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    Sino Biological sars cov sars cov 2 spike antibody chimeric mab
    Bifunctional molecules Display Specific Functional Activity Against <t>SARS-CoV-2</t> . (a) Functional competition ability is plotted vs. antibody concentration. Antibodies are indicated in the graph. (b) PBMC-mediated ADCC of MDCK-pIgR cells is plotted as green area per well (normalized to 0 h) vs concentration of bifunctional molecule (nM). Antibodies are indicated in the legend
    Sars Cov Sars Cov 2 Spike Antibody Chimeric Mab, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sars cov sars cov 2 spike antibody chimeric mab/product/Sino Biological
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sars cov sars cov 2 spike antibody chimeric mab - by Bioz Stars, 2022-08
    95/100 stars
      Buy from Supplier

    94
    Sino Biological sars cov 2 2019 ncov spike s2 antibody chimeric mab
    Alignment of selected PEPs with the viral <t>spike</t> sequences. The peptides were derived from a part of the <t>SARS-CoV-2</t> spike <t>S2</t> domain (residues 806-1091), encompassing the S2′ cleavage site, fusion peptide and heptad repeat 1. On the left, the structure of the SARS-CoV-2 spike in closed conformation is shown (PDB 6ZGE). The right panel shows an alignment of the relevant S2 sequences of SARS-CoV-2 (NCBI accession number YP_009724390), HCoV-OC43 (YP_009555241) and HCoV-229E (NP_073551), as well as the corresponding peptides. Sequence similarities from Clustal Omega-aligned sequences were rendered using ESPript 3.0. Shown in red shading: fully conserved residues; in red font: residues are similar according to physicochemical properties; and boxed in blue: ≥70% similarity. Secondary structure depiction shown on top was derived from PDB 6ZGE.
    Sars Cov 2 2019 Ncov Spike S2 Antibody Chimeric Mab, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sars cov 2 2019 ncov spike s2 antibody chimeric mab/product/Sino Biological
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sars cov 2 2019 ncov spike s2 antibody chimeric mab - by Bioz Stars, 2022-08
    94/100 stars
      Buy from Supplier

    Image Search Results


    Bifunctional molecules Display Specific Functional Activity Against SARS-CoV-2 . (a) Functional competition ability is plotted vs. antibody concentration. Antibodies are indicated in the graph. (b) PBMC-mediated ADCC of MDCK-pIgR cells is plotted as green area per well (normalized to 0 h) vs concentration of bifunctional molecule (nM). Antibodies are indicated in the legend

    Journal: mAbs

    Article Title: Bifunctional molecules targeting SARS-CoV-2 spike and the polymeric Ig receptor display neutralization activity and mucosal enrichment

    doi: 10.1080/19420862.2021.1987180

    Figure Lengend Snippet: Bifunctional molecules Display Specific Functional Activity Against SARS-CoV-2 . (a) Functional competition ability is plotted vs. antibody concentration. Antibodies are indicated in the graph. (b) PBMC-mediated ADCC of MDCK-pIgR cells is plotted as green area per well (normalized to 0 h) vs concentration of bifunctional molecule (nM). Antibodies are indicated in the legend

    Article Snippet: Of these, VHH2 and VHH6 were included in this analysis since VHH2 displayed cross-reactivity to mouse pIgR and both displayed strong transcytosis in an MDCK monolayer-based assay and in a human epithelial airway model. To mediate binding to the SARS-CoV-2 spike glycoprotein, we identified 2 antibodies that were reported to display neutralization activity – D001 (Sino Biological cat. # 40150-D001) and SAD-S35 (Acro Biosystems cat. # SAD-S35).

    Techniques: Functional Assay, Activity Assay, Concentration Assay

    Summary of the mechanism of pIgR-based targeted transport . SARS-CoV-2 viral entry occurs upon binding of the RBD domain of its spike glycoprotein to the ACE2 receptor on target cells. Bifunctional molecules gain access to the lung mucosa through pIgR-mediated transport and bind/neutralize SARS-CoV-2 by binding the RBD domain through their ACE2 ECD moiety in a steric mechanism

    Journal: mAbs

    Article Title: Bifunctional molecules targeting SARS-CoV-2 spike and the polymeric Ig receptor display neutralization activity and mucosal enrichment

    doi: 10.1080/19420862.2021.1987180

    Figure Lengend Snippet: Summary of the mechanism of pIgR-based targeted transport . SARS-CoV-2 viral entry occurs upon binding of the RBD domain of its spike glycoprotein to the ACE2 receptor on target cells. Bifunctional molecules gain access to the lung mucosa through pIgR-mediated transport and bind/neutralize SARS-CoV-2 by binding the RBD domain through their ACE2 ECD moiety in a steric mechanism

