anti s2  (Sino Biological)


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    Structured Review

    Sino Biological anti s2
    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. ( A ) Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] - and [N] - 293 T cells. All nine viruses were applied at equal titer to stable 293T/ACE2. ( B–C ) O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. ( D ) Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. ( E ) Western blot of Spike protein using <t>anti-S2</t> Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] - 293T products due to truncation of glycan biosynthesis. ( F ) Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] - 293Ts is almost fully proteolyzed during viral production (red arrowhead). *p
    Anti S2, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti s2 - by Bioz Stars, 2021-02
    94/100 stars

    Images

    1) Product Images from "Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration"

    Article Title: Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration

    Journal: eLife

    doi: 10.7554/eLife.61552

    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. ( A ) Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] - and [N] - 293 T cells. All nine viruses were applied at equal titer to stable 293T/ACE2. ( B–C ) O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. ( D ) Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. ( E ) Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] - 293T products due to truncation of glycan biosynthesis. ( F ) Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] - 293Ts is almost fully proteolyzed during viral production (red arrowhead). *p
    Figure Legend Snippet: N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. ( A ) Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] - and [N] - 293 T cells. All nine viruses were applied at equal titer to stable 293T/ACE2. ( B–C ) O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. ( D ) Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. ( E ) Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] - 293T products due to truncation of glycan biosynthesis. ( F ) Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] - 293Ts is almost fully proteolyzed during viral production (red arrowhead). *p

    Techniques Used: Modification, Expressing, Mutagenesis, Produced, Generated, Titration, Infection, Western Blot

    2) Product Images from "Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration"

    Article Title: Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration

    Journal: bioRxiv

    doi: 10.1101/2020.10.15.339838

    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. A . Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] − and [N] − 293T cells. All 9 viruses were applied at equal titer to stable 293T/ACE2. B - C . O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. D . Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. E . Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] − 293T products due to truncation of glycan biosynthesis. F . Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] − 293Ts is almost fully proteolyzed during viral production (red arrowhead). * P
    Figure Legend Snippet: N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. A . Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] − and [N] − 293T cells. All 9 viruses were applied at equal titer to stable 293T/ACE2. B - C . O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. D . Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. E . Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] − 293T products due to truncation of glycan biosynthesis. F . Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] − 293Ts is almost fully proteolyzed during viral production (red arrowhead). * P

    Techniques Used: Modification, Expressing, Mutagenesis, Produced, Generated, Titration, Infection, Western Blot

    3) Product Images from "Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration"

    Article Title: Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration

    Journal: bioRxiv

    doi: 10.1101/2020.10.15.339838

    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. A . Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] − and [N] − 293T cells. All 9 viruses were applied at equal titer to stable 293T/ACE2. B - C . O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. D . Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. E . Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] − 293T products due to truncation of glycan biosynthesis. F . Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] − 293Ts is almost fully proteolyzed during viral production (red arrowhead). * P
    Figure Legend Snippet: N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. A . Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] − and [N] − 293T cells. All 9 viruses were applied at equal titer to stable 293T/ACE2. B - C . O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. D . Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. E . Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] − 293T products due to truncation of glycan biosynthesis. F . Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] − 293Ts is almost fully proteolyzed during viral production (red arrowhead). * P

    Techniques Used: Modification, Expressing, Mutagenesis, Produced, Generated, Titration, Infection, Western Blot

    4) Product Images from "SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development"

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development

    Journal: bioRxiv

    doi: 10.1101/2020.02.16.951723

    Structural conservation of SARS-CoV RBD. RBD is shown as colored surface. ACE2 is shown as gray cartoon. The three surface mutation sites (i.e. N354D, D364Y, and V367F) observed in SARS-CoV-2 RBD are labeled. Mutation F342L is buried and not shown here.
    Figure Legend Snippet: Structural conservation of SARS-CoV RBD. RBD is shown as colored surface. ACE2 is shown as gray cartoon. The three surface mutation sites (i.e. N354D, D364Y, and V367F) observed in SARS-CoV-2 RBD are labeled. Mutation F342L is buried and not shown here.

    Techniques Used: Mutagenesis, Labeling

    Structure similarity between SARS-CoV-2 RBD and SARS-CoV RBD. RBD is shown in a space-filled model with colored surface. ACE2 is shown as gray tube model. The three glycosylation sites in SARS-CoV are labeled. Note that N 357 ST in SARS-CoV is changed to N 370 SA in SARS-CoV-2, which is different from the NXS/T pattern required for glycosylation, and hence this site is more likely to be unglycosylated. The two possible cross-reactive regions are marked with yellow circles.
    Figure Legend Snippet: Structure similarity between SARS-CoV-2 RBD and SARS-CoV RBD. RBD is shown in a space-filled model with colored surface. ACE2 is shown as gray tube model. The three glycosylation sites in SARS-CoV are labeled. Note that N 357 ST in SARS-CoV is changed to N 370 SA in SARS-CoV-2, which is different from the NXS/T pattern required for glycosylation, and hence this site is more likely to be unglycosylated. The two possible cross-reactive regions are marked with yellow circles.

