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a549 hace2 tmprss2 (InvivoGen)

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Brand: InvivoGen
Rating: 96 (194 reviews)

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InvivoGen a549 hace2 tmprss2

Susceptibility of the nine different SARS-CoV-2 strains to inhibitors of <t>TMPRSS2-mediated</t> fusion and cathepsin-mediated endocytosis. SARS-CoV-2 European wild-type (B.1.1), variant-of-concern (VOC) Alpha (B1.1.7 Q27*K68*, B.1.1.7 Q27*), Delta (AY.33), and Omicron (BA.1.17.2, BA.1.1, BA.2.9, BE.1.1, BA.5.1) were propagated in four human cell lines (Calu-3, Caco-2, <t>A549</t> <t>hACE2+/TMPRSS2+</t> , HEK293T) in the presence of increasing concentrations (0.024-100 µM) of camostat, an inhibitor of TMPRSS2-mediated viral direct fusion with cellular membrane (green curve), aloxistatin, an inhibitor of cathepsin-mediated viral endocytic uptake (pink curve), and a 1:1 mixture of both inhibitors (black curve). Viral load was determined in cell culture supernatants 48h p.i. using RT-qPCR and are presented as log 10 RNA copies/ml. Controls included cells infected with SARS-CoV-2 in the absence of inhibitors (“virus control”, VC), and cells fixed with 4% paraformaldehyde and exposed to SARS-CoV-2 (“background control”, BG), shown as dashed horizontal lines. Data show mean and standard error of three independent experiments.

A549 Hace2 Tmprss2, supplied by InvivoGen, used in various techniques. Bioz Stars score: 96/100, based on 194 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "SARS-CoV-2 evolution enhances endocytic uptake while preserving TMPRSS2-dependent fusion"

Article Title: SARS-CoV-2 evolution enhances endocytic uptake while preserving TMPRSS2-dependent fusion

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2025.1736891

Susceptibility of the nine different SARS-CoV-2 strains to inhibitors of TMPRSS2-mediated fusion and cathepsin-mediated endocytosis. SARS-CoV-2 European wild-type (B.1.1), variant-of-concern (VOC) Alpha (B1.1.7 Q27*K68*, B.1.1.7 Q27*), Delta (AY.33), and Omicron (BA.1.17.2, BA.1.1, BA.2.9, BE.1.1, BA.5.1) were propagated in four human cell lines (Calu-3, Caco-2, A549 hACE2+/TMPRSS2+ , HEK293T) in the presence of increasing concentrations (0.024-100 µM) of camostat, an inhibitor of TMPRSS2-mediated viral direct fusion with cellular membrane (green curve), aloxistatin, an inhibitor of cathepsin-mediated viral endocytic uptake (pink curve), and a 1:1 mixture of both inhibitors (black curve). Viral load was determined in cell culture supernatants 48h p.i. using RT-qPCR and are presented as log 10 RNA copies/ml. Controls included cells infected with SARS-CoV-2 in the absence of inhibitors (“virus control”, VC), and cells fixed with 4% paraformaldehyde and exposed to SARS-CoV-2 (“background control”, BG), shown as dashed horizontal lines. Data show mean and standard error of three independent experiments.

Figure Legend Snippet: Susceptibility of the nine different SARS-CoV-2 strains to inhibitors of TMPRSS2-mediated fusion and cathepsin-mediated endocytosis. SARS-CoV-2 European wild-type (B.1.1), variant-of-concern (VOC) Alpha (B1.1.7 Q27*K68*, B.1.1.7 Q27*), Delta (AY.33), and Omicron (BA.1.17.2, BA.1.1, BA.2.9, BE.1.1, BA.5.1) were propagated in four human cell lines (Calu-3, Caco-2, A549 hACE2+/TMPRSS2+ , HEK293T) in the presence of increasing concentrations (0.024-100 µM) of camostat, an inhibitor of TMPRSS2-mediated viral direct fusion with cellular membrane (green curve), aloxistatin, an inhibitor of cathepsin-mediated viral endocytic uptake (pink curve), and a 1:1 mixture of both inhibitors (black curve). Viral load was determined in cell culture supernatants 48h p.i. using RT-qPCR and are presented as log 10 RNA copies/ml. Controls included cells infected with SARS-CoV-2 in the absence of inhibitors (“virus control”, VC), and cells fixed with 4% paraformaldehyde and exposed to SARS-CoV-2 (“background control”, BG), shown as dashed horizontal lines. Data show mean and standard error of three independent experiments.

