H7N3-, and H7N7-HA as positive controls. Serum with titers > 40 were considered HI-positive for H7N9 virus.
    Figure Legend Snippet: Cross-reactivity between H7N9 HA and antibodies against heterosubtypes of influenza A viruses. ( A,B ) Cross-reactivities in ELISA. ELISA tests were performed with H7N9 HA expressed in insect cells as coating antigen. Antisera against H1, H2, H3, H4, H5, and H8 ( A ), and H9, H10, H11, H12, H13, and H16 ( B ) were serially diluted starting at a dilution of 256 ng/ml to react with the coating antigens. Antisera against H7N9 HA were used as positive control. ( C ) Cross-reactivities in indirect immunofluorescence assays. MDCK cells infected with Anhui/1 at an MOI of 0.1 were fixed with 4% formaldehyde and probed with antisera against HA proteins of H1, H2, H3, H4, H5, H8, H9, H10, H11, H12, H13, and H16 with a concentration of 0.5 μg/ml. Antisera against H7N9 HA were used as positive control. ( D ) Cross-reactivities in Hemagglutination inhibition (HI) assays. The assays were carried out using the A/Anhui/1/2013 (H7N9) strain and antisera against whole virus of H1N1, H3N2, and H5N1 with antisera against H7N9-, H7N2-, H7N3-, and H7N7-HA as positive controls. Serum with titers > 40 were considered HI-positive for H7N9 virus.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Positive Control, Immunofluorescence, Infection, Concentration Assay, HI Assay

    Cross-reactivities among H7 subtypes known to infect humans. ( A ) Phylogeny of H7 subtypes. Phylogenetic tree based on HA amino acid sequences of H7 subtypes generated using the Clustal W and MegAlign programs in the MEGA4.0 software package, including H7N9, H7N2, H7N3, H7N7, and H3N2. ( B ) Western blot analysis of lysates of three different preparations of MDCK cells infected with Anhui/1, Shanghai/1, and Shanghai/2 isolates. Isolates were harvested 48 h post infection at an MOI of 0.1. Blots were probed with the antisera against HA proteins of H7N9, H7N2, H7N3, and H7N7. ( C ) Cross-reactivities in ELISA. H7N9 HA expressed in insect cells was used as the antigen. Mouse antisera against H7N2, H7N3, and H7N7 were two-fold diluted from 1:2,000 to a final dilution of 1:128,000. Antisera against H7N9 HA were used as positive control. ( D ) Cross-reactivities in indirect immunofluorescence assays. Three different preparations of MDCK cells infected with Anhui/1, Shanghai/1, and Shanghai/2 at an MOI of 0.1 were fixed with 4% formaldehyde and probed with antisera against HA proteins of H7N2, H7N3, and H7N7 with a concentration of 0.5 μg/ml. Antisera against H7N9 HA were used as positive control. H7N9 index calculated by IFA data.
    Figure Legend Snippet: Cross-reactivities among H7 subtypes known to infect humans. ( A ) Phylogeny of H7 subtypes. Phylogenetic tree based on HA amino acid sequences of H7 subtypes generated using the Clustal W and MegAlign programs in the MEGA4.0 software package, including H7N9, H7N2, H7N3, H7N7, and H3N2. ( B ) Western blot analysis of lysates of three different preparations of MDCK cells infected with Anhui/1, Shanghai/1, and Shanghai/2 isolates. Isolates were harvested 48 h post infection at an MOI of 0.1. Blots were probed with the antisera against HA proteins of H7N9, H7N2, H7N3, and H7N7. ( C ) Cross-reactivities in ELISA. H7N9 HA expressed in insect cells was used as the antigen. Mouse antisera against H7N2, H7N3, and H7N7 were two-fold diluted from 1:2,000 to a final dilution of 1:128,000. Antisera against H7N9 HA were used as positive control. ( D ) Cross-reactivities in indirect immunofluorescence assays. Three different preparations of MDCK cells infected with Anhui/1, Shanghai/1, and Shanghai/2 at an MOI of 0.1 were fixed with 4% formaldehyde and probed with antisera against HA proteins of H7N2, H7N3, and H7N7 with a concentration of 0.5 μg/ml. Antisera against H7N9 HA were used as positive control. H7N9 index calculated by IFA data.

