a549 ko mavs cells  (InvivoGen)

Journal: bioRxiv

Article Title: Terminal Loop Sequences in Viral Double-Stranded RNAs Modulate RIG-I Signaling

doi: 10.1101/2025.08.02.668285

Figure Lengend Snippet: (A+B) Quantitative PCR (qPCR) for (A) type I interferon ( IFNB1 ) and (B) type III interferon ( IFNL1 ) expression by A549 cells at 6 hours post transfection (hpt) with 5 pmol of HCV X RNA, SeV cbVG 268, RSV cbVG 236, or NiV cbVG 378. One-way ANOVA was performed for statistical analysis. ns: p>0.05; * : p<0.05, *** : p<0.001; **** : p<0.0001. Data are represented as fold change over Mock. (C) qPCR for IFNL1 of control or MAVS-KO A549 cells at 6 hpt with 5 pmol of SeV cbVG 268, RSV cbVG 236, or NiV cbVG 378. One-way ANOVA was performed for statistical analysis. **** : p<0.0001. Data are represented as fold change over Mock. Data reported are biological triplicates.

Article Snippet: A549 human type II alveolar cells (ATCC, CCL-185) and MAVS-KO A549 cells (gifted from S. Weiss) were cultured at 37°C and 5% CO 2 with Dulbecco’s modified Eagle’s media (Thermofisher, 11995065) supplemented with 10% fetal bovine serum (FBS), 1 mM sodium pyruvate, 2 mM L-Glutamine, and 50 mg/mL gentamicin.

Techniques: Real-time Polymerase Chain Reaction, Expressing, Transfection, Control

Journal: bioRxiv

Article Title: Terminal Loop Sequences in Viral Double-Stranded RNAs Modulate RIG-I Signaling

doi: 10.1101/2025.08.02.668285

Figure Lengend Snippet: (A) Indicated deletions of RSV cbVG 236 were generated by in vitro transcription then 1 pmol of IVT RNA was transfected into A549 cells. (B) Expression of IFNL1 was measured by qPCR at 6 hpt. One-way ANOVA was performed for statistical analysis. ns: p>0.05; *** : p<0.001, **** : p<0.0001. Data are represented as fold change over cbVG 236. (C) Sequences from RSV cbVG 236 were attached to X RNA then in vitro transcribed. 1 pmol of RNA was transfected into A549 cells and expression of IFNB1 and IFNL1 was measured by qPCR at 6 hpt. One-way ANOVA was performed for statistical analysis. ns: p>0.05; * : p<0.05, **** : p<0.0001. Data are represented as fold change over the X RNA control. (D) Predicted structure of RNA stem loops from RSV cbVG 236. Data reported are biological triplicates.

Article Snippet: A549 human type II alveolar cells (ATCC, CCL-185) and MAVS-KO A549 cells (gifted from S. Weiss) were cultured at 37°C and 5% CO 2 with Dulbecco’s modified Eagle’s media (Thermofisher, 11995065) supplemented with 10% fetal bovine serum (FBS), 1 mM sodium pyruvate, 2 mM L-Glutamine, and 50 mg/mL gentamicin.

Techniques: Generated, In Vitro, Transfection, Expressing, Control

Journal: bioRxiv

Article Title: Terminal Loop Sequences in Viral Double-Stranded RNAs Modulate RIG-I Signaling

doi: 10.1101/2025.08.02.668285

Figure Lengend Snippet: (A) Indicated deletions of NiV cbVG 378 were generated by in vitro transcription then 1 pmol of IVT RNA was transfected into A549 cells. (B) Expression of IFNL1 was measured by qPCR at 6 hpt. One-way ANOVA was performed for statistical analysis. ns: p>0.05; *** : p<0.001, **** : p<0.0001. Data are represented as fold change over cbVG 378. (C) Sequences from NiV cbVG 378 were attached to X RNA then in vitro transcribed. 1 pmol of IVT RNA was transfected into A549 cells and expression of IFNB1 and IFNL1 was measured by qPCR at 6 hpt.. One-way ANOVA was performed for statistical analysis. ns: p>0.05; * : p<0.05, ** : p<0.01; *** : P<0.001; **** : p<0.0001. Data are represented as fold change over the X RNA control. (D) Predicted structure of RNA stem loops from NiV cbVG 378. Data reported are biological triplicates.