    Article Snippet: Of these, VHH2 and VHH6 were included in this analysis since VHH2 displayed cross-reactivity to mouse pIgR and both displayed strong transcytosis in an MDCK monolayer-based assay and in a human epithelial airway model. To mediate binding to the SARS-CoV-2 spike glycoprotein, we identified 2 antibodies that were reported to display neutralization activity – D001 (Sino Biological cat. # 40150-D001) and SAD-S35 (Acro Biosystems cat. # SAD-S35).

    Techniques: Binding Assay

    Alignment of selected PEPs with the viral spike sequences. The peptides were derived from a part of the SARS-CoV-2 spike S2 domain (residues 806-1091), encompassing the S2′ cleavage site, fusion peptide and heptad repeat 1. On the left, the structure of the SARS-CoV-2 spike in closed conformation is shown (PDB 6ZGE). The right panel shows an alignment of the relevant S2 sequences of SARS-CoV-2 (NCBI accession number YP_009724390), HCoV-OC43 (YP_009555241) and HCoV-229E (NP_073551), as well as the corresponding peptides. Sequence similarities from Clustal Omega-aligned sequences were rendered using ESPript 3.0. Shown in red shading: fully conserved residues; in red font: residues are similar according to physicochemical properties; and boxed in blue: ≥70% similarity. Secondary structure depiction shown on top was derived from PDB 6ZGE.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Alignment of selected PEPs with the viral spike sequences. The peptides were derived from a part of the SARS-CoV-2 spike S2 domain (residues 806-1091), encompassing the S2′ cleavage site, fusion peptide and heptad repeat 1. On the left, the structure of the SARS-CoV-2 spike in closed conformation is shown (PDB 6ZGE). The right panel shows an alignment of the relevant S2 sequences of SARS-CoV-2 (NCBI accession number YP_009724390), HCoV-OC43 (YP_009555241) and HCoV-229E (NP_073551), as well as the corresponding peptides. Sequence similarities from Clustal Omega-aligned sequences were rendered using ESPript 3.0. Shown in red shading: fully conserved residues; in red font: residues are similar according to physicochemical properties; and boxed in blue: ≥70% similarity. Secondary structure depiction shown on top was derived from PDB 6ZGE.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Derivative Assay, Sequencing

    Reactivity of cat samples in seroneutralization assays and pepscan. Samples from FIP cats (cats 3, 4, 7, 19 and 22) were collected between 2004 and 2007, the other samples were collected in 2020 for diagnosis of FeCV (cats 164, 243 and 245) or SARS-CoV-2 (cat 40). The virus-neutralizing activity (left) was determined by seroneutralization (SN) assay against FeCV in feline enterocytes, and SARS-CoV-2 in VeroE6 cells. The limit of detection (LOD) was a 1:8 (FeCV) or 1:40 dilution (SARS-CoV-2). A pepscan (right) was performed using PEP1-4 (derived from SARS-CoV-2 S), PEP71 (HCoV-OC43 S) and PEP72 (HCoV-229E S). The fold increase in OD 450 nm value is shown versus negative control peptide PEP74.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Reactivity of cat samples in seroneutralization assays and pepscan. Samples from FIP cats (cats 3, 4, 7, 19 and 22) were collected between 2004 and 2007, the other samples were collected in 2020 for diagnosis of FeCV (cats 164, 243 and 245) or SARS-CoV-2 (cat 40). The virus-neutralizing activity (left) was determined by seroneutralization (SN) assay against FeCV in feline enterocytes, and SARS-CoV-2 in VeroE6 cells. The limit of detection (LOD) was a 1:8 (FeCV) or 1:40 dilution (SARS-CoV-2). A pepscan (right) was performed using PEP1-4 (derived from SARS-CoV-2 S), PEP71 (HCoV-OC43 S) and PEP72 (HCoV-229E S). The fold increase in OD 450 nm value is shown versus negative control peptide PEP74.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Activity Assay, Derivative Assay, Negative Control