    Techniques Used: Labeling

    Cross-reactivity and neutralization efficiency of SARS nAbs against SARS-CoV-2. A. Binding of SARS nAbs to SARS-CoV S1 protein were tested by ELISA. Recombinant S1 protein of SARS-CoV were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. B. Binding of SARS nAbs to SARS-CoV-2 S1 protein were tested by ELSIA. Recombinant S1 protein of SARS-CoV-2 were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. C. Neutralization of SARS-CoV nAbs against SARS-CoV-2 PSV. D. Antibody competition with SARS-CoV RBD binding to ACE2. Recombinant SARS-CoV RBD protein was coated on plates, nAbs and recombinant ACE2 were then added for RBD binding competition measurements.
    Figure Legend Snippet: Cross-reactivity and neutralization efficiency of SARS nAbs against SARS-CoV-2. A. Binding of SARS nAbs to SARS-CoV S1 protein were tested by ELISA. Recombinant S1 protein of SARS-CoV were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. B. Binding of SARS nAbs to SARS-CoV-2 S1 protein were tested by ELSIA. Recombinant S1 protein of SARS-CoV-2 were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. C. Neutralization of SARS-CoV nAbs against SARS-CoV-2 PSV. D. Antibody competition with SARS-CoV RBD binding to ACE2. Recombinant SARS-CoV RBD protein was coated on plates, nAbs and recombinant ACE2 were then added for RBD binding competition measurements.

    Techniques Used: Neutralization, Binding Assay, Enzyme-linked Immunosorbent Assay, Recombinant

    Sequence analysis and structure modeling of SARS-CoV-2 RBD and SARS-CoV RBD and their interactions with ACE2. A. RBD sequence alignment of SARS-CoV and SARS-CoV-2, highlighting the predominant residues that contribute to the interactions with ACE2. The distinct interactions of RBD and ACE2 for the two viruses are indicated by the down-pointing orange triangles and up-pointing red triangles, respectively. RBM residues are underlined. The one-residue insertion is indicated by the red arrow. Asterisks indicate positions of fully conserved residues. Colons indicate positions of strictly conserved residues. Periods indicate positions of weakly conserved residues. B. Conformational comparison between the RBD-ACE2 complex structures for SARS-CoV-2 and SARS-CoV. The RBD and ACE2 structures in the SARS-CoV-2 RBD-ACE2 complex model are shown as orange and pink tubes, respectively. The RBD and ACE2 structures in the optimized SARS-CoV RBD-ACE2 complex structure are shown as blue and green tubes, respectively. The location of noticeable subtle conformational difference is indicated by an arrow. C. Distinct interaction patterns in the SARS-CoV-2 and SARS-CoV RBD-ACE2 interfaces. Structures of RBD and ACE2 are shown as cartoon in pink and green colors, respectively. The side chains of the residues in both protein components, representing their unique interactions, are shown as sticks. Polar interactions (salt-bridge and hydrogen bond) are shown as blue dash line. Non-polar interactions (π-stack, π-anion, and hydrophobic interactions) are shown as orange dash line.
    Figure Legend Snippet: Sequence analysis and structure modeling of SARS-CoV-2 RBD and SARS-CoV RBD and their interactions with ACE2. A. RBD sequence alignment of SARS-CoV and SARS-CoV-2, highlighting the predominant residues that contribute to the interactions with ACE2. The distinct interactions of RBD and ACE2 for the two viruses are indicated by the down-pointing orange triangles and up-pointing red triangles, respectively. RBM residues are underlined. The one-residue insertion is indicated by the red arrow. Asterisks indicate positions of fully conserved residues. Colons indicate positions of strictly conserved residues. Periods indicate positions of weakly conserved residues. B. Conformational comparison between the RBD-ACE2 complex structures for SARS-CoV-2 and SARS-CoV. The RBD and ACE2 structures in the SARS-CoV-2 RBD-ACE2 complex model are shown as orange and pink tubes, respectively. The RBD and ACE2 structures in the optimized SARS-CoV RBD-ACE2 complex structure are shown as blue and green tubes, respectively. The location of noticeable subtle conformational difference is indicated by an arrow. C. Distinct interaction patterns in the SARS-CoV-2 and SARS-CoV RBD-ACE2 interfaces. Structures of RBD and ACE2 are shown as cartoon in pink and green colors, respectively. The side chains of the residues in both protein components, representing their unique interactions, are shown as sticks. Polar interactions (salt-bridge and hydrogen bond) are shown as blue dash line. Non-polar interactions (π-stack, π-anion, and hydrophobic interactions) are shown as orange dash line.

