de-identified serum samples from 40 individuals with sars-cov-2 infections and 10 healthy donors Search Results


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Figure 3. Syncytia formation, cell surface expression, and S processing of Omicron XBB.1.5, CH.1.1, and CA.3.1 subvariants (A and B) Syncytia-forming activity. HEK293T-ACE2 cells were co-transfected with Omicron subvariant S proteins and GFP and incubated for 30 h before (A) imaging and (B) quantifying syncytia. D614G and no S serve as positive and negative controls, respectively. Comparisons in the extent of syncytia for each variant were made against D614G, with p values indicating statistical significance. Similar results were obtained by using CaLu3 cell as target (see data in Figure S4). (C and D) Cell surface expression of S proteins. HEK293T cells used for production of pseudotyped lentiviral vectors bearing S proteins (Figures 1 and 2) from Omicron subvariants were fixed and surface stained for S with an anti-S1 specific antibody <t>T62</t> followed by flow cytometric analyses. (C) Histogram plots of anti- S1 signals in transfected cells and (D) calculated relative mean fluorescence intensities of each subvariant by setting the value of D614G as 1. (E) S expression and processing. HEK293T cells used to produce pseudotyped vectors were lysed and probed with anti-S1, anti-S2, anti-GAPDH (loading control), or anti-p24 (HIV capsid, transfection control) antibodies; the signal for anti-GAPDH was from reblotting the membrane of anti-S1, and the signal for anti- S2 was from reblotting the membrane of anti-p24. S processing was quantified using NIH ImageJ used to determine an S1/S or S2/S ratio and normalized to D614G (D614G = 1.0). Bars in (B) and (D) represent means ± standard error. Dots represent three biological replicates from one typical experiment. Significance relative to D614G was determined using a one-way repeated measures ANOVA with Bonferroni’s multiple testing correction (n = 3). p values are displayed as ns p > 0.05 and ****p < 0.0001.
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Figure 3. Syncytia formation, cell surface expression, and S processing of Omicron XBB.1.5, CH.1.1, and CA.3.1 subvariants (A and B) Syncytia-forming activity. HEK293T-ACE2 cells were co-transfected with Omicron subvariant S proteins and GFP and incubated for 30 h before (A) imaging and (B) quantifying syncytia. D614G and no S serve as positive and negative controls, respectively. Comparisons in the extent of syncytia for each variant were made against D614G, with p values indicating statistical significance. Similar results were obtained by using CaLu3 cell as target (see data in Figure S4). (C and D) Cell surface expression of S proteins. HEK293T cells used for production of pseudotyped lentiviral vectors bearing S proteins (Figures 1 and 2) from Omicron subvariants were fixed and surface stained for S with an anti-S1 specific antibody <t>T62</t> followed by flow cytometric analyses. (C) Histogram plots of anti- S1 signals in transfected cells and (D) calculated relative mean fluorescence intensities of each subvariant by setting the value of D614G as 1. (E) S expression and processing. HEK293T cells used to produce pseudotyped vectors were lysed and probed with anti-S1, anti-S2, anti-GAPDH (loading control), or anti-p24 (HIV capsid, transfection control) antibodies; the signal for anti-GAPDH was from reblotting the membrane of anti-S1, and the signal for anti- S2 was from reblotting the membrane of anti-p24. S processing was quantified using NIH ImageJ used to determine an S1/S or S2/S ratio and normalized to D614G (D614G = 1.0). Bars in (B) and (D) represent means ± standard error. Dots represent three biological replicates from one typical experiment. Significance relative to D614G was determined using a one-way repeated measures ANOVA with Bonferroni’s multiple testing correction (n = 3). p values are displayed as ns p > 0.05 and ****p < 0.0001.
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Figure 3. Syncytia formation, cell surface expression, and S processing of Omicron XBB.1.5, CH.1.1, and CA.3.1 subvariants (A and B) Syncytia-forming activity. HEK293T-ACE2 cells were co-transfected with Omicron subvariant S proteins and GFP and incubated for 30 h before (A) imaging and (B) quantifying syncytia. D614G and no S serve as positive and negative controls, respectively. Comparisons in the extent of syncytia for each variant were made against D614G, with p values indicating statistical significance. Similar results were obtained by using CaLu3 cell as target (see data in Figure S4). (C and D) Cell surface expression of S proteins. HEK293T cells used for production of pseudotyped lentiviral vectors bearing S proteins (Figures 1 and 2) from Omicron subvariants were fixed and surface stained for S with an anti-S1 specific antibody <t>T62</t> followed by flow cytometric analyses. (C) Histogram plots of anti- S1 signals in transfected cells and (D) calculated relative mean fluorescence intensities of each subvariant by setting the value of D614G as 1. (E) S expression and processing. HEK293T cells used to produce pseudotyped vectors were lysed and probed with anti-S1, anti-S2, anti-GAPDH (loading control), or anti-p24 (HIV capsid, transfection control) antibodies; the signal for anti-GAPDH was from reblotting the membrane of anti-S1, and the signal for anti- S2 was from reblotting the membrane of anti-p24. S processing was quantified using NIH ImageJ used to determine an S1/S or S2/S ratio and normalized to D614G (D614G = 1.0). Bars in (B) and (D) represent means ± standard error. Dots represent three biological replicates from one typical experiment. Significance relative to D614G was determined using a one-way repeated measures ANOVA with Bonferroni’s multiple testing correction (n = 3). p values are displayed as ns p > 0.05 and ****p < 0.0001.
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Figure 3. Syncytia formation, cell surface expression, and S processing of Omicron XBB.1.5, CH.1.1, and CA.3.1 subvariants (A and B) Syncytia-forming activity. HEK293T-ACE2 cells were co-transfected with Omicron subvariant S proteins and GFP and incubated for 30 h before (A) imaging and (B) quantifying syncytia. D614G and no S serve as positive and negative controls, respectively. Comparisons in the extent of syncytia for each variant were made against D614G, with p values indicating statistical significance. Similar results were obtained by using CaLu3 cell as target (see data in Figure S4). (C and D) Cell surface expression of S proteins. HEK293T cells used for production of pseudotyped lentiviral vectors bearing S proteins (Figures 1 and 2) from Omicron subvariants were fixed and surface stained for S with an anti-S1 specific antibody <t>T62</t> followed by flow cytometric analyses. (C) Histogram plots of anti- S1 signals in transfected cells and (D) calculated relative mean fluorescence intensities of each subvariant by setting the value of D614G as 1. (E) S expression and processing. HEK293T cells used to produce pseudotyped vectors were lysed and probed with anti-S1, anti-S2, anti-GAPDH (loading control), or anti-p24 (HIV capsid, transfection control) antibodies; the signal for anti-GAPDH was from reblotting the membrane of anti-S1, and the signal for anti- S2 was from reblotting the membrane of anti-p24. S processing was quantified using NIH ImageJ used to determine an S1/S or S2/S ratio and normalized to D614G (D614G = 1.0). Bars in (B) and (D) represent means ± standard error. Dots represent three biological replicates from one typical experiment. Significance relative to D614G was determined using a one-way repeated measures ANOVA with Bonferroni’s multiple testing correction (n = 3). p values are displayed as ns p > 0.05 and ****p < 0.0001.
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Image Search Results


