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    Sino Biological sars cov 2 2019 ncov spike rbd g476s his recombinant protein
    Sequence diversity and characterization of 235 <t>SARS-CoV-2</t> S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). 27 circular dendrogram figure constructed using interactive tree of life (iTOL). 28
    Sars Cov 2 2019 Ncov Spike Rbd G476s His Recombinant Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sequence diversity and characterization of 235 SARS-CoV-2 S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). 27 circular dendrogram figure constructed using interactive tree of life (iTOL). 28

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Sequence diversity and characterization of 235 SARS-CoV-2 S1-binding antibodies. Phylogenetic tree of SARS-CoV-2 S1-binding IgG (blue lines) and VHH-Fc (black lines) candidates identified by phage display. Green bars represent the binding affinity of each candidate as measured by SPR. Relative binding affinity is displayed linearly, a longer bar indicates improved binding affinity. The longest bar represents an observed binding affinity of 2 nM, the shortest visible bar represents 6.6 μM. No bar indicates no binding observed. Purple gradient represents the percent inhibition of each antibody in the Vero E6 competition assay at 100 nM mAb, weak inhibitors are represented in white, strong inhibitors are represented in purple. Phylogenetic tree data generated by aligning variable heavy sequences with MUltiple Sequence Comparison by Log-Expectation (MUSCLE). 27 circular dendrogram figure constructed using interactive tree of life (iTOL). 28

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Sequencing, Binding Assay, SPR Assay, Inhibition, Competitive Binding Assay, Generated, Construct

    Effect of antibody cocktail treatment post-exposure in hamster challenge model (USAMRIID). (a) Animals were immunosuppressed and then exposed to SARS-CoV-2 virus, WA1 strain, on Day 0. Antibody cocktail containing TB181–36 and TB202–63 was administered on the indicated day post-exposure (D1, D2, etc marked by blue arrow, corresponding to Groups B-G). A control group received the cocktail on Day −1 (D-1, Group A). A group was immunosuppressed but not exposed to virus (cyclophosphamide [CYP] control, group i). An IgG monoclonal (c7D11 33 ) was administered to Group H as a negative control. Data is presented as mean ± standard error of mean, *p

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Effect of antibody cocktail treatment post-exposure in hamster challenge model (USAMRIID). (a) Animals were immunosuppressed and then exposed to SARS-CoV-2 virus, WA1 strain, on Day 0. Antibody cocktail containing TB181–36 and TB202–63 was administered on the indicated day post-exposure (D1, D2, etc marked by blue arrow, corresponding to Groups B-G). A control group received the cocktail on Day −1 (D-1, Group A). A group was immunosuppressed but not exposed to virus (cyclophosphamide [CYP] control, group i). An IgG monoclonal (c7D11 33 ) was administered to Group H as a negative control. Data is presented as mean ± standard error of mean, *p

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Negative Control

    Neutralizing activity of top antibody candidates. (a) 40 blinded samples were tested in a PRNT (at USAMRIID) using the authentic SARS-CoV-2 Washington isolate. All samples were run in at least two independent assays. Shaded bars indicate only one value used to determine titer, where the first assay used in a dilution series does not reach an endpoint titer. The NT 80 value was calculated by dividing the sample concentration by PRNT 80 titer. NT 80 values were sorted lowest to highest, or most potent to least potent. (b) in a separate experiment conducted by IBT, IgG and VHH antibodies again demonstrated potent neutralization in an authentic SARS-CoV-2 PRNT. NT 50 and NT 90 represent the antibody concentration required to reduce the number of plaques by 50% or 90%, respectively, compared to free virus

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Neutralizing activity of top antibody candidates. (a) 40 blinded samples were tested in a PRNT (at USAMRIID) using the authentic SARS-CoV-2 Washington isolate. All samples were run in at least two independent assays. Shaded bars indicate only one value used to determine titer, where the first assay used in a dilution series does not reach an endpoint titer. The NT 80 value was calculated by dividing the sample concentration by PRNT 80 titer. NT 80 values were sorted lowest to highest, or most potent to least potent. (b) in a separate experiment conducted by IBT, IgG and VHH antibodies again demonstrated potent neutralization in an authentic SARS-CoV-2 PRNT. NT 50 and NT 90 represent the antibody concentration required to reduce the number of plaques by 50% or 90%, respectively, compared to free virus

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Activity Assay, Plaque Reduction Neutralization Test, Concentration Assay, Neutralization

    Epitope mapping of SARS-CoV-2 S1-binding antibodies. (a) Solvent-accessible surface representation of spike protein trimer in closed (PDB: 6VXX) and open (PDB: 6VSB) conformations. VHH-Fc nanobodies (TB201, TB202) binding sites overlap with that of ACE2 in both conformations, while TB181 and TB182 IgGs access a more occluded region. (b) Cartoon representation of SARS-CoV-2 S protein RBD with critical residues highlighted as spheres for each monoclonal antibody. (c) Negative-staining electron microscopy analysis shows the distinct binding regions of antibodies identified from the distinct antibody libraries used in this study (colored surface). The SARS-CoV-2 spike protein NTD, C-terminal domain (CTD), RBD and bound ACE2 are shown as cartoon representations