Techniques Used: Variant Assay, Membrane, Cell Culture, Quantitative RT-PCR, Infection, Virus, Control

Degree of direct TMRPSS2-mediated fusion and cathepsin-mediated endocytic uptake of the nine different SARS-CoV-2 strains in four different cell lines. Calculation of the reduction in viral load induced by aloxistatin (pink columns) and camostat (green columns) at the non-toxic concentration of 25 µM as % inhibition induced by the mixture of the two inhibitors for Calu-3 cells (A) , HEK293T cells (B) , Caco-2 cells (C) and A549 hACE2+/TMPRSS2+ cells (D) . A higher percentage indicates a stronger role of the respective mode of entry for the respective virus strain. In A549 hACE2+/TMPRSS2+ cells, strains BA.1.17.2 and BA.1.1 were non-replicative (n.r.). In HEK293T cells, virus replication was observed for strains BE.1.1 and BA.5.1 only. Statistics was performed using two-way ANOVA with Šidák’s correction to account for multiple comparisons. *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001.

Figure Legend Snippet: Degree of direct TMRPSS2-mediated fusion and cathepsin-mediated endocytic uptake of the nine different SARS-CoV-2 strains in four different cell lines. Calculation of the reduction in viral load induced by aloxistatin (pink columns) and camostat (green columns) at the non-toxic concentration of 25 µM as % inhibition induced by the mixture of the two inhibitors for Calu-3 cells (A) , HEK293T cells (B) , Caco-2 cells (C) and A549 hACE2+/TMPRSS2+ cells (D) . A higher percentage indicates a stronger role of the respective mode of entry for the respective virus strain. In A549 hACE2+/TMPRSS2+ cells, strains BA.1.17.2 and BA.1.1 were non-replicative (n.r.). In HEK293T cells, virus replication was observed for strains BE.1.1 and BA.5.1 only. Statistics was performed using two-way ANOVA with Šidák’s correction to account for multiple comparisons. *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001.

Techniques Used: Concentration Assay, Inhibition, Virus

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Journal: Frontiers in Immunology

Article Title: SARS-CoV-2 evolution enhances endocytic uptake while preserving TMPRSS2-dependent fusion

doi: 10.3389/fimmu.2025.1736891

Figure Lengend Snippet: Susceptibility of the nine different SARS-CoV-2 strains to inhibitors of TMPRSS2-mediated fusion and cathepsin-mediated endocytosis. SARS-CoV-2 European wild-type (B.1.1), variant-of-concern (VOC) Alpha (B1.1.7 Q27*K68*, B.1.1.7 Q27*), Delta (AY.33), and Omicron (BA.1.17.2, BA.1.1, BA.2.9, BE.1.1, BA.5.1) were propagated in four human cell lines (Calu-3, Caco-2, A549 hACE2+/TMPRSS2+ , HEK293T) in the presence of increasing concentrations (0.024-100 µM) of camostat, an inhibitor of TMPRSS2-mediated viral direct fusion with cellular membrane (green curve), aloxistatin, an inhibitor of cathepsin-mediated viral endocytic uptake (pink curve), and a 1:1 mixture of both inhibitors (black curve). Viral load was determined in cell culture supernatants 48h p.i. using RT-qPCR and are presented as log 10 RNA copies/ml. Controls included cells infected with SARS-CoV-2 in the absence of inhibitors (“virus control”, VC), and cells fixed with 4% paraformaldehyde and exposed to SARS-CoV-2 (“background control”, BG), shown as dashed horizontal lines. Data show mean and standard error of three independent experiments.

