EMBO/sd-character-level-ner huggingface dataset:
The non-structural protein NS1 of ZIKV enhances ZIKV-induced NLRP3 inflammasome activation.Figure 1(A) ELISA of supernatant IL-1β for unprimed THP-1 cells (UT) or LPS-primed (500 ng/ml, 3 hrs) THP-1 cells then infected with ZIKV (MOI=1) for 36 hrs. Uninfected cells serves as mock control. (B) Immunoblot analysis of supernatant (Sup) and cell extracts (Lys) of THP-1 cells, left untreated or primed by LPS (500 ng/ml, 3 hrs), after ZIKV infection (MOI=1) for 36 hrs. (C) ELISA of IL-1β in the supernatants of wild type (WT), NLRP3 knockout (KO) #1 or AIM2 KO#1 THP-1 cells left untreated (UT), or pretreated with LPS (500 ng/ml, 3 hrs) followed by ATP (5 mM, 6 hrs) stimulation, or stimulated with poly (dA:dT) (1mg/ml, 6 hrs), or infected with ZIKV (MOI=1, 36 hrs). (D) ELISA of IL-1β in the supernatants of two clones of NLRP3 KO THP-1 cells with or without ZIKV infection (MOI=1) at the indicated time points. (E) ELISA of IL-1β in the supernatants of PBMCs from two donors transfected with control (ctrl) siRNA or NLRP3 siRNA followed by ZIKV infection (MOI=1) for 36 hrs. (F) ELISA of IL-1β in the supernatant of WT, NLRP3 KO or AIM2 KO THP-1 cells with ZIKV (MR766 or GZ01) (MOI=1) or DENV-2 (MOI=1) infection for 36 hrs. (G) ELISA of IL-1β in the supernatants of THP-1 cells pre-infected with ZIKV for 24 hrs or mock control. The cells were then treated with LPS (500 ng/ml, 3 hrs) followed by ATP (5 mM) treatment for 6 hrs. (H) Immunoblot analysis of supernatant (Sup) and cell extracts (Lys) of THP-1 cells pre-infected with ZIKV (MOI=1) or mock control for 24 hrs. The cells were then treated with LPS (500 ng/ml, 3 hrs) followed by ATP (5 mM) stimulation for 6 hrs. (I) Immunoblot analysis of supernatants and cell extracts of 293T cells transfected with plasmids expressing NLRP3, ASC, pro-caspase-1 and pro-IL-1β together with NS1. (J) Immunoblot analysis of protein extracts of Flag-tagged NS1-inducible THP-1 cells treated with increasing doses of doxycycline (Dox) for 24 hrs. (K) ELISA of IL-1β in the supernatants of Flag-NS1-inducible THP-1 cells left unprimed then treated with ATP (5 mM, 6 hrs) or poly (I:C) (2 mg/ml, 6 hrs), or pre-treated with LPS (500 ng/ml, 3 hrs) followed by ATP (5 mM, 6 hrs) or poly (I:C) (2 mg/ml, 6 hrs) stimulation. (L) Immunoblot analysis of supernatants (Sup) and cell extracts (Lys) of Flag-NS1-inducible THP-1 cells pre-treated with LPS (500 ng/ml, 3 hrs) followed by ATP (5 mM, 6 hrs) or poly (I:C) (2 mg/ml, 6 hrs) stimulation.
Figure 8A, B. Representative exposure-matched FISH/IF images for DRG neurons co-transfected with control vs. nucleolin (Ncl) siRNA plus siRNA-resistant wild type (WT; A) or ∆GAR (B) Ncl cDNAs. Axonal Kpnb1 mRNA is decreased with the Ncl knockdown, and this is not rescued by expression of ∆GAR Ncl mutant (scale bars - 10 µm). C, D, Quantification of RNA signals from FISH/IF for Kpnb1, mTOR, and Inpp5f in cell bodies (C) and axons (D) for DRG cultures transfected as in A are shown. Axons of neurons cotransfected with Ncl siRNA plus ∆GAR show significantly lower signals for each mRNA compared to Ncl siRNA plus WT and control siRNA plus WT or ∆GAR; N ≥ 10 for cell bodies, N ≥ 25 for axons over 3 biological repeats; means ± SEM; **** p ≤ 0.001 by one-way ANOVA with Tukey HSD post hoc.