    Isolation of peptide-purified antibodies (pAbs) from human serum. (A) Pepscan analysis of human serum sample #20Hu384 (obtained from a COVID-19 convalescent patient) prior to purification. (B) Purification principle. Serum #20Hu384 was submitted to peptide-affinity chromatography using immobilized PEP3, PEP71, PEP72 or PEP79. (C) Elution profiles during chromatography. The fractions with the highest concentrations were combined. (D) Pepscan analysis of the pAbs purified on columns with immobilized PEP3, PEP71, PEP72 or PEP79. The lowest panel shows the profile of the control sample containing late (low-protein) elution fractions (= fractions 8 and 9 from PEP79 column). The bars show the OD 450 nm value. (E) Western blot analysis of S-plasmid transfected PK-15 cells shows binding of pAb-PEP3 to cleaved (S2) and full-length SARS-CoV-2 S. (F) Antibody titers of serum #20Hu384, the four pAbs and elution buffer in IPMA assays for SARS-CoV-2 S and N; HCoV-229E and -OC43; and FeCV.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Isolation of peptide-purified antibodies (pAbs) from human serum. (A) Pepscan analysis of human serum sample #20Hu384 (obtained from a COVID-19 convalescent patient) prior to purification. (B) Purification principle. Serum #20Hu384 was submitted to peptide-affinity chromatography using immobilized PEP3, PEP71, PEP72 or PEP79. (C) Elution profiles during chromatography. The fractions with the highest concentrations were combined. (D) Pepscan analysis of the pAbs purified on columns with immobilized PEP3, PEP71, PEP72 or PEP79. The lowest panel shows the profile of the control sample containing late (low-protein) elution fractions (= fractions 8 and 9 from PEP79 column). The bars show the OD 450 nm value. (E) Western blot analysis of S-plasmid transfected PK-15 cells shows binding of pAb-PEP3 to cleaved (S2) and full-length SARS-CoV-2 S. (F) Antibody titers of serum #20Hu384, the four pAbs and elution buffer in IPMA assays for SARS-CoV-2 S and N; HCoV-229E and -OC43; and FeCV.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Isolation, Purification, Affinity Chromatography, Chromatography, Western Blot, Plasmid Preparation, Transfection, Binding Assay

    Antibody titers in pre-pandemic human plasma samples (N = 496; period 2016-2017). The IPMA titers for antibodies against HCoV-229E, HCoV-OC43, SARS-CoV-2 S and SARS-CoV-2 N of a panel of 496 pre-pandemic plasma samples are given in pie charts (left). For each slice, the absolute number of samples is added, except for two samples (having a titer

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Antibody titers in pre-pandemic human plasma samples (N = 496; period 2016-2017). The IPMA titers for antibodies against HCoV-229E, HCoV-OC43, SARS-CoV-2 S and SARS-CoV-2 N of a panel of 496 pre-pandemic plasma samples are given in pie charts (left). For each slice, the absolute number of samples is added, except for two samples (having a titer

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques:

    Antibody titers in sera from 20 hospitalized COVID-19 patients, from day 0 up to day 32 post-symptom onset. For 15 patients (A–O) , SARS-CoV-2 neutralizing antibody titers (SN titer) were determined, together with IPMA-based antibody titers against SARS-CoV-2 N and S, HCoV-OC43 and HCoV-229E. Sera from patients (P–T) were only partially analysed (lower part of the heatmap).

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Antibody titers in sera from 20 hospitalized COVID-19 patients, from day 0 up to day 32 post-symptom onset. For 15 patients (A–O) , SARS-CoV-2 neutralizing antibody titers (SN titer) were determined, together with IPMA-based antibody titers against SARS-CoV-2 N and S, HCoV-OC43 and HCoV-229E. Sera from patients (P–T) were only partially analysed (lower part of the heatmap).

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques:

    Antibody titers in sera from 20 COVID-19 patients across the first four weeks post-symptom onset. Antibody titers based on IPMA for HCoV-229E, HCoV-OC43, SARS-CoV-2 S (S-IPMA) and N (N-IPMA). The boxes extend from the 25th to 75th percentiles, while the whiskers range from the minimum to maximum values. Each individual point is plotted, the line in the middle (when applicable) is the median. Not significant (ns), P > 0.05; ***P ≤ 0.001; ****P ≤ 0.0001 (ordinary one-way ANOVA followed by Tukey’s multiple comparisons test, one week versus the next).

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Antibody titers in sera from 20 COVID-19 patients across the first four weeks post-symptom onset. Antibody titers based on IPMA for HCoV-229E, HCoV-OC43, SARS-CoV-2 S (S-IPMA) and N (N-IPMA). The boxes extend from the 25th to 75th percentiles, while the whiskers range from the minimum to maximum values. Each individual point is plotted, the line in the middle (when applicable) is the median. Not significant (ns), P > 0.05; ***P ≤ 0.001; ****P ≤ 0.0001 (ordinary one-way ANOVA followed by Tukey’s multiple comparisons test, one week versus the next).