Article Snippet: SARS-CoV-2 strains were propagated in human Calu-3, Caco-2 (CLS Cell Lines Service, Eppelheim, Germany), A549 hACE2+/TMPRSS2+ (InvivoGen, San Diego, US), and HEK293T cell lines using DMEM (Gibco, Waltham, MA) supplemented with 1% streptomycin/penicillin and 10% fetal calf serum (Pan Biotech, Aidenbach, Germany).

Techniques: Variant Assay, Membrane, Cell Culture, Quantitative RT-PCR, Infection, Virus, Control

Journal: Frontiers in Immunology

Article Title: SARS-CoV-2 evolution enhances endocytic uptake while preserving TMPRSS2-dependent fusion

doi: 10.3389/fimmu.2025.1736891

Figure Lengend Snippet: Degree of direct TMRPSS2-mediated fusion and cathepsin-mediated endocytic uptake of the nine different SARS-CoV-2 strains in four different cell lines. Calculation of the reduction in viral load induced by aloxistatin (pink columns) and camostat (green columns) at the non-toxic concentration of 25 µM as % inhibition induced by the mixture of the two inhibitors for Calu-3 cells (A) , HEK293T cells (B) , Caco-2 cells (C) and A549 hACE2+/TMPRSS2+ cells (D) . A higher percentage indicates a stronger role of the respective mode of entry for the respective virus strain. In A549 hACE2+/TMPRSS2+ cells, strains BA.1.17.2 and BA.1.1 were non-replicative (n.r.). In HEK293T cells, virus replication was observed for strains BE.1.1 and BA.5.1 only. Statistics was performed using two-way ANOVA with Šidák’s correction to account for multiple comparisons. *p<0.05, **p<0.01, ***p<0.001, ****p<0.0001.

Techniques: Concentration Assay, Inhibition, Virus

Evaluation of the antiviral activity and toxicity of different compounds of our in-house collection against VSV pseudotyped with BA.2 (A) and BA.4/5 S (B) proteins. VSV pseudotyped with the indicated S proteins was preincubated with the different compounds at 20 μM, followed by the infection of A549-ACE2-TMPRSS2 cells. Viral infection was monitored by counting GFP-expressing cells. Toxicity was assessed via the analysis of cell confluency. Bars indicate the mean and SE for n = 3. Individual data points are shown as circles.

Journal: ACS Omega

Article Title: A Tetrapodal Tryptophan Derivative with Multiple Exposed Free Carboxylic Acids Blocks Host Cell Entry of Omicron SARS-Cov-2 and Respiratory Syncytial Virus

doi: 10.1021/acsomega.5c10442

Figure Lengend Snippet: Evaluation of the antiviral activity and toxicity of different compounds of our in-house collection against VSV pseudotyped with BA.2 (A) and BA.4/5 S (B) proteins. VSV pseudotyped with the indicated S proteins was preincubated with the different compounds at 20 μM, followed by the infection of A549-ACE2-TMPRSS2 cells. Viral infection was monitored by counting GFP-expressing cells. Toxicity was assessed via the analysis of cell confluency. Bars indicate the mean and SE for n = 3. Individual data points are shown as circles.

Article Snippet: A549-ACE2-TMPRSS2 cells (catalog a549-hace2tpsa) were purchased from InVivoGen.

Techniques: Activity Assay, Infection, Expressing

Compound 2 blocks the entry of RSV into cells. Time-of-addition experiment with 2 treatment at 4 μM prior to and during infection ( Preincubation and Pre - + Post-incubation ) or following infection ( Post-incubation ) of A549 cells with RSV-A encoding the fluorescent protein mKate2 (see ). Viral infection was quantified at 24 h post infection by examination of mKate2 fluorescence.