    Techniques Used: Generated, Software, Western Blot, Infection, Enzyme-linked Immunosorbent Assay, Positive Control, Immunofluorescence, Concentration Assay

    Cross-reactivities between the HA proteins of heterosubtypes of influenza A viruses and antibodies against H7N9. The cross-reactivities were analyzed using ELISA ( A,B ) and Western blot ( C ) with recombinant HA proteins of H1, H2, H3, H4, H5, H6, H8, H9, H10, H11, H12, H13, and H16 as antigens. HA proteins were two-fold diluted with a starting dilution of 2,560 ng/ml.
    Figure Legend Snippet: Cross-reactivities between the HA proteins of heterosubtypes of influenza A viruses and antibodies against H7N9. The cross-reactivities were analyzed using ELISA ( A,B ) and Western blot ( C ) with recombinant HA proteins of H1, H2, H3, H4, H5, H6, H8, H9, H10, H11, H12, H13, and H16 as antigens. HA proteins were two-fold diluted with a starting dilution of 2,560 ng/ml.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot, Recombinant

    Cross-neutralization of the divergent H7 subtype and heterosubtypes of influenza A viruses to H7N9 virus. The microneutralization (MN) assay was performed using the H7N9 virus strains of Anhui/1 ( A ), Shanghai/1 ( B ), and Shanghai/2 ( C ) and serial dilutions of mouse and rabbit HA antisera. The concentrations of antisera were determined as a series of two-fold dilutions starting with 1:10. Sera with titers ≥20 were considered neutralizing antibodies (NAbs)-positive for H7N9.
    Figure Legend Snippet: Cross-neutralization of the divergent H7 subtype and heterosubtypes of influenza A viruses to H7N9 virus. The microneutralization (MN) assay was performed using the H7N9 virus strains of Anhui/1 ( A ), Shanghai/1 ( B ), and Shanghai/2 ( C ) and serial dilutions of mouse and rabbit HA antisera. The concentrations of antisera were determined as a series of two-fold dilutions starting with 1:10. Sera with titers ≥20 were considered neutralizing antibodies (NAbs)-positive for H7N9.

    Techniques Used: Neutralization

    Identification of the cross-reactive regions by Western blot. The lysates of MDCK cells infected with Anhui/1 ( A ), Shanghai/1 ( B ), and Shanghai/2 ( C ) isolates at an MOI of 0.1 were harvested 48 h post infection and probed with antisera to HA proteins of H1, H2, H3, H4, H5, H8, H9, H10, H11, H12, H13, and H16. Antisera against H7N9 HA were used as positive control.
    Figure Legend Snippet: Identification of the cross-reactive regions by Western blot. The lysates of MDCK cells infected with Anhui/1 ( A ), Shanghai/1 ( B ), and Shanghai/2 ( C ) isolates at an MOI of 0.1 were harvested 48 h post infection and probed with antisera to HA proteins of H1, H2, H3, H4, H5, H8, H9, H10, H11, H12, H13, and H16. Antisera against H7N9 HA were used as positive control.

    Techniques Used: Western Blot, Infection, Positive Control

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    Sino Biological anti s1 polyclonal rabbit antibody
    Effects of Ala cavity mutations on fusion function. A , Reducing SDS-PAGE and western blotting of SARS CoV-2 S glycoproteins expressed in 293T cells with <t>rabbit</t> <t>anti-S1</t> <t>polyclonal</t> antibody. B , Cell-cell fusion activity of S glycoproteins determined in a luciferase reporter assay. Relative fusion activity: relative light units obtained with mutant and control vectors / relative light units obtained with WT S x 100. Mean ± SEM from 3 independent experiments shown. C , Representative microscopy fields at 10x magnification. Control vectors: S2P-1273 contains proline at positions 986 and 987 and lacks a furin cleavage site; HIV-1 Env: a HIV-1 glycoprotein expression vector, pcDNA3.1 AD8 -WT.
    Anti S1 Polyclonal Rabbit Antibody, 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
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    Sino Biological rabbit anti sars 2 s
    Effects of Ala cavity mutations on fusion function. A , Reducing SDS-PAGE and western blotting of SARS CoV-2 S glycoproteins expressed in 293T cells with <t>rabbit</t> <t>anti-S1</t> <t>polyclonal</t> antibody. B , Cell-cell fusion activity of S glycoproteins determined in a luciferase reporter assay. Relative fusion activity: relative light units obtained with mutant and control vectors / relative light units obtained with WT S x 100. Mean ± SEM from 3 independent experiments shown. C , Representative microscopy fields at 10x magnification. Control vectors: S2P-1273 contains proline at positions 986 and 987 and lacks a furin cleavage site; HIV-1 Env: a HIV-1 glycoprotein expression vector, pcDNA3.1 AD8 -WT.
    Rabbit Anti Sars 2 S, 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
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    Sino Biological rabbit anti rbd wild type antibody
    Determination of protein stability by immunofluorescence microscopy and ELISA. (A) <t>pYD1-RBD/EBY200</t> before heat inactivation. (B) pYD1-RBD/EBY200 after heat inactivation. (C) Determination of protein stability of lyophilized yeast powder at 25°C for 1 month by ELISA. (D) Fresh lyophilized yeast powder at 4°C after 3 days. (E) Lyophilized yeast power at 4°C after 10 months. (F) Fresh lyophilized yeast powder with empty vector pYD1.
    Rabbit Anti Rbd Wild Type Antibody, 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/rabbit anti rbd wild type antibody/product/Sino Biological
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    Image Search Results