| Comprehensive transcriptome analysis also identified REST/NRSF target genes in up-regulated genes in offspring derived from aged fathers.Figure 4A. Volcano plot for DEGs in the embryonic brain of YFO and AFO at E14.5 (n=3 in each group). Green lines indicate a twofold change and p=0.01. Orange dots indicate REST/NRSF target genes. Data information: Data are presented in the volcano plot or line chart format. *p<0.05, ** p<0.01, ***p<0.001, determined by nominal GSEA p-value. B. GO gene sets in AFO up-regulated genes. C. GO gene sets in AFO down-regulated genes. D. Motif gene sets in AFO up-regulated genes. E. GSEA plots of DEGs in NRSF/REST target gene sets. Data information *p<0.05, ** p<0.01, ***p<0.001, determined by nominal GSEA p-value. NES, normalized enrichment score. F. GSEA plots of DEGs for early-fetal gene sets. G. GSEA plots of DEGs for late-fetal gene sets. Data information: *p<0.05, ** p<0.01, ***p<0.001, determined by nominal GSEA p-value. NES, normalized enrichment score. H. GSEA plots of DEGs for SFARI-related gene sets. I. GSEA plots of DEGs for DNA hypo-methylation neighboring gene sets. J. GSEA plots of DEGs for DNA hypo-methylation neighboring gene sets with REST/NRSF binding motifs. Data information *p<0.05, ** p<0.01, ***p<0.001, determined by nominal GSEA p-value. NES, normalized enrichment score.
Figure 3A. Immunoblot analysis of p-TBK1, -IKKi, -IRF3, -P38, -JNK1/2, -ERK1/2 and -IκBα in lysates of RKIP+/+, RKIP+/- and RKIP-/- peritoneal macrophages stimulated with VSV (MOI, 0.1) for the indicated time. B. Immunoblot assay of RKIP+/+, RKIP+/- and RKIP-/- peritoneal macrophage cells treated with intracellular poly(I:C) (1 μg/ml). C. Immunoblot analysis of phosphorylated (p-) TBK1, IKKi, IRF3, P38, JNK1/2, ERK1/2 in peritoneal macrophage transfected with RKIP-specific or scrambled siRNA, followed by infection with VSV (MOI, 0.1). β-actin was used as a loading control. D. Immunoblot analysis of p- TBK1, -IKKi, -IRF3, -P38, -JNK1/2, -ERK1/2 and -IκBα in lysates of VSV-treated RAW264.7 cells stably over-expressing RKIP. E. Immunoblot analysis in lysates of RAW264.7 cells stably overexpressing RKIP treated with intracellular poly(I:C) (1 μg/ml). F. Luciferase activity in 293T cells transfected with plasmid encoding a luciferase reporter for IFN-β (IFN-β-luc) or ISRE (ISRE-luc), and an expression vector for RKIP (0, 50, 100, 200 ng each), together with plasmids encoding RIG-I CARD, TBK1, IKKi and IRF3 5D.
Cortex glial overgrowth mediated by htlACT overexpression triggers NB cell cycle delayA-E) Representative images showing that both pan-glial (repo-GAL4>) and cortex glial (NP2222-GAL4>) htlACT overexpression significantly reduce NB EdU index, quantified in (E) (n=15 ,14; 10, 16 brain lobes).Figure 5A-E) Representative images showing that both pan-glial (repo-GAL4>) and cortex glial (NP2222-GAL4>) htlACT overexpression significantly reduce NB EdU index, quantified in (E) (n=15 ,14; 10, 16 brain lobes). (A, B, C, D) are single sections with Mira and EdU staining, and (A', B' C', D') are Z-projection of the EdU staining. pan-glial (repo-GAL4) htlACT overexpression lengthens NB cell cycle, quantified in (F) The cell cycle length is measured as the length between consecutive divisions. Representative still images from ex vivo CNS live imaging at 72ALH showing that pan-glial (repo-GAL4) htlACT overexpression lengthens NB cell cycle, (n= 25, 6 NBs imaged from 3 brains per genotype). NBs (Dpn::GFP, red; Histone RFP, grey) are circled with blue dashed lines. I) Schematic depicting concurrent glial FGF activation (repo-LexA >LexAop-htlACT), and NB overexpression of fly-FUCCI (dnab-GAL4>UAS-GFP::E2F1, UAS-RFP::CycB). The fly-FUCCI system utilizes the fusion protein GFP::E2F1 (a marker for cells in G2, M and G1phase) and RFP::CycB ( a marker for cells in S, G2, M phase) to monitor cell cycle progression. Cells in G1 phase are GFP+ RFP- (green), cells in G2/ M phase are GFP+RFP+ (yellow), and cells in S phase are GFP-RFP+ (red), whereas, cells in G1-S transition are weakly