Journal: ACS Omega

Article Title: A Tetrapodal Tryptophan Derivative with Multiple Exposed Free Carboxylic Acids Blocks Host Cell Entry of Omicron SARS-Cov-2 and Respiratory Syncytial Virus

doi: 10.1021/acsomega.5c10442

Figure Lengend Snippet: Compound 2 blocks the entry of RSV into cells. Time-of-addition experiment with 2 treatment at 4 μM prior to and during infection ( Preincubation and Pre - + Post-incubation ) or following infection ( Post-incubation ) of A549 cells with RSV-A encoding the fluorescent protein mKate2 (see ). Viral infection was quantified at 24 h post infection by examination of mKate2 fluorescence.

Article Snippet: A549-ACE2-TMPRSS2 cells (catalog a549-hace2tpsa) were purchased from InVivoGen.

Techniques: Infection, Incubation, Fluorescence

rH234A exhibited impaired replication in human lung-derived epithelial cells. ( A and B ) A549-AT cells were infected with rWT or rH234A at 0.1 and 1 MOI. The culture supernatants were collected for extracellular viral titration ( A ). Whole cell lysates were collected for RNA extraction and subsequent quantification of viral N mRNA level ( B ). Data in A and B were shown as mean ± SD ( n = 3), and data in B were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. **, P < 0.01; ***, P < 0.001. ( C ) Western blotting of viral N protein in A549-AT cells (0.1 MOI). β-Actin was served as a loading control. ( D−F ) Growth curves of rWT and rH234A in A549-A (0.1 or 5 MOI) or Calu-3 cells (0.1 MOI). Data in this figure are representative of at least two independent experiments. Data in D−F are shown as mean ± SD ( n = 3).

Journal: Journal of Virology

Article Title: SARS-CoV-2 Nsp15 endoribonuclease subverts host defenses to enhance viral fitness in lung cells

doi: 10.1128/jvi.01175-25

Figure Lengend Snippet: rH234A exhibited impaired replication in human lung-derived epithelial cells. ( A and B ) A549-AT cells were infected with rWT or rH234A at 0.1 and 1 MOI. The culture supernatants were collected for extracellular viral titration ( A ). Whole cell lysates were collected for RNA extraction and subsequent quantification of viral N mRNA level ( B ). Data in A and B were shown as mean ± SD ( n = 3), and data in B were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. **, P < 0.01; ***, P < 0.001. ( C ) Western blotting of viral N protein in A549-AT cells (0.1 MOI). β-Actin was served as a loading control. ( D−F ) Growth curves of rWT and rH234A in A549-A (0.1 or 5 MOI) or Calu-3 cells (0.1 MOI). Data in this figure are representative of at least two independent experiments. Data in D−F are shown as mean ± SD ( n = 3).

Article Snippet: A Caco2 cell line expressing hACE2 and hTMPRSS2 (Caco2-AT) and an A549 cell line expressing hACE2 and hTMPRSS2 (A549-AT), gifts from Dr. Mohsan Saeed (Boston University), were cultured in DMEM with 10% FBS, 1× Pen/Strep, 1 μg/mL puromycin, and 1 μg/mL blasticidin (InvivoGen, ant-bl-05).

Techniques: Derivative Assay, Infection, Titration, RNA Extraction, Comparison, Western Blot, Control

rH234A exhibited impaired replication in primary human lung epithelial cells. ( A ) Schematic diagram of HBEC differentiation. ( B and C ) Differentiated HBECs in Transwell inserts were inoculated with rWT or rH234A at 0.1 MOI. ( B ) The apical mucus layers were collected for viral titration, and ( C ) the cells on the membrane were harvested for viral N mRNA quantification. ( D ) Schematic diagram of alveolar type 2 organoids induction and differentiation. ( E and F ) AT2 organoids grown in Matrigel were inoculated with rWT or rH234A at 0.1 MOI. ( E ) The culture Matrigel content was collected for viral titration. ( F ) The organoids were harvested for viral N mRNA quantification. Data in this figure are representative of two independent experiments and shown as mean ± SD ( n = 3). Data in C and F were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. *, P < 0.05; **, P < 0.01. The images in A and D were prepared using Biorender.com .