    Techniques Used: Sequencing

    Measurements of SARS-CoV-2 and SARS-CoV S1 binding to ACE2. A. Serial diluted recombinant S1 proteins of SARS-CoV-2, SARS-CoV and MERS-CoV were coated on 96 well plates, incubated with the recombinant Fc-tagged ACE2 (ACE2-Fc) for binding evaluation. B. Recombinant S1 proteins of SARS-CoV-2 and SARS-CoV were incubated with 293T-ACE2 cells and subjected to FACS evaluation for binding.
    Figure Legend Snippet: Measurements of SARS-CoV-2 and SARS-CoV S1 binding to ACE2. A. Serial diluted recombinant S1 proteins of SARS-CoV-2, SARS-CoV and MERS-CoV were coated on 96 well plates, incubated with the recombinant Fc-tagged ACE2 (ACE2-Fc) for binding evaluation. B. Recombinant S1 proteins of SARS-CoV-2 and SARS-CoV were incubated with 293T-ACE2 cells and subjected to FACS evaluation for binding.

    Techniques Used: Binding Assay, Recombinant, Incubation, FACS

    5) Product Images from "A single dose of recombinant VSV-ΔG-spike vaccine provides protection against SARS-CoV-2 challenge"

    Article Title: A single dose of recombinant VSV-ΔG-spike vaccine provides protection against SARS-CoV-2 challenge

    Journal: bioRxiv

    doi: 10.1101/2020.06.18.160655

    Histopathology and viral load of rVSV-ΔG-spike vaccinated and infected lungs: General histology (H E) and SARS-CoV-2 Immunolabeling of hamster lungs with and without pre vaccination. Lungs were isolated and processed for paraffin embedding from Naïve (A, E, I), vaccinated + infected 10 6 5dpi (B, F, J; C, G, K), and SARS-CoV-2 5×10 6 5dpi (D, H, L) and groups. Sections (5μm) were taken for H E staining (A-H) and SARS-CoV-2 immunolabeling (I-L, DAPI-Blue, SARS-CoV-2-Green). Pictures A-D: magnification-x1, bar= 100μm; Pictures E-H: magnification-x10, bar= 100μm; Pictures I-L: magnification-x60, bar= 10μm. Black arrows indicate patches of focal inflammation, pleural invaginatio and alveolar collapse. “*”-indicates hemorrhagic areas. “#”-indicates edema and protein rich exudates. Black arrow heads indicate pulmonary mononuclear cells. White arrows indicate CoV-2 positiv immunolabeling. Naïve group: n=4, SARS-CoV-2 5×10 6 pfu/animal 5dpi group: n=1, vaccinated+infecte 10 6 pfu/animal 5dpi group: n=2. (M) Tissue/Air space ratio.
    Figure Legend Snippet: Histopathology and viral load of rVSV-ΔG-spike vaccinated and infected lungs: General histology (H E) and SARS-CoV-2 Immunolabeling of hamster lungs with and without pre vaccination. Lungs were isolated and processed for paraffin embedding from Naïve (A, E, I), vaccinated + infected 10 6 5dpi (B, F, J; C, G, K), and SARS-CoV-2 5×10 6 5dpi (D, H, L) and groups. Sections (5μm) were taken for H E staining (A-H) and SARS-CoV-2 immunolabeling (I-L, DAPI-Blue, SARS-CoV-2-Green). Pictures A-D: magnification-x1, bar= 100μm; Pictures E-H: magnification-x10, bar= 100μm; Pictures I-L: magnification-x60, bar= 10μm. Black arrows indicate patches of focal inflammation, pleural invaginatio and alveolar collapse. “*”-indicates hemorrhagic areas. “#”-indicates edema and protein rich exudates. Black arrow heads indicate pulmonary mononuclear cells. White arrows indicate CoV-2 positiv immunolabeling. Naïve group: n=4, SARS-CoV-2 5×10 6 pfu/animal 5dpi group: n=1, vaccinated+infecte 10 6 pfu/animal 5dpi group: n=2. (M) Tissue/Air space ratio.