Figure 3. Syncytia formation, cell surface expression, and S processing of Omicron XBB.1.5, CH.1.1, and CA.3.1 subvariants (A and B) Syncytia-forming activity. HEK293T-ACE2 cells were co-transfected with Omicron subvariant S proteins and GFP and incubated for 30 h before (A) imaging and (B) quantifying syncytia. D614G and no S serve as positive and negative controls, respectively. Comparisons in the extent of syncytia for each variant were made against D614G, with p values indicating statistical significance. Similar results were obtained by using CaLu3 cell as target (see data in Figure S4). (C and D) Cell surface expression of S proteins. HEK293T cells used for production of pseudotyped lentiviral vectors bearing S proteins (Figures 1 and 2) from Omicron subvariants were fixed and surface stained for S with an anti-S1 specific antibody T62 followed by flow cytometric analyses. (C) Histogram plots of anti- S1 signals in transfected cells and (D) calculated relative mean fluorescence intensities of each subvariant by setting the value of D614G as 1. (E) S expression and processing. HEK293T cells used to produce pseudotyped vectors were lysed and probed with anti-S1, anti-S2, anti-GAPDH (loading control), or anti-p24 (HIV capsid, transfection control) antibodies; the signal for anti-GAPDH was from reblotting the membrane of anti-S1, and the signal for anti- S2 was from reblotting the membrane of anti-p24. S processing was quantified using NIH ImageJ used to determine an S1/S or S2/S ratio and normalized to D614G (D614G = 1.0). Bars in (B) and (D) represent means ± standard error. Dots represent three biological replicates from one typical experiment. Significance relative to D614G was determined using a one-way repeated measures ANOVA with Bonferroni’s multiple testing correction (n = 3). p values are displayed as ns p > 0.05 and ****p < 0.0001.