    Effects of Ala cavity mutations on fusion function. A , Reducing SDS-PAGE and western blotting of SARS CoV-2 S glycoproteins expressed in 293T cells with rabbit anti-S1 polyclonal antibody. B , Cell-cell fusion activity of S glycoproteins determined in a luciferase reporter assay. Relative fusion activity: relative light units obtained with mutant and control vectors / relative light units obtained with WT S x 100. Mean ± SEM from 3 independent experiments shown. C , Representative microscopy fields at 10x magnification. Control vectors: S2P-1273 contains proline at positions 986 and 987 and lacks a furin cleavage site; HIV-1 Env: a HIV-1 glycoprotein expression vector, pcDNA3.1 AD8 -WT.

    Journal: bioRxiv

    Article Title: Enhanced stability of the SARS CoV-2 spike glycoprotein trimer following modification of an alanine cavity in the protein core

    doi: 10.1101/2022.11.08.515567

    Figure Lengend Snippet: Effects of Ala cavity mutations on fusion function. A , Reducing SDS-PAGE and western blotting of SARS CoV-2 S glycoproteins expressed in 293T cells with rabbit anti-S1 polyclonal antibody. B , Cell-cell fusion activity of S glycoproteins determined in a luciferase reporter assay. Relative fusion activity: relative light units obtained with mutant and control vectors / relative light units obtained with WT S x 100. Mean ± SEM from 3 independent experiments shown. C , Representative microscopy fields at 10x magnification. Control vectors: S2P-1273 contains proline at positions 986 and 987 and lacks a furin cleavage site; HIV-1 Env: a HIV-1 glycoprotein expression vector, pcDNA3.1 AD8 -WT.

    Article Snippet: Proteins were transferred to nitrocellulose prior to Western blotting with anti-S1 polyclonal rabbit antibody (Sino biological) and Goat anti-rabbit IR-Dye800CW (Odyssey).

    Techniques: SDS Page, Western Blot, Activity Assay, Luciferase, Reporter Assay, Mutagenesis, Microscopy, Expressing, Plasmid Preparation

    Determination of protein stability by immunofluorescence microscopy and ELISA. (A) pYD1-RBD/EBY200 before heat inactivation. (B) pYD1-RBD/EBY200 after heat inactivation. (C) Determination of protein stability of lyophilized yeast powder at 25°C for 1 month by ELISA. (D) Fresh lyophilized yeast powder at 4°C after 3 days. (E) Lyophilized yeast power at 4°C after 10 months. (F) Fresh lyophilized yeast powder with empty vector pYD1.

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: Determination of protein stability by immunofluorescence microscopy and ELISA. (A) pYD1-RBD/EBY200 before heat inactivation. (B) pYD1-RBD/EBY200 after heat inactivation. (C) Determination of protein stability of lyophilized yeast powder at 25°C for 1 month by ELISA. (D) Fresh lyophilized yeast powder at 4°C after 3 days. (E) Lyophilized yeast power at 4°C after 10 months. (F) Fresh lyophilized yeast powder with empty vector pYD1.

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

    Techniques: Immunofluorescence, Microscopy, Enzyme-linked Immunosorbent Assay, Plasmid Preparation

    Immunofluorescence microscopy of recombinant yeast cells. (A) pYD1/EBY200. (B) pYD1-RBD (WT)/EBY200. (C) pYD1-mRBD (B.1.17)/EBY200. (D) pYD1-mRBD (B.1.617.1)/EBY200. (E) pYD1-mRBD (B.1.351)/EBY200 (left: light; right: matching fluorescence, Scale bar: 10 µm).