    Techniques Used: Histopathology, Infection, Immunolabeling, Isolation, Staining

    Surface antigenic similarity of rVSV-ΔG-spike and SARS-CoV-2: (A) Immunofluorescent images of Vero E6 cells infected with either WT-VSV (left panel), rVSV-ΔG-spike (middle panel), or SARS-CoV-2, stained with serum from COVID-19 human convalescent serum (right panel). (B) Correlation analysis of neutralization of rVSV-ΔG-spike and SARS-CoV-2 by a panel of sera from COVID-19 convalescent patients. For each sera (n=12), NT 50 values were determined for neutralization of rVSV-ΔG-spike, or SARS-CoV-2. The NT 50 values were plotted to determine the correlation between th neutralization assays. R 2 =0.911.
    Figure Legend Snippet: Surface antigenic similarity of rVSV-ΔG-spike and SARS-CoV-2: (A) Immunofluorescent images of Vero E6 cells infected with either WT-VSV (left panel), rVSV-ΔG-spike (middle panel), or SARS-CoV-2, stained with serum from COVID-19 human convalescent serum (right panel). (B) Correlation analysis of neutralization of rVSV-ΔG-spike and SARS-CoV-2 by a panel of sera from COVID-19 convalescent patients. For each sera (n=12), NT 50 values were determined for neutralization of rVSV-ΔG-spike, or SARS-CoV-2. The NT 50 values were plotted to determine the correlation between th neutralization assays. R 2 =0.911.

    Techniques Used: Infection, Staining, Neutralization

    Characterization of rVSV-ΔG-spike: (A) A summary of the genome analysis of several passage of rVSV-ΔG-spike, showing Ct values of VSV-G, VSV-N, and SARS-CoV-2-S indicating the elimination of VSV-G over time, together with increased titer. Also, plaques are formed at late passages. (B) Immunofluorescence images of Vero E6 cells infected with early passage (P5)-rVSV-ΔG-spike, or lat passage (P13)-rVSV-ΔG-spike, stained with a SARS-CoV-2 antibody (green) and DAPI for nuclei stainin (blue). Top and bottom panels show insets at low (10X) and high magnification (25x), respectively. rVSV-ΔG-spike at P5 forms syncytia, whereas P13 show individual infected cells, with no evidence of syncytia. (C) Transmission electron microscopy of rVSV-ΔG-spike (top panel) compared to WT-VSV. Right panel shows immunogold labeling against RBD.
    Figure Legend Snippet: Characterization of rVSV-ΔG-spike: (A) A summary of the genome analysis of several passage of rVSV-ΔG-spike, showing Ct values of VSV-G, VSV-N, and SARS-CoV-2-S indicating the elimination of VSV-G over time, together with increased titer. Also, plaques are formed at late passages. (B) Immunofluorescence images of Vero E6 cells infected with early passage (P5)-rVSV-ΔG-spike, or lat passage (P13)-rVSV-ΔG-spike, stained with a SARS-CoV-2 antibody (green) and DAPI for nuclei stainin (blue). Top and bottom panels show insets at low (10X) and high magnification (25x), respectively. rVSV-ΔG-spike at P5 forms syncytia, whereas P13 show individual infected cells, with no evidence of syncytia. (C) Transmission electron microscopy of rVSV-ΔG-spike (top panel) compared to WT-VSV. Right panel shows immunogold labeling against RBD.

    Techniques Used: Immunofluorescence, Infection, Staining, Transmission Assay, Electron Microscopy, Labeling

    Single-dose rVSV-ΔG-spike vaccine efficacy in hamsters following SARS-CoV-2 challenge. (A) Body weight changes of hamsters infected with SARS-CoV-2 (n=12), and hamsters vaccinated wit rVSV-ΔG-spike and infected with 5×10 6 pfu/hamster (n=10) 25 days post-vaccination, compared to moc hamsters (n=8). p
    Figure Legend Snippet: Single-dose rVSV-ΔG-spike vaccine efficacy in hamsters following SARS-CoV-2 challenge. (A) Body weight changes of hamsters infected with SARS-CoV-2 (n=12), and hamsters vaccinated wit rVSV-ΔG-spike and infected with 5×10 6 pfu/hamster (n=10) 25 days post-vaccination, compared to moc hamsters (n=8). p

    Techniques Used: Infection

    Dose-dependent vaccination of hamsters with rVSV-ΔG-spike. (A) Body weight changes of mock-vaccinated hamsters (n=4), and hamsters vaccinated with rVSV-ΔG-spike ranging from 10 4 to 10 8 pfu/hamster (n=8, n=10, n=10, n=10, n=8, for each vaccinated group, respectively). (B) NT 50 values of neutralization of SARS-CoV-2 by sera from hamsters following i.m. vaccination with rVSV-ΔG-spik ranging from 10 4 to 10 8 pfu/hamster. n=4 for each group. Means and SEM are indicated below the graph.
    Figure Legend Snippet: Dose-dependent vaccination of hamsters with rVSV-ΔG-spike. (A) Body weight changes of mock-vaccinated hamsters (n=4), and hamsters vaccinated with rVSV-ΔG-spike ranging from 10 4 to 10 8 pfu/hamster (n=8, n=10, n=10, n=10, n=8, for each vaccinated group, respectively). (B) NT 50 values of neutralization of SARS-CoV-2 by sera from hamsters following i.m. vaccination with rVSV-ΔG-spik ranging from 10 4 to 10 8 pfu/hamster. n=4 for each group. Means and SEM are indicated below the graph.