Article Snippet: A549 human type II alveolar cells (ATCC, CCL-185) and MAVS-KO A549 cells (gifted from S. Weiss) were cultured at 37°C and 5% CO 2 with Dulbecco’s modified Eagle’s media (Thermofisher, 11995065) supplemented with 10% fetal bovine serum (FBS), 1 mM sodium pyruvate, 2 mM L-Glutamine, and 50 mg/mL gentamicin.

Techniques: Generated, In Vitro, Transfection, Expressing, Control

Journal: bioRxiv

Article Title: Terminal Loop Sequences in Viral Double-Stranded RNAs Modulate RIG-I Signaling

doi: 10.1101/2025.08.02.668285

Figure Lengend Snippet: (A) Predicted RNA structures of high immunostimulatory and low immunostimulatory stem loops derived from cbVGs. (B-E) Indicated mutations were generated for cbVG sequences attached to the X RNA. The following sequences were mutated: (B) SeV 70-114, (C) RSV 1-48, (D) NiV 85-136, and (E) NiV 324-361. RNAs were in vitro transcribed and 1 pmol of IVT RNA was transfected into A549 cells. Expression of IFNL1 was measured by qPCR at 6 hpt. One-way ANOVAs were performed for statistical analysis. ns: p>0.05; * : p<0.05, ** : p<0.01; *** : P<0.001; **** : p<0.0001. Data are represented as fold change over the wild-type stem loops. Data reported are biological triplicates.

Article Snippet: A549 human type II alveolar cells (ATCC, CCL-185) and MAVS-KO A549 cells (gifted from S. Weiss) were cultured at 37°C and 5% CO 2 with Dulbecco’s modified Eagle’s media (Thermofisher, 11995065) supplemented with 10% fetal bovine serum (FBS), 1 mM sodium pyruvate, 2 mM L-Glutamine, and 50 mg/mL gentamicin.

Techniques: Derivative Assay, Generated, In Vitro, Transfection, Expressing

Journal: Viruses

Article Title: Mitochondrial Antiviral Signaling (MAVS) Protein Modulates the Transition from Acute to Persistent Parainfluenza Virus Infection and Resistance to Complement-Mediated Cell Lysis

doi: 10.3390/v18040416

Figure Lengend Snippet: Loss of MAVS impairs antiviral gene induction independent of STAT1. ( A ) WT or MAVS KO A549 cells were mock-infected or infected with Le-PIV5 at an MOI of 10 and harvested at 24 or 48 hpi. Total RNA was analyzed by quantitative PCR to assess expression of IFN-β, IFIT1, and OAS2. Gene expression levels are expressed relative to the corresponding mock-infected controls. ( B ) Protein lysates from WT or MAVS KO cells that were mock-infected or infected with Le-PIV5 at a MOI of 10 were collected at 24 and 48 hpi and analyzed by Western blotting for STAT1 protein. β-actin was used as a loading control. ** indicates a p value < 0.01, *** indicates a p value < 0.001, and **** indicates a p value < 0.0001.

Article Snippet: A549 KO-MAVS cells were purchased commercially (A549-DualTM KO-MAVS cells, catalog #a549d-komavs; InvivoGen, San Diego, CA, USA) and grown in DMEM 10% HI FBS, 100 U/mL penicillin, 100 μg/mL streptomycin, 100 μg/mL Normocin.

Techniques: Infection, Real-time Polymerase Chain Reaction, Expressing, Gene Expression, Western Blot, Control

Journal: Molecular Cell

Article Title: Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung epithelial cells