labelled by both GFP and RFP (grey). J-L) Representative images showing that the percentage of NBs in G1-S transition and G2/M phase are both significantly increased with significantly less cells remaining in G1 phase, quantified in (L) (n= 9, 10 brain lobes). NBs in G1 phase (Mira+, GFP+) are circled by green dashed lines; NBs in G1-S transition (Mira+, GFP-RFP-) are circled by grey dashed lines; NBs in S phase (Mira+, RFP+) are circled by red dashed lines; and NBs in G2/M phase (Mira+, GFP+RFP+) are circled by yellow dashed lines. M-O) Representative images showing that the number of EdU+ neurons generated per NB is significantly reduced upon pan-glial overexpression of FGF (repo-LexA > LexAop-htlACT; yellow arrows), quantified in (O) n= 94, 127 NB lineages imaged from 5 and 7 brain lobes, respectively). NB lineages are marked with dnab-gal4 > GFP.
Altered OxPhos protein level and respiration in TIMM50 mutant fibroblasts A Western blot for representatives of all five respiratory complexes in control and TIMM50 mutant fibroblasts grown in glucose or galactose.Figure 4Western blot for representatives of all five respiratory complexes in control and TIMM50 mutant fibroblasts grown in glucose or galactose. Two biological replicates are shown for each cell line and condition. Significant changes in protein levels in TIMM50 mutant fibroblasts compared to controls have been boxed in red. B Western blot for representatives of all five respiratory complexes in control and TIMM50 mutant fibroblasts, transduced with the empty vector (EV) or with wild-type TIMM50 grown in glucose or galactose. Two biological replicates were obtained for each cell line and condition. Significant changes in protein levels in TIMM50 mutant fibroblasts complemented with TIMM50 compared to EV have been boxed in red. Oxygen consumption measurements in control and TIMM50 mutant fibroblasts grown in glucose or galactose. Values of basal and maximal respiration along with ATP-production dependent, proton leak respiration and spare capacity are shown. Data are shown as mean ± SD, n = 4 biological replicates; ∗p < 0.05, ∗∗p < 0.01, ∗*∗p < 0.001 grouping both controls together. D Oxygen consumption measurements in control and TIMM50 mutant fibroblasts, transduced with the empty vector (EV) or with wild-type TIMM50 grown in glucose or galactose. Values of basal and maximal respiration along with ATP-production dependent, proton leak respiration and spare capacity are shown. Data are shown as mean ± SD, n = 4 biological replicates; ∗p < 0.05, ∗∗p < 0.01, ∗*∗p < 0.001.
Gene and protein expression of PD downregulated key TFs and proposed theoretic model.Figure 7A, BGraphical representation of gene and protein expression of the key TFs FOXA1, NR3C1, HNF4A and FOSL2 (A) (see also Fig EV3B and Source data for Fig 7), or of the PD upregulated genes (B) (see also Fig EV3A and Source data for Fig 7) identified in iPSC‐derived DAn from PD patients, normalized to the expression of controls, and expressed, respectively, as log2 or lineal fold change (FC) values. (For gene expression, linear model with empirical bayes moderation of the variance similar to ANOVA with FDR‐adjusted P < 0.05; for protein expression, two‐tailed Student's t‐test (**P < 0.01, *P < 0.05). Samples were studied at least in three independent experiments. Data are represented as group mean ± SEM). CProposed model in which deficits of the key TFs FOXA1,NR3C1,HNF4A, and FOSL2 relevant to PD lead to DNA methylation changes. Key 1 denotes differentially methylated gene, key 2 denotes DEG, key 3 denotes significant correlation of DNA methylation with proximal gene expression, key 4 denotes significant correlation of key TF gene expression with distal DNA methylation at enhancers, and key 5 denotes differentially expressed protein. Blue‐shaded boxes indicate gene expression downregulation, whereas red‐shaded boxes indicate upregulation. Illustration of our model was built by selecting most prominent alterations detected by unbiased genomewide approaches in our study.