    Techniques Used: Neutralization

    Establishment of golden Syrian hamster SARS-CoV-2 model: (A) Body weight changes of hamsters infected with SARS-CoV-2 at either 5×10 4 (n=7), 5×10 5 (n=7), or 5×10 6 (n=10) pfu/hamster, compared to mock-infected hamsters (n=6). p
    Figure Legend Snippet: Establishment of golden Syrian hamster SARS-CoV-2 model: (A) Body weight changes of hamsters infected with SARS-CoV-2 at either 5×10 4 (n=7), 5×10 5 (n=7), or 5×10 6 (n=10) pfu/hamster, compared to mock-infected hamsters (n=6). p

    Techniques Used: Infection

    rVSV-ΔG-spike design and generation strategy: (A) A schematic diagram of the genom organization of WT-VSV genome (top diagram) and rVSV-ΔG-spike (bottom diagram). N: Nucleoprotein, P: Phosphoprotein, M: Matrix, L: Large polymerase, G: Glycoprotein, SPIKE: SARS-CoV-2 spike. (B) pVSV-ΔG-spike map; in red, the inserted S gene. (C) Schematic representation of the generation proces of creating rVSV-ΔG-spike vaccine. Infection of BHK-21 cells with MVA-T7, followed by co-transfecti with pVSV-ΔG-spike, and VSV-system accessory plasmids; Transfection of BHK-21 cells with pCAGGS-VSV-G, followed by infection with the supernatant of the primary transfection to create P1; serial passaging to create rVSV-ΔG-spike.
    Figure Legend Snippet: rVSV-ΔG-spike design and generation strategy: (A) A schematic diagram of the genom organization of WT-VSV genome (top diagram) and rVSV-ΔG-spike (bottom diagram). N: Nucleoprotein, P: Phosphoprotein, M: Matrix, L: Large polymerase, G: Glycoprotein, SPIKE: SARS-CoV-2 spike. (B) pVSV-ΔG-spike map; in red, the inserted S gene. (C) Schematic representation of the generation proces of creating rVSV-ΔG-spike vaccine. Infection of BHK-21 cells with MVA-T7, followed by co-transfecti with pVSV-ΔG-spike, and VSV-system accessory plasmids; Transfection of BHK-21 cells with pCAGGS-VSV-G, followed by infection with the supernatant of the primary transfection to create P1; serial passaging to create rVSV-ΔG-spike.

    Techniques Used: Infection, Transfection, Passaging

    Detection and neutralization of SARS-CoV-2 by sera from hamsters following s.c. vaccinatio with rVSV-ΔG-spike: (A) Immunofluorescence images of Vero E6 cells infected with SARS-CoV-2, stai with sera from either mock-vaccinated hamsters (left panel) or rVSV-ΔG-spike vaccinated-hamsters (right panel). (B) Plaque reduction neutralization test (PRNT) of hamster sera collected from naïve hamster (PBF, n=5) or hamsters vaccinated with rVSV-ΔG-spike 25 days following vaccination (n=5). (C) Bod weight changes of mock-vaccinated hamsters (Mock, n=16), and hamsters vaccinated with rVSV-ΔG-spike (n=8).
    Figure Legend Snippet: Detection and neutralization of SARS-CoV-2 by sera from hamsters following s.c. vaccinatio with rVSV-ΔG-spike: (A) Immunofluorescence images of Vero E6 cells infected with SARS-CoV-2, stai with sera from either mock-vaccinated hamsters (left panel) or rVSV-ΔG-spike vaccinated-hamsters (right panel). (B) Plaque reduction neutralization test (PRNT) of hamster sera collected from naïve hamster (PBF, n=5) or hamsters vaccinated with rVSV-ΔG-spike 25 days following vaccination (n=5). (C) Bod weight changes of mock-vaccinated hamsters (Mock, n=16), and hamsters vaccinated with rVSV-ΔG-spike (n=8).

    Techniques Used: Neutralization, Immunofluorescence, Infection, Plaque Reduction Neutralization Test

    Related Articles

    Neutralization:

    Article Title: Recombinant SARS-CoV-2 RBD with a built in T helper epitope induces strong neutralization antibody response
    Article Snippet: .. Neutralization activity elicited by Ad5-nCoV vaccine reached about 28 (256) in mice based on SARS-CoV-2 neutralization assay . .. In this study, the immune serum could protect Vero E6 cells from SARS-CoV-2 infection with neutralizing antibody titer 256 on Day35 ( A).