doi: 10.1016/j.molcel.2022.04.033

Figure Lengend Snippet: NLRP1 is an innate immune sensor of SARS-CoV-2 infection (A) Western blot examination of NLRP1, NLRP3, and ACTIN in various human epithelial cells and cell lines. (B) Cell death (LDH) and viability (ATP Glo) evaluation in A549 ACE2/NLRP1+ and A549 ACE2/NLRP1− airway epithelial cell lines infected with various multiplicity of infection (MOI) of SARS-CoV-2 for 24 h. (C) Florescence microscopy and associated quantifications of ASC-GFP specks in A549 ACE2/NLRP1+/ASC-GFP and A549 ACE2/NLRP1−/ASC-GFP airway epithelial cell lines infected with SARS-CoV-2 (MOI 0.05) for 24 h. Nucleus was stained with Hoechst (blue), and nucleocapsid (N) was stained in red after fixation. Brightfield/ASC-GFP pictures were taken in dish during cell infection. Images shown are from one experiment and are representative of n = 3 independent experiments. For quantifications, the percentage of cells with ASC complexes was determined by determining the ratios of cells positives for ASC speckles on the total nuclei. At least 10 fields from n = 3 independent experiments were analyzed. Values are expressed as mean ± SEM. (D) Cell death (LDH) evaluation in A549 NLRP1+ and A549 NLRP1− airway epithelial cell lines infected with SARS-CoV-2 (MOI 0.05) for 24 h in the presence/absence of the pan-caspase inhibitor Z-VAD (25 μM), NSP5 protease inhibitor PF-00835231 (10 μM), or the RNA-dependent RNA polymerase (RdRp) inhibitor remdesivir (5 μM). (E) Florescence microscopy and associated quantifications of ASC-GFP specks in A549 ACE2/NLRP1+/ASC-GFP and A549 ACE2/NLRP1−/ASC-GFP airway epithelial cell lines infected with SARS-CoV-2 (MOI 0.05) for 24 h. Nucleus was stained with Hoechst (blue). Brightfield/ASC-GFP pictures were taken in dish during cell infection. Images shown are from one experiment and are representative of n = 3 independent experiments; scale bars, 10 μm. For quantifications, the percentage of cells with ASC complexes was determined by determining the ratios of cells positives for ASC speckles on the total nuclei. At least 10 fields from n = 3 independent experiments were analyzed. Values are expressed as mean ± SEM. (F) Cell death (LDH) evaluation in NHBE airway epithelial cells infected with various multiplicity of infection (MOI) of SARS-CoV-2 for 36 h in the presence/absence of the pan-caspase inhibitor Z-VAD (25 μM), Necroptosis inhibitor Necrostatin-1s (Nec1s, 30 μM), or the Ferroptosis inhibitor Ferrostatin-1 (Fe1, 10 μM). (G) Western blot characterization of genetic invalidation of NLRP1 in NHBE population using CRISPR-Cas9 and measure of cell lysis (LDH release) in NHBE WT and NHBE NLRP1−/− airway epithelial cells infected with various multiplicity of infection (MOI) of Wuhan or Delta variant SARS-CoV-2 for 36 h. Efficiency of genetic invalidation by single-guide RNAs (sgRNAs were evaluated at the whole cell population. Data information: western blot (A and G) images are from one experiment performed 3 times. Graphs (B), (D), (F), and (G) show data presented as means ± SEM from n = 3 (F and G), n = 4 (B) and n = 6 (D) independent pooled experiments; ∗∗∗ p ≤ 0.001 for the indicated comparisons with t test. Images (C and E) are representative of one experiment performed 3 times.

Article Snippet: A549-Dual™ KO-MAVS Cells , a549d-komavs , Invivogen.

Techniques: Infection, Western Blot, Microscopy, Staining, Protease Inhibitor, CRISPR, Lysis, Variant Assay

Journal: Molecular Cell

Article Title: Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung epithelial cells