Figure 2LNCaP cells were transfected with the indicated plasmids for 48 h and harvested for western blot analysis with the indicated antibodies to detect the interaction between BRD4 and SPOP (A) LNCaP cells were transfected with the indicated plasmids for 48 h and harvested for western blot analysis with the indicated antibodies to detect the BRD4 ubiquitination (B). C. C4-2 cells were stably infected with the lenti-virus expressing empty vector (EV) or SPOP mutants and harvested for western blot analysis with the indicated antibodies. D. C4-2 xenograft tumors expressing EV or F133V and SPOP WT and Q165P PDX tumors were harvested for western blot analysis with the indicated antibodies. T1: tumor 1; T2: tumor 2. E. Representative IHC images of PTEN protein in SPOP WT and Q165P PDX tumors. Scale bars: 100 µm for 20 x fields; 50 µm for 40 x fields.
POLG NSCs exhibited decreased TFAM level and mtDNA depletion, but not mtDNA deletion, consistent with iPSC-derived DA neurons.Figure 6A, B: Flow cytometric analysis of TOMM20 (A, n=3, technical replicates per clone for control; n=4, technical replicates per clone for WS5A and CP2A) and TFAM protein expression (B, n=3, technical replicates per clone for control and CP2A; n=5, technical replicates per clone for WS5A) in NSCs. Expressed as specific TFAM level (total TFAM/TOMM20). C: Relative mtDNA copy number analyzed by RT-qPCR using primers and fluorogenic probes for regions of ND1 and nuclear gene APP in all NSCs (n=4, technical replicates per clone for control; n=5, technical replicates per clone for WS5A; n=7, technical replicates per clone for CP2A). D, E: Flow cytometric analysis of TOMM20 expression level (D, n=4, technical replicates per clone) and TFAM protein expression (E, n=4, technical replicates for control and WS5A; n=5, technical replicates for CP2A) in fibroblasts. Expressed as specific TFAM level (total TFAM/TOMM20). F: Relative mtDNA copy number analyzed by RT-qPCR for regions of ND1 and nuclear gene APP in fibroblasts (n=3, technical replicates for control; n=4, technical replicates for WS5A and CP2A). G: Long-PCR for detection of mtDNA deletions in NSCs and their parental fibroblasts from WS5A and CP2A patients. H: Representative images of confocal microscopy with immunofluorescence labeling of DA neuron-specific marker TH (green) and neuron-specific marker MAP2 (red) for iPSC-derived DA neurons (scale bars, 25 µm). Nuclei are stained with DAPI (blue). I: Histogram of the positive cell population stained with DA marker TH in iPSC-derived DA neurons using flow cytometric analysis. J: Flow cytometric measurement of specific TFAM level (total TFAM/TOMM20) in iPSC-derived DA neurons from Detroit 551 control, WS5A and CP2A POLG patients (n=8, technical replicates per clone for control; n=5, technical replicates per clone for WS5A; n=4, technical replicates per clone for CP2A). K: Relative mtDNA copy number analyzed by RT-qPCR for regions of ND1 and nuclear gene APP in all iPSC-derived DA neurons (n=3, technical replicates per clone).