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: Immunofluorescence microscopy of recombinant yeast cells. (A) pYD1/EBY200. (B) pYD1-RBD (WT)/EBY200. (C) pYD1-mRBD (B.1.17)/EBY200. (D) pYD1-mRBD (B.1.617.1)/EBY200. (E) pYD1-mRBD (B.1.351)/EBY200 (left: light; right: matching fluorescence, Scale bar: 10 µm).

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

    Techniques: Immunofluorescence, Microscopy, Recombinant, Fluorescence

    Cellular immune responses in splenocytes from mice vaccinated with yeast surface-displayed B.1.617.1 mRBD. (A) The appearance of IFN-γ-expressing spots in an ELISpot assay plate. Each dot represents a single cell secreting IFN-γ. (B) Level of IFN-γ expression per 2 × 10 5 splenocytes. (C) The total cytokine response on flow cytometry with intracellular cytokine staining 5 weeks after the fourth immunization or 120 days after priming. The levels of IFN-γ, IL-2, and TNF-α secretion by CD4 + and CD8 + T cells were quantified for each group and expressed as the frequency of cells expressing any one of the three cytokines. (D) Frequency of CD4 + T cells positive for each cytokine (IFN-γ, IL-2, and TNF-α) after stimulation with wild-type RBD antigen. (E) The proportions of CD4 + T cells secreting any combination of IFN-γ, IL-2, and TNF-α after stimulation with wild-type RBD antigen. A t -test was performed to compare the mRBD of the B.1.617.1 group and the PYD1/EBY200 (Empty vector) group. Asterisks represent significance: ** p

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: Cellular immune responses in splenocytes from mice vaccinated with yeast surface-displayed B.1.617.1 mRBD. (A) The appearance of IFN-γ-expressing spots in an ELISpot assay plate. Each dot represents a single cell secreting IFN-γ. (B) Level of IFN-γ expression per 2 × 10 5 splenocytes. (C) The total cytokine response on flow cytometry with intracellular cytokine staining 5 weeks after the fourth immunization or 120 days after priming. The levels of IFN-γ, IL-2, and TNF-α secretion by CD4 + and CD8 + T cells were quantified for each group and expressed as the frequency of cells expressing any one of the three cytokines. (D) Frequency of CD4 + T cells positive for each cytokine (IFN-γ, IL-2, and TNF-α) after stimulation with wild-type RBD antigen. (E) The proportions of CD4 + T cells secreting any combination of IFN-γ, IL-2, and TNF-α after stimulation with wild-type RBD antigen. A t -test was performed to compare the mRBD of the B.1.617.1 group and the PYD1/EBY200 (Empty vector) group. Asterisks represent significance: ** p

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

    Techniques: Mouse Assay, Expressing, Enzyme-linked Immunospot, Flow Cytometry, Staining, Plasmid Preparation

    Humoral immune responses elicited by wild-type SARS-CoV-2 Spike RBD and its mutant variants. (A) Wild-type RBD-specific IgG serum antibody after 2nd (day 28), 3rd (day 44), and 4th (day 64) immunizations. (B) B.1.1.7, B.1.671.1, and B.1.1351 mRBD-specific IgG serum antibody after 4th (day 64) immunization. (C) The neutralization titer of B.1.617.1 mRBD antiserum against wild-type RBD was determined by competitive ELISA. Serum samples were collected 2 weeks after the fourth immunization (Day 64), and detected after mixing the samples from the same group in equal volume. Data points represent individual animals. For statistical analysis, t -test was performed to compare to PYD1/EBY200 (Empty vector) and PBS groups. Asterisks represent significance: * p

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: Humoral immune responses elicited by wild-type SARS-CoV-2 Spike RBD and its mutant variants. (A) Wild-type RBD-specific IgG serum antibody after 2nd (day 28), 3rd (day 44), and 4th (day 64) immunizations. (B) B.1.1.7, B.1.671.1, and B.1.1351 mRBD-specific IgG serum antibody after 4th (day 64) immunization. (C) The neutralization titer of B.1.617.1 mRBD antiserum against wild-type RBD was determined by competitive ELISA. Serum samples were collected 2 weeks after the fourth immunization (Day 64), and detected after mixing the samples from the same group in equal volume. Data points represent individual animals. For statistical analysis, t -test was performed to compare to PYD1/EBY200 (Empty vector) and PBS groups. Asterisks represent significance: * p