doi: 10.1016/j.molcel.2022.04.033

Figure Lengend Snippet: SARS-CoV-2 NSP5 protease-cleaved NLRP1 at the Q333 site nucleates NLRP1 inflammasome (A) Florescence microscopy and associated quantifications of ASC-GFP specks in A549 NLRP1+/ASC-GFP and A549 NLRP1−/ASC-GFP airway epithelial cell lines infected with SARS-CoV-2 (MOI 0.05) for 24 h in the presence or absence of proteasome inhibitor bortezomib (0.1 μM) or inhibitor of the glycine N-degron pathway MLN4924 (1 μM). Images shown are from one experiment and are representative of n = 3 independent experiments; scale barss 10 μm. For quantifications, the percentage of cells with ASC complexes was determined by determining the ratios of cells positives for ASC speckles on the total cells presents in the wells. At least 10 fields from n = 3 independent experiments were analyzed. Values are expressed as mean ± SEM. (B) Western blot examination of NLRP1 cleavage using an anti-NLRP1 N-terminal antibody (aa 1–323) upon coincubation of SARS-CoV-2, SARS-CoV-1, or MERS-CoV 3CL (NSP5) proteases (5 μM) with A549 NLRP1+ airway epithelial cell lysates in presence or absence of the 3CL inhibitors GC-376 (10 μM) or PF-00835231 (10 μM). NLRP1 N-terminal, NLRP1 C-terminal, NSP5, and ACTIN were immunoblotted. (C) Florescence microscopy and associated quantifications of ASC-GFP specks in A549 NLRP1+/ASC-GFP airway epithelial cell lines transduced with a doxycycline (dox)-inducible plasmid encoding NSP5 or its catalytically inactive mutant NSP5 C145A . Images shown are from one experiment and are representative of n = 3 independent experiments; scale bars, 10 μm. For quantifications, the percentage of cells with ASC complexes was determined by determining the ratios of cells positives for ASC speckles on the total cells presents in the wells. At least 10 fields from n = 3 independent experiments were analyzed. Values are expressed as mean ± SEM. (D) Schematic representation of the approximate NLRP1 N-terminal fragment generated by NSP5 protease cut. (E) Western blot examinations of the ability of NSP5 to cleave various NLRP1 constructs mutated in glutamine (Q) at various sites. Immunoblots show anti-N-terminal NLRP1, ACTIN, and NSP5. (F) Florescence microscopy and associated quantifications of ASC-GFP specks in A549 NLRP1+/ASC-GFP or A549 NLRP1 Q333A /ASC-GFP airway epithelial cell lines transduced with a doxycycline (dox)-inducible plasmid encoding NSP5 or its catalytically inactive mutant NSP5 C145A . Images shown are from one experiment and are representative of n = 3 independent experiments; scale bars, 10 μm. For quantifications, the percentage of cells with ASC complexes was determined by determining the ratios of cells positives for ASC speckles on the total nuclei (Blue). At least 10 fields from n = 3 independent experiments were analyzed. Values are expressed as mean ± SEM. (G) Cell death (LDH) evaluation in A549 NLRP1+ and A549 NLRP1− airway epithelial cell lines expressing a doxycycline (dox)-inducible plasmid encoding NSP5 in the presence or absence of the proteasome inhibitor bortezomib (0.1 μM) or inhibitor of the glycine N-degron pathway MLN4924 (1 μM). (H) Western blot examination of NLRP1 cleavage using an anti-NLRP1 N-terminal antibody (aa 1–323) after infection of A549 NLRP1− , A549 NLRP1+ A549 NLRP1Q333A , or A549 NLRP1Q130A airway epithelial cells with SARS-CoV-2 (MOI 0.05) for 24 h in the presence/absence of the proteasome inhibitor bortezomib (0.1 μM, Bort.). NLRP1 N-terminal, NSP5, and ACTIN were immunoblotted. ∗ NS: prominent nonspecific bands, not specific. (I) Cell death (LDH) evaluation in A549 NLRP1+ and A549 NLRP1Q333A airway epithelial cell lines infected with SARS-CoV-2 (MOI 0.05) for 24 h. (J) Western blot examination of NLRP1 cleavage using an anti-NLRP1 N-terminal antibody (aa 1–323) after infection of NHBE WT airway epithelial cells with SARS-CoV-2 (MOI 1) for 36 h in the presence/absence of the proteasome inhibitor bortezomib (0.1 μM) or inhibitor of the glycine N-degron pathway MLN4924 (1 μM). NLRP1 N-terminal, nucleocapsid, and ACTIN were immunoblotted. (K) Measure of cell lysis (LDH release) in NHBE WT and NHBE NLRP1−/− airway epithelial cells infected with SARS-CoV-2 (MOI 1) for 36 h in the presence/absence of the proteasome inhibitor bortezomib (0.1 μM) or inhibitor of the glycine N-degron pathway MLN4924 (1 μM). Data information: images (A, C, and F) show one experiment performed 3 times. Western blot (B, E, H, and J) images are from one experiment performed 3 times. Graphs (C, G, I, and K) show data presented as means ± SEM from n = 3 independent pooled experiments; ∗∗∗ p ≤ 0.001 for the indicated comparisons with t test.

Article Snippet: A549-Dual™ KO-MAVS Cells , a549d-komavs , Invivogen.