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Epitope mapping of SARS-CoV-2 S1-binding antibodies. (a) Solvent-accessible surface representation of spike protein trimer in closed (PDB: 6VXX) and open (PDB: 6VSB) conformations. VHH-Fc nanobodies (TB201, TB202) binding sites overlap with that of ACE2 in both conformations, while TB181 and TB182 IgGs access a more occluded region. (b) Cartoon representation of SARS-CoV-2 S protein RBD with critical residues highlighted as spheres for each monoclonal antibody. (c) Negative-staining electron microscopy analysis shows the distinct binding regions of antibodies identified from the distinct antibody libraries used in this study (colored surface). The SARS-CoV-2 spike protein NTD, C-terminal domain (CTD), RBD and bound ACE2 are shown as cartoon representations

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Binding Assay, Negative Staining, Electron Microscopy

    Identification of high-affinity mAbs against SARS-CoV-2 S1 subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. 26 SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Identification of high-affinity mAbs against SARS-CoV-2 S1 subunit and pre-fusion stabilized S trimers. (a) Schematic of antibody library designs used in phage panning. Numbers on white text on green indicate the number of CDRs represented within each oligo pool per library. Purple blocks represent human or humanized germline framework regions; gray blocks represent llama framework regions. (b) Binding affinity of lead antibodies, as determined by SPR, demonstrating nanomolar binding to the SARS-CoV-2 spike S1 subunit. Leads from TB181 COVID-19 scFv and TB182 Fab libraries were reformatted and expressed as IgG1, while leads from TB201 VHH and TB202 VHH libraries were converted to VHH-Fc. Apparent binding affinity to spike trimers stabilized in the pre-fusion conformation are in the picomolar range. 26 SPR experiments were performed on a Carterra LSA SPR biosensor, binding affinities were calculated by fitting to 1:1 model in Carterra Kinetics Tool software. See Materials and Methods for complete assay description. (c) Competition ELISA showing decreasing levels of S1 RBD binding to immobilized ACE2 on Nunc Maxisorp plates with increasing concentrations of antibody. The experiment was performed in singlicate. (d) inhibition flow cytometry experiment showing lowering levels of S1 RBD binding to Vero E6 cells expressing ACE2 as measured by decreasing mean fluorescence intensity (MFI) as antibody concentrations increase. The experiment was performed in triplicate with standard deviation shown as error bars

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Binding Assay, SPR Assay, Software, Enzyme-linked Immunosorbent Assay, Inhibition, Flow Cytometry, Expressing, Fluorescence, Standard Deviation

    Competition binning of SARS-CoV-2 S1-binding antibodies. Cross-competition of antibody candidates with SARS-CoV-2 S1 protein was assayed by high throughput (HT)-SPR using the carterra LSA. Red, yellow, and green cells in the heat map represent competitive, weakly competitive, and noncompetitive blocked analyte/ligand pairs, respectively. White cells represent unaddressed pairs in the assay. Numbers in cell indicate the relative binding response to SARS-CoV-2 S1 only

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Competition binning of SARS-CoV-2 S1-binding antibodies. Cross-competition of antibody candidates with SARS-CoV-2 S1 protein was assayed by high throughput (HT)-SPR using the carterra LSA. Red, yellow, and green cells in the heat map represent competitive, weakly competitive, and noncompetitive blocked analyte/ligand pairs, respectively. White cells represent unaddressed pairs in the assay. Numbers in cell indicate the relative binding response to SARS-CoV-2 S1 only

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Binding Assay, High Throughput Screening Assay, SPR Assay

    Hamster challenge models. (a-c) In a pre-challenge hamster challenge model, 31 administration of monoclonal antibodies 12 hours prior to SARS-CoV-2 (WA1) infection prevented weight loss. TB202–3 and TB202–63, both in VHH-Fc format, conferred protection from weight loss at 1 mg/kg relative to isotype control c7D11 (*p

    Journal: mAbs

    Article Title: Rapid discovery of diverse neutralizing SARS-CoV-2 antibodies from large-scale synthetic phage libraries

    doi: 10.1080/19420862.2021.2002236

    Figure Lengend Snippet: Hamster challenge models. (a-c) In a pre-challenge hamster challenge model, 31 administration of monoclonal antibodies 12 hours prior to SARS-CoV-2 (WA1) infection prevented weight loss. TB202–3 and TB202–63, both in VHH-Fc format, conferred protection from weight loss at 1 mg/kg relative to isotype control c7D11 (*p

    Article Snippet: Commercially sourced SARS-CoV-2 protein reagents were as follows: S1 WA1 (Acro S1N-C52H4), S1 D614G (Acro S1N-C5256), S1 HV69–70del N501Y D614G (Sino Biological 40591-V08H7), S1 HV69–70del Y453F D614G (Sino Biological 40591-V08H8), S RBD WA1 (Acro SPD-C52H3), S RBD N501Y (Acro SPD-C52Hn), S RBD Y453F (Sino Biological SPD-C52Hn), S RBD N439K (Sino Biological 40592-V08H1), S RBD K417N (Sino Biological 40592-V08H5), S RBD E484K (Sino Biological 40592-V08H8), SARS S1 (Acro S1N-S52H5), S Trimer WA1 (Acro SPN-C52H9), S Trimer B.1.1.7 Alpha (Acro SPN-C52H6), S Trimer B.1.351 Beta (Acro SPN-C52Hk), S Trimer P.1 Gamma (Acro SPN-C52Hg), S Trimer B.1.617.1 Kappa (Acro SPN-C52Hr), S Trimer B.1.617.2 Delta (Acro SPN-C52He).

    Techniques: Infection