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques:

    Pepscan analysis on sera from hospitalized COVID-19 patients. (A) Paired sera from eight hospitalized COVID-19 patients, collected at an early and late time-point post-symptom onset, were analysed by pepscan. Bar graphs show the fold increase in OD 450 nm value versus control peptide PEP74 (colored in salmon). The series of 76 peptides consisted of: 70 overlapping peptides derived from SARS-CoV-2 (PEP1-PEP70 and PEP76); 2 peptides derived from HCoV-OC43 (PEP71 and -78); 2 peptides derived from HCoV-229E (PEP72 and -77); and PEP74: negative control peptide (scrambled). (B) Serum samples from additional time points (ranging from day 0 up to day 32 post-symptom onset) and seven additional hospitalized COVID-19 patients were subjected to pepscan. The fold increase in OD 450 nm value for PEP1-4 (derived from SARS-CoV-2 S), PEP71 (HCoV-OC43 S) and PEP72 (HCoV-229E S) is shown versus negative control peptide PEP74.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Pepscan analysis on sera from hospitalized COVID-19 patients. (A) Paired sera from eight hospitalized COVID-19 patients, collected at an early and late time-point post-symptom onset, were analysed by pepscan. Bar graphs show the fold increase in OD 450 nm value versus control peptide PEP74 (colored in salmon). The series of 76 peptides consisted of: 70 overlapping peptides derived from SARS-CoV-2 (PEP1-PEP70 and PEP76); 2 peptides derived from HCoV-OC43 (PEP71 and -78); 2 peptides derived from HCoV-229E (PEP72 and -77); and PEP74: negative control peptide (scrambled). (B) Serum samples from additional time points (ranging from day 0 up to day 32 post-symptom onset) and seven additional hospitalized COVID-19 patients were subjected to pepscan. The fold increase in OD 450 nm value for PEP1-4 (derived from SARS-CoV-2 S), PEP71 (HCoV-OC43 S) and PEP72 (HCoV-229E S) is shown versus negative control peptide PEP74.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Derivative Assay, Negative Control

    IPMA assay for determination of antibody titers against SARS-CoV-2 S or N, or HCoV-229E, HCoV-OC43 and FeCV. (A) Assay principle and representative images of positive IPMA staining. For SARS-CoV-2, we used PK-15 cells transfected with an expression plasmid for V5-tagged S- or N-protein. For HCoV-229E, HCoV-OC43 and FeCV, we used virus-infected Huh7 cells, HRT-18 cells and feline enterocytes, respectively. Either serum, plasma, pleural fluid, ascites or purified antibody were used as primary antibodies; peroxidase-labelled goat anti-human or rabbit anti-cat IgG were used as secondary antibodies. (B) Staining with commercial antibodies confirmed SARS-CoV-2 N and S expression in transfected PK-15 cells, as evident from strong colocalization of anti-V5 and anti-N staining (top panels); and anti-V5, anti-S1 and anti-S2 staining (bottom panels). (C) Western blot showing proper expression of N and S in the transfected PK-15 cells, with full-length S undergoing S1/S2 cleavage and N -glycosylation, as evident from PGNase F treatment on the cell lysates.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: IPMA assay for determination of antibody titers against SARS-CoV-2 S or N, or HCoV-229E, HCoV-OC43 and FeCV. (A) Assay principle and representative images of positive IPMA staining. For SARS-CoV-2, we used PK-15 cells transfected with an expression plasmid for V5-tagged S- or N-protein. For HCoV-229E, HCoV-OC43 and FeCV, we used virus-infected Huh7 cells, HRT-18 cells and feline enterocytes, respectively. Either serum, plasma, pleural fluid, ascites or purified antibody were used as primary antibodies; peroxidase-labelled goat anti-human or rabbit anti-cat IgG were used as secondary antibodies. (B) Staining with commercial antibodies confirmed SARS-CoV-2 N and S expression in transfected PK-15 cells, as evident from strong colocalization of anti-V5 and anti-N staining (top panels); and anti-V5, anti-S1 and anti-S2 staining (bottom panels). (C) Western blot showing proper expression of N and S in the transfected PK-15 cells, with full-length S undergoing S1/S2 cleavage and N -glycosylation, as evident from PGNase F treatment on the cell lysates.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Staining, Transfection, Expressing, Plasmid Preparation, Infection, Purification, Western Blot