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

    Techniques: Mutagenesis, Neutralization, Competitive ELISA, Plasmid Preparation

    Humoral and cellular immune responses of pYD1-RBD (wild-type)/EBY200 recombinant yeast cells inactivated with 25% ethanol at 40°C. Female BALB/c mice were subcutaneously immunized with recombinant yeast or PBS on days 1, 15, and 31. (A) Plasma samples collected on days 28 and 54 after initial immunization were used to determine the levels of RBD-specific IgG by ELISA. Data points represent individual animals. (B) Blood samples were collected on day 54 after initial immunization, and samples from the same group were pooled. Aliquots of 2 × 10 5 PBMCs isolated from each pooled blood sample were stimulated with SARS-CoV-2 S-RBD antigen, concanavalin A (Con A), or medium only. IFN-γ-expressing cells were counted. Each dot represents a single cell that secretes IFN-γ. (C) Quantification of the number of IFN-γ-expressing cells per 2 × 10 5 PBMCs. PBMC: peripheral blood mononuclear cell. For statistical analysis, t -test was performed to compare empty vector and PBS groups. Asterisks represent significance: ** p

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: Humoral and cellular immune responses of pYD1-RBD (wild-type)/EBY200 recombinant yeast cells inactivated with 25% ethanol at 40°C. Female BALB/c mice were subcutaneously immunized with recombinant yeast or PBS on days 1, 15, and 31. (A) Plasma samples collected on days 28 and 54 after initial immunization were used to determine the levels of RBD-specific IgG by ELISA. Data points represent individual animals. (B) Blood samples were collected on day 54 after initial immunization, and samples from the same group were pooled. Aliquots of 2 × 10 5 PBMCs isolated from each pooled blood sample were stimulated with SARS-CoV-2 S-RBD antigen, concanavalin A (Con A), or medium only. IFN-γ-expressing cells were counted. Each dot represents a single cell that secretes IFN-γ. (C) Quantification of the number of IFN-γ-expressing cells per 2 × 10 5 PBMCs. PBMC: peripheral blood mononuclear cell. For statistical analysis, t -test was performed to compare empty vector and PBS groups. Asterisks represent significance: ** p

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

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

    RBD displayed on the S . cerevisiae surface. (A) Schematic illustration of RBD displayed on the yeast surface. (B) Western blotting analysis of RBD and its mutant variants expressed on the surface of S . cerevisiae EBY200.

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: RBD displayed on the S . cerevisiae surface. (A) Schematic illustration of RBD displayed on the yeast surface. (B) Western blotting analysis of RBD and its mutant variants expressed on the surface of S . cerevisiae EBY200.

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

    Techniques: Western Blot, Mutagenesis

    Glycosylation analysis of N331 and N343 of RBD. (A) Western blotting analysis of RBD protein and its mutant variants expressed on the surface of S . cerevisiae EBY200; lane 1: Mark, lane 2: PYD1-RBD/EBY200, lane 3: PYD1-RBD (N331Q)/EBY200, lane 4: PYD1-RBD (N343Q)/EBY200, lane 5: PYD1-RBD (N331Q N343Q)/EBY200. (B) Binding of SARS-CoV-2 Spike protein RBD and its deglycosylation mutant variants to human ACE2. (C) Neutralizing activity of RBD and RBD (N331Q/N343Q) with SARS-CoV-2 IgG.

    Journal: Frontiers in Immunology

    Article Title: Display of receptor-binding domain of SARS-CoV-2 Spike protein variants on the Saccharomyces cerevisiae cell surface

    doi: 10.3389/fimmu.2022.935573

    Figure Lengend Snippet: Glycosylation analysis of N331 and N343 of RBD. (A) Western blotting analysis of RBD protein and its mutant variants expressed on the surface of S . cerevisiae EBY200; lane 1: Mark, lane 2: PYD1-RBD/EBY200, lane 3: PYD1-RBD (N331Q)/EBY200, lane 4: PYD1-RBD (N343Q)/EBY200, lane 5: PYD1-RBD (N331Q N343Q)/EBY200. (B) Binding of SARS-CoV-2 Spike protein RBD and its deglycosylation mutant variants to human ACE2. (C) Neutralizing activity of RBD and RBD (N331Q/N343Q) with SARS-CoV-2 IgG.

    Article Snippet: Remove the PBS and resuspend the cell pellets in 250 µl of PBS, 1 mg/ml BSA, and 1 µg of rabbit anti-RBD (wild-type) antibody (Sino Biological, Beijing, China) on ice for 30 min with occasional mixing.

    Techniques: Western Blot, Mutagenesis, Binding Assay, Activity Assay