Journal: Journal of Virology

Article Title: SARS-CoV-2 Nsp15 endoribonuclease subverts host defenses to enhance viral fitness in lung cells

doi: 10.1128/jvi.01175-25

Figure Lengend Snippet: rH234A exhibited impaired replication in primary human lung epithelial cells. ( A ) Schematic diagram of HBEC differentiation. ( B and C ) Differentiated HBECs in Transwell inserts were inoculated with rWT or rH234A at 0.1 MOI. ( B ) The apical mucus layers were collected for viral titration, and ( C ) the cells on the membrane were harvested for viral N mRNA quantification. ( D ) Schematic diagram of alveolar type 2 organoids induction and differentiation. ( E and F ) AT2 organoids grown in Matrigel were inoculated with rWT or rH234A at 0.1 MOI. ( E ) The culture Matrigel content was collected for viral titration. ( F ) The organoids were harvested for viral N mRNA quantification. Data in this figure are representative of two independent experiments and shown as mean ± SD ( n = 3). Data in C and F were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. *, P < 0.05; **, P < 0.01. The images in A and D were prepared using Biorender.com .

Techniques: Titration, Membrane, Comparison

SARS-CoV-2 Nsp15 antagonizes type I and III IFN activation. ( A ) Quantification of IFN- β, IFN- λ 3 , ISG56 mRNA, and viral N gene in A549-A cells infected with 5 MOI of rWT or rH234A by RT-qPCR. ( B ) Immunoblotting phosphorylated Stat1 (p-Stat1), total Stat1 (t-Stat1), viral N protein (N pro), and β-actin of A549-A cells infected with 5 MOI of rWT or rH234A. ( C ) RT-qPCR quantification of IFN- β, IFN- λ 3 , ISG56 mRNA, and viral N gene in Calu-3 cells infected with 1 MOI of rWT or rH234A. ( D ) RT-qPCR quantification of IFN- β, IFN- λ 3 , ISG56 mRNA, and viral N gene in Caco2-AT cells infected with 0.1 MOI of rWT or rH234A. Data in A , C , and D are shown as mean ± SD ( n = 3) and were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. Data in this figure are representative of at least two independent experiments. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Journal: Journal of Virology

Article Title: SARS-CoV-2 Nsp15 endoribonuclease subverts host defenses to enhance viral fitness in lung cells

doi: 10.1128/jvi.01175-25

Figure Lengend Snippet: SARS-CoV-2 Nsp15 antagonizes type I and III IFN activation. ( A ) Quantification of IFN- β, IFN- λ 3 , ISG56 mRNA, and viral N gene in A549-A cells infected with 5 MOI of rWT or rH234A by RT-qPCR. ( B ) Immunoblotting phosphorylated Stat1 (p-Stat1), total Stat1 (t-Stat1), viral N protein (N pro), and β-actin of A549-A cells infected with 5 MOI of rWT or rH234A. ( C ) RT-qPCR quantification of IFN- β, IFN- λ 3 , ISG56 mRNA, and viral N gene in Calu-3 cells infected with 1 MOI of rWT or rH234A. ( D ) RT-qPCR quantification of IFN- β, IFN- λ 3 , ISG56 mRNA, and viral N gene in Caco2-AT cells infected with 0.1 MOI of rWT or rH234A. Data in A , C , and D are shown as mean ± SD ( n = 3) and were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. Data in this figure are representative of at least two independent experiments. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Techniques: Activation Assay, Infection, Quantitative RT-PCR, Western Blot, Comparison