    Infection:

    Article Title: A single dose of recombinant VSV-ΔG-spike vaccine provides protection against SARS-CoV-2 challenge
    Article Snippet: .. The hamster model is a robust and reproducible model as evident by the dose-dependent response in body weight to different SARS-CoV-2 infection doses. ..

    Mouse Assay:

    Article Title: Recombinant SARS-CoV-2 RBD with a built in T helper epitope induces strong neutralization antibody response
    Article Snippet: .. Neutralization activity elicited by Ad5-nCoV vaccine reached about 28 (256) in mice based on SARS-CoV-2 neutralization assay . .. In this study, the immune serum could protect Vero E6 cells from SARS-CoV-2 infection with neutralizing antibody titer 256 on Day35 ( A).

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development
    Article Snippet: .. SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV. .. Luciferase assay system (Cat: E1501) was purchased from Promega.

    Generated:

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development
    Article Snippet: .. SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV. .. Luciferase assay system (Cat: E1501) was purchased from Promega.

    Activity Assay:

    Article Title: Recombinant SARS-CoV-2 RBD with a built in T helper epitope induces strong neutralization antibody response
    Article Snippet: .. Neutralization activity elicited by Ad5-nCoV vaccine reached about 28 (256) in mice based on SARS-CoV-2 neutralization assay . .. In this study, the immune serum could protect Vero E6 cells from SARS-CoV-2 infection with neutralizing antibody titer 256 on Day35 ( A).

    Western Blot:

    Article Title: Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration
    Article Snippet: .. Identity of expressed protein and also viral Spike was determined using western blotting with anti-Fc (Jackson), anti-RBD (Sino Biologicals), anti-S2 (Sino Biologicals) and anti-ACE2 (R & D Systems) pAbs. .. Identity of expressed protein and also viral Spike was determined using western blotting with anti-Fc (Jackson), anti-RBD (Sino Biologicals), anti-S2 (Sino Biologicals) and anti-ACE2 (R & D Systems) pAbs.

    Recombinant:

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development
    Article Snippet: .. SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV. .. Luciferase assay system (Cat: E1501) was purchased from Promega.

    Plaque Reduction Neutralization Test:

    Article Title: SARS-CoV-2 is transmitted via contact and via the air between ferrets
    Article Snippet: .. Additionally, presera and sera collected at 21 dpi/dpe were tested for the presence of SARS-CoV-2 neutralizing antibodies using a plaque reduction neutralization test (PRNT) . ..

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    Sino Biological anti s2
    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. ( A ) Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] - and [N] - 293 T cells. All nine viruses were applied at equal titer to stable 293T/ACE2. ( B–C ) O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. ( D ) Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. ( E ) Western blot of Spike protein using <t>anti-S2</t> Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] - 293T products due to truncation of glycan biosynthesis. ( F ) Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] - 293Ts is almost fully proteolyzed during viral production (red arrowhead). *p
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    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. ( A ) Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] - and [N] - 293 T cells. All nine viruses were applied at equal titer to stable 293T/ACE2. ( B–C ) O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. ( D ) Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. ( E ) Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] - 293T products due to truncation of glycan biosynthesis. ( F ) Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] - 293Ts is almost fully proteolyzed during viral production (red arrowhead). *p

    Journal: eLife

    Article Title: Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration

    doi: 10.7554/eLife.61552

    Figure Lengend Snippet: N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. ( A ) Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] - and [N] - 293 T cells. All nine viruses were applied at equal titer to stable 293T/ACE2. ( B–C ) O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. ( D ) Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. ( E ) Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] - 293T products due to truncation of glycan biosynthesis. ( F ) Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] - 293Ts is almost fully proteolyzed during viral production (red arrowhead). *p

    Article Snippet: Identity of expressed protein and also viral Spike was determined using western blotting with anti-Fc (Jackson), anti-RBD (Sino Biologicals), anti-S2 (Sino Biologicals) and anti-ACE2 (R and D Systems) pAbs.

    Techniques: Modification, Expressing, Mutagenesis, Produced, Generated, Titration, Infection, Western Blot

    N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. A . Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] − and [N] − 293T cells. All 9 viruses were applied at equal titer to stable 293T/ACE2. B - C . O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. D . Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. E . Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] − 293T products due to truncation of glycan biosynthesis. F . Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] − 293Ts is almost fully proteolyzed during viral production (red arrowhead). * P