Techniques: Microscopy, Infection, Western Blot, Transduction, Plasmid Preparation, Mutagenesis, Generated, Construct, Expressing, Lysis

Journal: Molecular Cell

Article Title: Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung epithelial cells

doi: 10.1016/j.molcel.2022.04.033

Figure Lengend Snippet: NSP5 protease cleaves Gasdermin D in its pore-forming domain (A) Cell death (LDH) evaluation in A549 NLRP1+ , A549 NLRP1− , or A549 NLRP1+/GSDMD− airway epithelial cell lines infected for 24 h with SARS-CoV-2 (MOIs 0.1, 0.01, and 0.001) or stimulated with doxycycline (dox)-induced NSP5 expression. (B) Measure of cell lysis (LDH release) and cell viability (Cell titer Glo) in NHBE WT and NHBE GSDMD−/− airway epithelial cells infected with various SARS-CoV-2 viral strains (MOI 1) for 36 h. (C) Western blot examination of Gasdermin D (GSDMD) processing in A549 NLRP1+ cells infected with SARS-CoV-2 at MOI of 0.1 for 24 h. GSDMD was immunoblotted using an anti-C-terminal antibody (recognizes full-length and C-terminal cleaved forms of GSDMD) or with an anti-GSDMD active N-terminal fragment (30 kDa) specific antibody. NLRP1, ACTIN, and SARS-CoV-2 nucleocapsid were also evaluated. (D) Western blot examination of GSDMD and NLRP1 cleavages upon coincubation of SARS-CoV-2 NSP3 protease or SARS-CoV-2/SARS-CoV1 3CL (NSP5) proteases (5 μM) with A549 NLRP1+ or A549 NLRP1− cell lysates in the presence or absence of the 3CL inhibitor PF-00835231 (10 μM). GSDMD (anti C-terminal), NLRP1 N-terminal, NSP5, and ACTIN were immunoblotted. (E) Coomassie observation of recombinant GSDMD cleavage by various amounts of SARS-CoV-2 NSP5 protease and top-down mass-spectrometry identification of GSDMD-cleaved fragments. In blue are represented the various GSDMD fragments identified upon NSP5 coincubation. In red is the NSP5 protease detected by mass spectrometry. (F) Western blot examination and schematic representation of GSDMD cleavage by SARS-CoV-2 3CL (NSP5) or recombinant human caspase-1 (CASP1) proteases in cell lysates from A549 expressing WT GSDMD or GSDMD 193A constructs. GSDMD (anti-C-terminal), NSP5, and ACTIN were immunoblotted. (G) Cell death (LDH) evaluation in A549 cells expressing doxycycline-inducible GSDMD fragments, including GSDMD full-length (FL), caspase-1-generated active GSDMD (1–275), or NSP5-generated 1–193 and 194–484 GSDMD fragments. Cell lysis was determined 18 h after doxycycline (dox) addition in the culture medium. (H and I) Cell death (LDH) evaluation in A549 NLRP1+/GSDMD− cells complemented or not with constructs coding for WT GSDMD or GSDMD 193A . Cells were transduced with dox-inducible NSP5 plasmids, treated with the NLRP1 activator Val-boro (10 μM) or infected (I) with SARS-CoV-2 (MOI 0.01). Cell lysis was determined 18 h after doxycycline (dox) addition, 10 h after Val-boro addition in the culture medium, or 24 h after infection. Data information: graphs (A, B, G, H, and I) show data presented as means ± SEM from n = 3 independent pooled experiments; ∗∗∗ p ≤ 0.001 for the indicated comparisons with t test. Western blot (C, D, and F) images are from one experiment performed 3 times. Images (E) show one experiment performed 3 times.

Article Snippet: A549-Dual™ KO-MAVS Cells , a549d-komavs , Invivogen.