The H14 and W332 residues are important for Nsp15-mediated IFN antagonism. ( A ) Growth kinetic curves of recombinant viruses in Vero-AT cells (0.01 MOI). ( B ) Growth curves (left) and titer fold difference (right) of recombinant viruses in A549-A cells (0.1 MOI) (right). ( C ) RT-qPCR quantification of IFN- β, IFN- λ 1 , and ISG56 mRNA in Caco2-AT cells infected with 0.1 MOI of indicated recombinant virus. Data in A and B are representative of at least two independent experiments and are shown as mean ± SD ( n = 3-6). Data in C are the pooled results of two independent experiments, shown as mean ± SD ( n = 4-6), and were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Journal: Journal of Virology

Article Title: SARS-CoV-2 Nsp15 endoribonuclease subverts host defenses to enhance viral fitness in lung cells

doi: 10.1128/jvi.01175-25

Figure Lengend Snippet: The H14 and W332 residues are important for Nsp15-mediated IFN antagonism. ( A ) Growth kinetic curves of recombinant viruses in Vero-AT cells (0.01 MOI). ( B ) Growth curves (left) and titer fold difference (right) of recombinant viruses in A549-A cells (0.1 MOI) (right). ( C ) RT-qPCR quantification of IFN- β, IFN- λ 1 , and ISG56 mRNA in Caco2-AT cells infected with 0.1 MOI of indicated recombinant virus. Data in A and B are representative of at least two independent experiments and are shown as mean ± SD ( n = 3-6). Data in C are the pooled results of two independent experiments, shown as mean ± SD ( n = 4-6), and were analyzed with a two-way analysis of variance Tukey’s multiple comparison test. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Techniques: Recombinant, Quantitative RT-PCR, Infection, Virus, Comparison

rH234A infection differentially promotes the nuclear trafficking of PABPC1. ( A ) RNA integrity analysis of A549-A cells infected with rWT or rH234A at 5 MOI. The cells were harvested at indicated times for whole RNA extraction and subsequent TapeStation analysis. ( B ) The RIN of the total RNA collected in A . ( C ) Immunofluorescence assay (IFA) of viral dsRNA and host PABPC1 protein. A549-A cells were infected with rWT or rH234A at 5 MOI and fixed at 24 HPI. Viral dsRNA and host PABPC1 protein were probed with specific antibodies, and the nucleus was stained with Hoechst 33342. Infected cells with or without PABPC1 nuclear translocation are indicated with yellow- and white-color arrows, respectively. Scale bar: 20 µM. ( D ) Quantification of PABPC1 nuclear localization in virus-infected cells from 14 to 15 views of IFA slides. Data are shown as mean ± SEM ( n = 14-15) and analyzed using unpaired t -test with Welch’s correction. Data in the figure are representative of at least two independent experiments.

Journal: Journal of Virology

Article Title: SARS-CoV-2 Nsp15 endoribonuclease subverts host defenses to enhance viral fitness in lung cells

doi: 10.1128/jvi.01175-25

Figure Lengend Snippet: rH234A infection differentially promotes the nuclear trafficking of PABPC1. ( A ) RNA integrity analysis of A549-A cells infected with rWT or rH234A at 5 MOI. The cells were harvested at indicated times for whole RNA extraction and subsequent TapeStation analysis. ( B ) The RIN of the total RNA collected in A . ( C ) Immunofluorescence assay (IFA) of viral dsRNA and host PABPC1 protein. A549-A cells were infected with rWT or rH234A at 5 MOI and fixed at 24 HPI. Viral dsRNA and host PABPC1 protein were probed with specific antibodies, and the nucleus was stained with Hoechst 33342. Infected cells with or without PABPC1 nuclear translocation are indicated with yellow- and white-color arrows, respectively. Scale bar: 20 µM. ( D ) Quantification of PABPC1 nuclear localization in virus-infected cells from 14 to 15 views of IFA slides. Data are shown as mean ± SEM ( n = 14-15) and analyzed using unpaired t -test with Welch’s correction. Data in the figure are representative of at least two independent experiments.