    Journal: bioRxiv

    Article Title: Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration

    doi: 10.1101/2020.10.15.339838

    Figure Lengend Snippet: N-glycan modification of SARS-CoV-2 pseudovirus abolishes entry into 293T/ACE2 cells. A . Pseudovirus expressing VSVG envelope protein, Spike-WT and Spike-mutant were produced in wild-type, [O] − and [N] − 293T cells. All 9 viruses were applied at equal titer to stable 293T/ACE2. B - C . O-glycan truncation of Spike partially reduced viral entry. N-glycan truncation abolished viral entry. In order to combine data from multiple viral preparations and independent runs in a single plot, all data were normalized by setting DsRed signal produced by virus generated in wild-type 293T to 10,000 normalized MFI or 100% normalized DsRed positive value. D . Viral titration study performed with Spike-mutant virus shows complete loss of viral infection over a wide range. E . Western blot of Spike protein using anti-S2 Ab shows reduced proteolysis of Spike-mut compared to Spike-WT. The full Spike protein and free S2-subunit resulting from S1-S2 cleavage is indicated. Molecular mass is reduced in [N] − 293T products due to truncation of glycan biosynthesis. F . Anti-FLAG Ab binds the C-terminus of Spike-mutant. Spike produced in [N] − 293Ts is almost fully proteolyzed during viral production (red arrowhead). * P

    Article Snippet: Identity of expressed protein and also viral Spike was determined using western blotting with anti-Fc (Jackson), anti-RBD (Sino Biologicals), anti-S2 (Sino Biologicals) and anti-ACE2 (R & D Systems) pAbs.

    Techniques: Modification, Expressing, Mutagenesis, Produced, Generated, Titration, Infection, Western Blot

    Structural conservation of SARS-CoV RBD. RBD is shown as colored surface. ACE2 is shown as gray cartoon. The three surface mutation sites (i.e. N354D, D364Y, and V367F) observed in SARS-CoV-2 RBD are labeled. Mutation F342L is buried and not shown here.

    Journal: bioRxiv

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development

    doi: 10.1101/2020.02.16.951723

    Figure Lengend Snippet: Structural conservation of SARS-CoV RBD. RBD is shown as colored surface. ACE2 is shown as gray cartoon. The three surface mutation sites (i.e. N354D, D364Y, and V367F) observed in SARS-CoV-2 RBD are labeled. Mutation F342L is buried and not shown here.

    Article Snippet: SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV.

    Techniques: Mutagenesis, Labeling

    Structure similarity between SARS-CoV-2 RBD and SARS-CoV RBD. RBD is shown in a space-filled model with colored surface. ACE2 is shown as gray tube model. The three glycosylation sites in SARS-CoV are labeled. Note that N 357 ST in SARS-CoV is changed to N 370 SA in SARS-CoV-2, which is different from the NXS/T pattern required for glycosylation, and hence this site is more likely to be unglycosylated. The two possible cross-reactive regions are marked with yellow circles.

    Journal: bioRxiv

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development

    doi: 10.1101/2020.02.16.951723

    Figure Lengend Snippet: Structure similarity between SARS-CoV-2 RBD and SARS-CoV RBD. RBD is shown in a space-filled model with colored surface. ACE2 is shown as gray tube model. The three glycosylation sites in SARS-CoV are labeled. Note that N 357 ST in SARS-CoV is changed to N 370 SA in SARS-CoV-2, which is different from the NXS/T pattern required for glycosylation, and hence this site is more likely to be unglycosylated. The two possible cross-reactive regions are marked with yellow circles.

    Article Snippet: SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV.

    Techniques: Labeling

    Cross-reactivity and neutralization efficiency of SARS nAbs against SARS-CoV-2. A. Binding of SARS nAbs to SARS-CoV S1 protein were tested by ELISA. Recombinant S1 protein of SARS-CoV were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. B. Binding of SARS nAbs to SARS-CoV-2 S1 protein were tested by ELSIA. Recombinant S1 protein of SARS-CoV-2 were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. C. Neutralization of SARS-CoV nAbs against SARS-CoV-2 PSV. D. Antibody competition with SARS-CoV RBD binding to ACE2. Recombinant SARS-CoV RBD protein was coated on plates, nAbs and recombinant ACE2 were then added for RBD binding competition measurements.

    Journal: bioRxiv

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development

    doi: 10.1101/2020.02.16.951723

    Figure Lengend Snippet: Cross-reactivity and neutralization efficiency of SARS nAbs against SARS-CoV-2. A. Binding of SARS nAbs to SARS-CoV S1 protein were tested by ELISA. Recombinant S1 protein of SARS-CoV were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. B. Binding of SARS nAbs to SARS-CoV-2 S1 protein were tested by ELSIA. Recombinant S1 protein of SARS-CoV-2 were coated on plates, serial diluted nAbs were added for binding to recombinant S1 protein. C. Neutralization of SARS-CoV nAbs against SARS-CoV-2 PSV. D. Antibody competition with SARS-CoV RBD binding to ACE2. Recombinant SARS-CoV RBD protein was coated on plates, nAbs and recombinant ACE2 were then added for RBD binding competition measurements.