Journal: Cell reports

Article Title: Enhanced evasion of neutralizing antibody response by Omicron XBB.1.5, CH.1.1, and CA.3.1 variants.

doi: 10.1016/j.celrep.2023.112443

Figure Lengend Snippet: Figure 3. Syncytia formation, cell surface expression, and S processing of Omicron XBB.1.5, CH.1.1, and CA.3.1 subvariants (A and B) Syncytia-forming activity. HEK293T-ACE2 cells were co-transfected with Omicron subvariant S proteins and GFP and incubated for 30 h before (A) imaging and (B) quantifying syncytia. D614G and no S serve as positive and negative controls, respectively. Comparisons in the extent of syncytia for each variant were made against D614G, with p values indicating statistical significance. Similar results were obtained by using CaLu3 cell as target (see data in Figure S4). (C and D) Cell surface expression of S proteins. HEK293T cells used for production of pseudotyped lentiviral vectors bearing S proteins (Figures 1 and 2) from Omicron subvariants were fixed and surface stained for S with an anti-S1 specific antibody T62 followed by flow cytometric analyses. (C) Histogram plots of anti- S1 signals in transfected cells and (D) calculated relative mean fluorescence intensities of each subvariant by setting the value of D614G as 1. (E) S expression and processing. HEK293T cells used to produce pseudotyped vectors were lysed and probed with anti-S1, anti-S2, anti-GAPDH (loading control), or anti-p24 (HIV capsid, transfection control) antibodies; the signal for anti-GAPDH was from reblotting the membrane of anti-S1, and the signal for anti- S2 was from reblotting the membrane of anti-p24. S processing was quantified using NIH ImageJ used to determine an S1/S or S2/S ratio and normalized to D614G (D614G = 1.0). Bars in (B) and (D) represent means ± standard error. Dots represent three biological replicates from one typical experiment. Significance relative to D614G was determined using a one-way repeated measures ANOVA with Bonferroni’s multiple testing correction (n = 3). p values are displayed as ns p > 0.05 and ****p < 0.0001.

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies anti-SARS-CoV-2 S1 Sino Biological Cat# 40150-T62; RRID:AB_2920715 anti-SARS-CoV-2 S2 Sino Biological Cat# 40590-T62; RRID: AB_2857932 anti-p24 NIH Cat# ARP-1513; RRID: AB_2832923 anti-GAPDH Santa Cruz Biotechnology Cat# sc-47724; RRID: AB_627678 S309 mAb Pinto et al.39 N/A anti-Mouse IgG (whole molecule)–Peroxidase Sigma-Aldrich Cat# A5278; RRID: AB_258232 anti-Rabbit IgG (whole molecule)–Peroxidase Sigma-Aldrich Cat# A9169; RRID: AB_258434 anti-Rabbit IgG (whole molecule)–FITC antibody Sigma-Aldrich Cat# F9887; RRID: AB_259816 Biological samples 3-dose HCWs Sera Evans et al.9, Qu et al.14 N/A 3-dose Bivalent HCWs Sera This paper N/A Omicron BA.4/5-wave Infected First Responders and Household Contacts Sera Qu et al.17 N/A Chemicals, peptides, and recombinant proteins Transporter 5 Transfection Reagent Polysciences Cat# 26008-5 Dulbecco’s Modified Eagles Medium (DMEM) Sigma-Aldrich Cat#: 11965-092 Fetal Bovine Serum (FBS) Thermo Fisher Scientific Cat#: F1051 0.05% Trypsin + 0.53 mM EDTA Corning Cat# 25-052-CI Penicillin-Streptomycin HyClone Cat#: SV30010 QIAprep Spin Miniprep Kit QIAGEN Cat# 27106 Coelenterazine GoldBio Cat#: CZ2.5, CAS: 55779-48-1 Deposited data NT50 Values and De-identified patient data SeroNet Coordinating Center, NCI, NIH N/A Experimental models: Cell lines HEK293T ATCC Cat#: CRL-11268; RRID: CVCL_1926 HEK293T-ACE2 BEI Resources Cat#: NR-52511; RRID: CVCL_A7UK Calu-3 ATCC RRID: CVCL_0609 Recombinant DNA pNL4-3-inGluc David Derse, NIH47 N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_D614G GenScript Biotech48 N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_BA.2 GenScript Biotech9 N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_BA.4/5 GenScript Biotech9 N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_BA.2.75.2 GenScript Biotech15 N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_BA.2.75.2-N1199D GenScript Biotech15 N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_BQ.1.1 GenScript Biotech15 pcDNA3.1-SARS-CoV-2-Flag-S-Flag_XBB This paper N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_XBB.1 This paper N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_XBB-S486P This paper N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_XBB.1.5 This paper N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_CH.1.1 This paper N/A pcDNA3.1-SARS-CoV-2-Flag-S-Flag_CA.3.1 This paper N/A (Continued on next page) Cell Reports 42, 112443, May 30, 2023 11

Techniques: Expressing, Activity Assay, Transfection, Incubation, Imaging, Variant Assay, Staining, Control, Membrane