Techniques: Infection, RNA Extraction, Immunofluorescence, Staining, Translocation Assay, Virus

Journal: Journal of Virology

Article Title: SARS-CoV-2 Nsp15 endoribonuclease subverts host defenses to enhance viral fitness in lung cells

doi: 10.1128/jvi.01175-25

Figure Lengend Snippet: rH234A infection does not trigger stress granule formation in human lung cells. ( A ) Immunoblotting p-PKR, t-PKR, p-eIF2α, t-eIF2α, and β-actin of A549-A cells infected with 5 MOI of either rWT or rH234A and harvested at the indicated HPIs. The band intensities were measured with ImageJ. The relative protein levels were calculated as the band intensity relative to β-actin compared to the mock groups. ( B ) Immunofluorescence assay of viral N protein (N pro, red) and host G3BP1 protein (green). A549-A cells were cultured with 2% fetal calf serum media (Starvation) or infected with rWT or rH234A at 5 MOI and fixed at 24 HPI. The N protein and G3BP1 were detected with specific antibodies, and the nucleus was stained with Hoechst 33342. Scale bar: 20 µM. ( C ) Some cells in B show colocalization of the N protein and G3BP1. The RGB profile shows the fluorescent intensity signals of the N protein and G3BP1. Scale bar: 20 µM. Data in this figure are representative of at least two independent experiments.

Techniques: Infection, Western Blot, Immunofluorescence, Cell Culture, Staining

In vitro antiviral activity of selected compounds. (A) Antiviral activity against VSV pseudotyped with the S protein of Wuhan-Hu-1 and cellular toxicity for the indicated compounds in VeroE6 cells ( n = 3). (B) Virus production of SARS-CoV-2 infection by the indicated compounds at 20 μM or remdesivir (30 μM) in either A549-ACE2 or VeroE6-TMPRSS2 cells. (C) Antiviral activity of fingolimod against VSV pseudotyped with the indicated S protein ( n = 3). (D) Concentration reducing 50% of viral infection of VSV pseudotyped with the indicated S protein. All data represent the mean and standard error of 3 independent replicates. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 by two-tailed t test on log-transformed data.

Journal: ACS Omega

Article Title: Exploring SARS-CoV‑2 Spike RBD Pockets as Targets for Generic Drugs: A Combined Computational, Biophysical, and Biological Approach

doi: 10.1021/acsomega.5c05175

Figure Lengend Snippet: In vitro antiviral activity of selected compounds. (A) Antiviral activity against VSV pseudotyped with the S protein of Wuhan-Hu-1 and cellular toxicity for the indicated compounds in VeroE6 cells ( n = 3). (B) Virus production of SARS-CoV-2 infection by the indicated compounds at 20 μM or remdesivir (30 μM) in either A549-ACE2 or VeroE6-TMPRSS2 cells. (C) Antiviral activity of fingolimod against VSV pseudotyped with the indicated S protein ( n = 3). (D) Concentration reducing 50% of viral infection of VSV pseudotyped with the indicated S protein. All data represent the mean and standard error of 3 independent replicates. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 by two-tailed t test on log-transformed data.

Article Snippet: VeroE6-TMPRSS2 (Catalog No. JCRB1819, Japanese Collection of Research Bioresources), VeroE6 (kindly provided by Dr. Luis Enjuanes, CNB–CSIC, Spain), and A549-Ace2-TMPRSS2 (Catalog No. a549-hace2tpsa, Invivogen) were cultured in DMEM high glucose, with glutamine, 10% FBS, and 1% penicillin/streptomycin.

Techniques: In Vitro, Activity Assay, Virus, Infection, Concentration Assay, Two Tailed Test, Transformation Assay

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