    Virus-neutralizing properties of peptide-purified human antibodies and parent serum 20Hu384. (A) The virus-neutralizing activity was determined by seroneutralization (SN) assay against FeCV in feline enterocytes, HCoV-OC43 in HRT-18 cells, and SARS-CoV-2 in VeroE6 cells. The limit of detection (LOD) was a 1:8 (FeCV) or 1:40 dilution (HCoV-OC43 and SARS-CoV-2). (B, C) Evaluation of the pAbs (starting dilution: 1:2) in a SARS-CoV-2 neutralization assay in Calu-3 cells. (B) Evaluation based on viral load quantification at 24 h p.i. The three right panels show the negative control (elution buffer); parent human serum #20Hu384; and positive control antibody (S1-mAb: SARS-CoV-2 neutralizing anti-S1 antibody). Data are the mean ± SEM of two independent experiments, performed in duplicate. The Y-axis shows the fold reduction in viral RNA versus untreated virus control, based on qRT-PCR analysis of the supernatants at 24 h p.i. *P ≤ 0.05; **P ≤ 0.01; ***P ≤ 0.001, ****P ≤ 0.0001 (multiple unpaired t-test with Holm-Šídák correction; treated sample versus untreated virus control). (C) In parallel, virus replication was quantified by immunofluorescence staining for dsRNA at 72 h p.i. The graphs represent the percentage neutralization in function of antibody dilution or concentration.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Virus-neutralizing properties of peptide-purified human antibodies and parent serum 20Hu384. (A) The virus-neutralizing activity was determined by seroneutralization (SN) assay against FeCV in feline enterocytes, HCoV-OC43 in HRT-18 cells, and SARS-CoV-2 in VeroE6 cells. The limit of detection (LOD) was a 1:8 (FeCV) or 1:40 dilution (HCoV-OC43 and SARS-CoV-2). (B, C) Evaluation of the pAbs (starting dilution: 1:2) in a SARS-CoV-2 neutralization assay in Calu-3 cells. (B) Evaluation based on viral load quantification at 24 h p.i. The three right panels show the negative control (elution buffer); parent human serum #20Hu384; and positive control antibody (S1-mAb: SARS-CoV-2 neutralizing anti-S1 antibody). Data are the mean ± SEM of two independent experiments, performed in duplicate. The Y-axis shows the fold reduction in viral RNA versus untreated virus control, based on qRT-PCR analysis of the supernatants at 24 h p.i. *P ≤ 0.05; **P ≤ 0.01; ***P ≤ 0.001, ****P ≤ 0.0001 (multiple unpaired t-test with Holm-Šídák correction; treated sample versus untreated virus control). (C) In parallel, virus replication was quantified by immunofluorescence staining for dsRNA at 72 h p.i. The graphs represent the percentage neutralization in function of antibody dilution or concentration.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Purification, Activity Assay, Neutralization, Negative Control, Positive Control, Quantitative RT-PCR, Immunofluorescence, Staining, Concentration Assay

    Pepscan analysis on ten pre-pandemic plasma samples. Bar graphs show the fold increase in OD 450 nm value versus control peptide PEP74 (colored in salmon). The series of 76 peptides consisted of: 72 overlapping peptides derived from SARS-CoV-2 (PEP1-PEP70 and PEP76); 2 peptides derived from HCoV-OC43 (PEP71 and -78); 2 peptides derived from HCoV-229E (PEP72 and -77); and PEP74: negative control peptide (scrambled). PEP64 (unspecific binder) was removed for clarity.

    Journal: Frontiers in Immunology

    Article Title: Functional Analysis of Human and Feline Coronavirus Cross-Reactive Antibodies Directed Against the SARS-CoV-2 Fusion Peptide

    doi: 10.3389/fimmu.2021.790415

    Figure Lengend Snippet: Pepscan analysis on ten pre-pandemic plasma samples. Bar graphs show the fold increase in OD 450 nm value versus control peptide PEP74 (colored in salmon). The series of 76 peptides consisted of: 72 overlapping peptides derived from SARS-CoV-2 (PEP1-PEP70 and PEP76); 2 peptides derived from HCoV-OC43 (PEP71 and -78); 2 peptides derived from HCoV-229E (PEP72 and -77); and PEP74: negative control peptide (scrambled). PEP64 (unspecific binder) was removed for clarity.

    Article Snippet: Commercial antibodies anti-S2 (Sino Biological, 40590-D001) and REGN10987 (kindly donated by PharmAbs, KU Leuven) were included as controls.

    Techniques: Derivative Assay, Negative Control

    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