H3K27me3 amplification and SMARCB1 deletion drives mithramycin sensitivity in rhabdoid tumor.Figure 4A, B: Mithramycin displaces BRD9 and SMARCE1 SWI/SNF subunits from chromatin in a time-dependent manner in G401 (A) but only BRD9 with SMARCB1 re-expression in G401 (B) cells. Western blot analysis showing whole cell lysate (Total), cytoplasmic soluble (CS), nuclear soluble (NS), and chromatin bound (Chr) fractions collected after exposure to solvent (S) or 100nM mithramycin for 8 or 18h and probed for the SWI/SNF subunits (BRD9, SMARCB1 or SMARCE1) or H3 (chromatin fraction control) and GAPDH (soluble fraction control). C: BT12 cells show a threshold of exposure that leads to irreversible growth inhibition. The cells were exposed to 100nM MMA for the indicated times followed by replacement with drug-free medium. Beyond 8h (red) of mithramycin exposure, the cells do not recover proliferative potential and exhibit a phenotype consistent with cell death. Data represents mean with standard deviation derived from three independent experiments. D: Mithramycin leads to H3K27me3 amplification in a time-dependent manner that precedes the induction of apoptosis as measured by the cleavage of PARP. Western blot lysates collected at 2h, 4h, 6h, 8h, 12h, 18h, 24h of continuous 100nM mithramycin treatment. E: Suppression of EZH2 expression and activity antagonizes mithramycin activity in BT12 rhabdoid tumor cells. Data represents dose response curves of mithramycin in BT12 cells following a 48h exposure in the presence of siRNA silencing of the PRC2 subunit EZH2 or treatment with the EZH2 inhibitor EPZ-6438 relative to mithramycin alone (media) or a non-targeting siRNA (siNeg). Data represents mean with standard deviation derived from three independent experiments. F: Suppression of SMARCB1 sensitizes U2OS osteosarcoma cells (wild type SWI/SNF) to mithramycin. Data represents dose response curves of mithramycin in BT12 cells following a 48h exposure in the presence of siRNA silencing of the SWI/SNF subunit SMARCB1 relative to a non-targeting siRNA (siNeg). Data represents mean with standard deviation derived from three independent experiments. G. Western blot showing concentration-dependent increase in H3K27me3 following exposure to 100nM, 50nM, 25nM mithramycin for 18h in SMARCB1- silenced U2OS cells relative to loading control (H3). Knockdown of SMARCB1 following siRNA suppression triggers mithramycin-dependent H3K27me3 amplification, while siNegative (control) does not have an effect on H3K27me3 following mithramycin exposure.
Figure 1 A Exponentially growing cell cultures were serially diluted (1:10) before being spotted out onto YEPD plates with or without methyl methanesulfonalte (MMS), hydroxyurea (HU), phleomycin (Phleo) or camptothecin (CPT) at the indicated concentrations  B Appropriate dilutions of cell cultures were distributed on YEPD plates with or without different concentrations of CPT. Plates were incubated 3 days at 25°C to determine the colony-forming units. Plotted values are the mean values with error bars denoting SD (n = 3)  C Wild-type and tel1∆ strains expressing a fully functional Top1-HA tagged protein were arrested in G1 with α-factor (αf) and released into YEPD supplemented with CPT (50 μM). Western blot with anti-HA antibodies (top) and Coomassie staining (bottom) of protein extracts prepared at the indicated time points  D, E Exponentially growing cell cultures were serially diluted (1:10) before being spotted out onto YEPD plates with or without CPT  D, E Exponentially growing cell cultures were serially diluted (1:10) before being spotted out onto YEPD plates with or without CPT  F Colony-forming unit-assay as in (B)
Figure 1WT and SNX10 KO Caco-2 cells were treated with indicated doses of OMVs for 24h. Protein expression of E-cadherin and SNX10 was determined by immunoblots (A) and quantified by ImageJ software (B) (n = 3 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001. WT and SNX10 KO Caco-2 cells were treated with indicated doses of OMVs for 24h. The fold changes in mRNA levels of CDH1 (encoding E-cadherin) and SNX10 in Caco-2 cells were determined by RT-qPCR (C) (n = 6 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001. WT and SNX10 KO Caco-2 cells were treated with OMVs (100 μg/mL) for the indicated time. Protein expression of E-cadherin and SNX10 was determined by immunoblots WT and SNX10 KO Caco-2 cells were treated with OMVs (100 μg/mL) for the indicated time. Protein expression of E-cadherin and SNX10 was quantified by ImageJ software (E) (n = 3 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001. WT and SNX10 KO Caco-2 cells were treated with OMVs (100 μg/mL) for the indicated time. The fold changes in mRNA levels of CDH1 and SNX10 were determined by RT-qPCR (F) (n = 6 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001. G, H Confocal images of E-cadherin staining in Caco-2 cells treated with OMVs (100 μg/mL) for the indicated time were captured (G), and the fluorescence intensity of E-cadherin staining was quantified by ImageJ software (H) (n = 3 independent experiments, n = 18 fields analysed). Scale bar: 20 μm. Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001. I TEER value of Caco-2 cell monolayers incubated with or without OMVs (100 μg/mL) for 24 h was analyzed (n = 9 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001. J Caco-2 cell monolayers on transwell membranes were treated with or without OMVs (100 μg/mL) for 24h. FITC-dextran was added to these cells (top of the membrane). After 2h, FITC-dextran levels in the bottom chamber wells were measured (n = 9 independent experiments). Data information: Data are means ± SD. One-way ANOVA followed by Bonferroni post hoc test was used for statistical analyzes. *p < 0.05; **p < 0.01; ***p < 0.001.