Techniques: Infection, Expressing, Lysis, Western Blot, Recombinant, Mass Spectrometry, Construct, Generated, Transduction

Journal: Molecular Cell

Article Title: Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung epithelial cells

doi: 10.1016/j.molcel.2022.04.033

Figure Lengend Snippet: NLRP1 engages a caspase-3/Gasdermin E-dependent pyroptosis pathway upon SARS-CoV-2 infection (A) Western blot examination of Gasdermin E, caspases-3, and caspases-8 processing in A549 NLRP1+ and A549 NLRP1− cells after 24 h of infection with SARS-CoV-2 (MOI 0.05) in the presence or absence of the pan-caspase inhibitor Z-VAD (25 μM). Immunoblots were performed against full-length and processed forms of Gasdermin E (p55 and p30), caspase-8 (p54 and p15), caspase-3 (p35 and p17/19), SARS-CoV-2 nucleocapsid (p40), NLRP1 N-terminal (p130/110), and ACTIN (p40). (B) Western blot examination of Gasdermin E and caspases-3 processing in NHBE WT and NHBE NLRP1−/− cells after 36 h of infection with SARS-CoV-2 (MOI 1). Immunoblots were performed against full-length and processed forms of Gasdermin E (p55 and p30), caspase-3 (p35 and p17/19), SARS-CoV-2 nucleocapsid (p40), NLRP1 N-terminal (p130/110), and ACTIN (p40). (C and D) Measure of caspase-1 (C) and caspase-3/-7 (D) activities in SARS-CoV-2-infected (MOI 0.5) NHBE WT or A549 NLRP1+ cells for 36 h in the presence or absence of inhibitors of caspase-1 (Z-YVAD, 40 μM) or caspase-3/-7 (Z-DEVD, 30μM). Val-boro (5 μM) was used a positive control of NLRP1-driven caspase activity for 10 H. (E) Measure of cell lysis (LDH release) in A549 NLRP1+ or NHBE-infected cells with SARS-CoV-2 (MOI 0.05 and 1, respectively) for 24 h in the presence/absence of the pan-caspase inhibitor Z-VAD (25 μM), the caspase-1 inhibitor Z-YVAD (40 μM), the caspase-8 inhibitor Z-IETD (40 μM), or the caspase-3 inhibitor Z-DEVD (30 μM). (F) Western blot characterization of genetic invalidation of CASP3 in A549 population cells using CRISPR-Cas9 approaches and measure of cell lysis (LDH release) in A549 NLRP1+ or A549 NLRP1+/CASP3− -infected cells with SARS-CoV-2 (MOI 0.05) for 24 h in the presence/absence of the pan-caspase inhibitor Z-VAD (25 μM), the caspase-1 inhibitor Z-YVAD (40 μM), or the caspase-3 inhibitor Z-DEVD (30 μM). Efficiency of genetic invalidation by single-guide RNAs (sgRNAs) targeting GFP or caspase-3 was evaluated at the whole cell population. (G) Western blot characterization of genetic invalidation of GSDME in A549 population cells using CRISPR-Cas9 approaches and measure of cell lysis (LDH release) in A549 NLRP1+ , A549 NLRP1+/GSDMD− , or A549 NLRP1+/GSDME− -infected cells with SARS-CoV-2 (MOIs 0.001, 0.01, and 0.1) for 24 h. Efficiency of genetic invalidation by single-guide RNAs (sgRNAs) targeting GFP or GSDME was evaluated at the whole cell population. (H) Western blot characterization of genetic invalidation of GSDME in NHBE population cells using CRISPR-Cas9 approaches and measure of cell lysis (LDH release) in NHBE WT or NHBE GSDME − / − -infected cells with SARS-CoV-2 (MOIs 0.1, 0.5, and 1) for 36 h. Efficiency of genetic invalidation by single-guide RNAs (sgRNAs) targeting GFP or GSDME was evaluated at the whole cell population. Data information: western blot (A, B, and E–G) images are from one experiment performed 3 times. Graphs (C–G) show data presented as means ± SEM from n = 3 independent pooled experiments; ∗∗∗ p ≤ 0.001 for the indicated comparisons with t test.

Article Snippet: A549-Dual™ KO-MAVS Cells , a549d-komavs , Invivogen.

Techniques: Infection, Western Blot, Positive Control, Activity Assay, Lysis, CRISPR

Journal: Molecular Cell

Article Title: Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung epithelial cells

doi: 10.1016/j.molcel.2022.04.033

Figure Lengend Snippet:

Article Snippet: A549-Dual™ KO-MAVS Cells , a549d-komavs , Invivogen.

Techniques: Virus, Variant Assay, Recombinant, Microscopy, Plasmid Preparation, Mutagenesis, Construct, Software