    Article Snippet: SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV.

    Techniques: Neutralization, Binding Assay, Enzyme-linked Immunosorbent Assay, Recombinant

    Sequence analysis and structure modeling of SARS-CoV-2 RBD and SARS-CoV RBD and their interactions with ACE2. A. RBD sequence alignment of SARS-CoV and SARS-CoV-2, highlighting the predominant residues that contribute to the interactions with ACE2. The distinct interactions of RBD and ACE2 for the two viruses are indicated by the down-pointing orange triangles and up-pointing red triangles, respectively. RBM residues are underlined. The one-residue insertion is indicated by the red arrow. Asterisks indicate positions of fully conserved residues. Colons indicate positions of strictly conserved residues. Periods indicate positions of weakly conserved residues. B. Conformational comparison between the RBD-ACE2 complex structures for SARS-CoV-2 and SARS-CoV. The RBD and ACE2 structures in the SARS-CoV-2 RBD-ACE2 complex model are shown as orange and pink tubes, respectively. The RBD and ACE2 structures in the optimized SARS-CoV RBD-ACE2 complex structure are shown as blue and green tubes, respectively. The location of noticeable subtle conformational difference is indicated by an arrow. C. Distinct interaction patterns in the SARS-CoV-2 and SARS-CoV RBD-ACE2 interfaces. Structures of RBD and ACE2 are shown as cartoon in pink and green colors, respectively. The side chains of the residues in both protein components, representing their unique interactions, are shown as sticks. Polar interactions (salt-bridge and hydrogen bond) are shown as blue dash line. Non-polar interactions (π-stack, π-anion, and hydrophobic interactions) are shown as orange dash line.

    Journal: bioRxiv

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development

    doi: 10.1101/2020.02.16.951723

    Figure Lengend Snippet: Sequence analysis and structure modeling of SARS-CoV-2 RBD and SARS-CoV RBD and their interactions with ACE2. A. RBD sequence alignment of SARS-CoV and SARS-CoV-2, highlighting the predominant residues that contribute to the interactions with ACE2. The distinct interactions of RBD and ACE2 for the two viruses are indicated by the down-pointing orange triangles and up-pointing red triangles, respectively. RBM residues are underlined. The one-residue insertion is indicated by the red arrow. Asterisks indicate positions of fully conserved residues. Colons indicate positions of strictly conserved residues. Periods indicate positions of weakly conserved residues. B. Conformational comparison between the RBD-ACE2 complex structures for SARS-CoV-2 and SARS-CoV. The RBD and ACE2 structures in the SARS-CoV-2 RBD-ACE2 complex model are shown as orange and pink tubes, respectively. The RBD and ACE2 structures in the optimized SARS-CoV RBD-ACE2 complex structure are shown as blue and green tubes, respectively. The location of noticeable subtle conformational difference is indicated by an arrow. C. Distinct interaction patterns in the SARS-CoV-2 and SARS-CoV RBD-ACE2 interfaces. Structures of RBD and ACE2 are shown as cartoon in pink and green colors, respectively. The side chains of the residues in both protein components, representing their unique interactions, are shown as sticks. Polar interactions (salt-bridge and hydrogen bond) are shown as blue dash line. Non-polar interactions (π-stack, π-anion, and hydrophobic interactions) are shown as orange dash line.

    Article Snippet: SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV.

    Techniques: Sequencing

    Measurements of SARS-CoV-2 and SARS-CoV S1 binding to ACE2. A. Serial diluted recombinant S1 proteins of SARS-CoV-2, SARS-CoV and MERS-CoV were coated on 96 well plates, incubated with the recombinant Fc-tagged ACE2 (ACE2-Fc) for binding evaluation. B. Recombinant S1 proteins of SARS-CoV-2 and SARS-CoV were incubated with 293T-ACE2 cells and subjected to FACS evaluation for binding.

    Journal: bioRxiv

    Article Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development

    doi: 10.1101/2020.02.16.951723

    Figure Lengend Snippet: Measurements of SARS-CoV-2 and SARS-CoV S1 binding to ACE2. A. Serial diluted recombinant S1 proteins of SARS-CoV-2, SARS-CoV and MERS-CoV were coated on 96 well plates, incubated with the recombinant Fc-tagged ACE2 (ACE2-Fc) for binding evaluation. B. Recombinant S1 proteins of SARS-CoV-2 and SARS-CoV were incubated with 293T-ACE2 cells and subjected to FACS evaluation for binding.

    Article Snippet: SARS-CoV neutralizing antibodies were generated from mice (M103, M127) or rabbits (R314, R301, R325, R302, R258, R348) immunized with recombinant S1 protein of SARS-CoV.

    Techniques: Binding Assay, Recombinant, Incubation, FACS