Activation of thermogenesis by increased sympathetic innervation of BAT in Cdk4-/- mice is blunted by β-adrenergic antagonist treatment.Figure 4A-B TH immunohistochemical staining in iBAT sections (A) (scale bar 20 μm, arrows indicate TH parenchymal fibers) and corresponding quantification of the number of TH fibers relative to 100 adipocytes (B) (Cdk4+/+ (n=6) and Cdk4-/- (n=6)). C Hematoxylin-eosin staining in scWAT showing multilocular adipocytes in Cdk4-/- (scale bar 50 μm). D Expression of thermogenic genes and brown adipocyte markers in scWAT of Cdk4+/+ (n=5) and Cdk4-/- (n=6) mice as assessed by RT-PCR. E-F Acute cold test (4°C) after treatment with the β-adrenergic antagonist propranolol (Prop) in Cdk4+/+ (n=7) and Cdk4-/- (n=6) animals or with vehicle (NaCl) (Cdk4+/+ (n=7) and Cdk4-/- (n=6)) (E) and corresponding quantification of the area under the curve (AUC).
a) Constructs CTM-GFP and mCTM-GFP.figf1(a) Constructs CTM-GFP and mCTM-GFP. (b) Quantification of CTM-GFP and mCTM-GFP relative to WT-GFP in HEK cells 24 h after individual transfections with WT-GFP, mCTM-GFP (n = 6) or CTM-GFP. Cells transfected with WT-GFP or CTM-GFP were treated without (no treatment; n = 13) or with serum deprivation (+ SD; n = 5; to enhance CMA activity) or with macroautophagy inhibitor 3-methyladenine (+ 3-MA; 10 mM; n = 5), proteasome inhibitor (+ MG132; 5 μM; n = 6), lysosome inhibitor (+ NH4Cl; 20 mM; n = 6) or pepstatin A (+ Pep A; 10 μM; n = 5). Top, representative immunoblots of cell lysates for GFP. Membranes reprobed for β-actin were used as a loading control. Bottom, means ± s.e.m. of relative protein levels, normalized to WT-GFP (arbitrarily set as 1; white bar); n represents the number of independent experiments from at least 4 separate cultures. One-way ANOVA with Fisher least significant difference test, F(12,73) = 20.939. ***P 0.001 versus WT-GFP (white bar); ΔΔΔP 0.001 relative to untreated CTM-GFP levels (gray bar). Full-length blots are presented in Supplementary Figure 9. (c) Representative confocal images of colocalization of GFP with the lysosome marker LAMP-1 in COS-7 cells transfected with either WT-GFP (n = 17) or CTM-GFP (n = 16). Scale bar, 20 μm.
Figure 1A RT-qPCR analysis of lincRNA-EPS transcripts in the BMDMs infected with VSV (MOI 1), SeV (MOI 1), or HSV-1 (MOI 5) for indicated time points. B RT-qPCR analysis of lincRNA-EPS transcripts in the BMDMs transfected with 1 μg/mL low molecular weight (LMW), high molecular weight (HMW) polyI:C, and polydA:dT for 6 h. C, D RT-qPCR analysis of lincRNA-EPS transcripts in the BMDMs stimulated with 500 U/mL IFN-α for different time points (C), or different concentrations for 2 h (D). E, F RT-qPCR analysis of lincRNA-EPS transcripts in the BMDMs stimulated with 500 U/mL IFN-β for different time points (E), or different concentrations for 2 h (F). G, H RT-qPCR analysis of lincRNA-EPS transcripts in the WT and Ifnar1-/- BMDMs transfected with 1 μg/mL polyI:C (LMW) for 6 h (G) and infected with SeV (MOI 1) for indicated time points (H). I BMDMs were pretreated with NF-κB inhibitor BAY11-7082 (1 μM) for 1 h and infected with VSV (MOI 1) for 6 h. The percentage of lincRNA-EPS transcripts downregulation in the VSV-infected group compared with the Mock group was calculated. J Cell nucleus and cytoplasm were separated from untreated (Mock) and VSV-infected iBMMs, RNA was extracted for RT-qPCR analysis and compared with Mock group.