Effect of Effect of lytic replication on EBV and cell gene expression
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA655689 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR12401446.fastq.gz | Fastqsanger.gz | |||
| SRR12401447.fastq.gz | Fastqsanger.gz | |||
| SRR12401448.fastq.gz | Fastqsanger.gz | |||
| SRR12401449.fastq.gz | Fastqsanger.gz | |||
| SRR12401450.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 6 |
Similar Datasets
Project description:The effect of Epstein Barr virus replication on cellular gene expression was studied using AGSiZ epithelial cells which are derived from a gastric carcinoma. The cell line is infected with a recombinant strain of EBV known as Akata BX-1. The cell line was further stably transduced with an inducible EBV Zta transactivator gene. When cells are treated with doxycycline, robust lytic replication of EBV is achieved. Cells made permissive for lytic replication in this manner were harvested for RNA suitable for deep sequencing at 24 and 48 hours post induction in parallel with cells that were mock induced with doxycycline to serve as a control for cells not undergoing EBV replication.
2021-04-15 | GSE155811 | GEO
Project description:Epstein-Barr virus nuclear antigen 1 (EBNA1) is essential for the replication and stable maintenance of the viral episome in infected cells. Here, we identify the SUMO E3 ligase PIAS1 as a key regulator of EBNA1 through site-specific SUMOylation. Our Chromatin-Immunoprecipitation Sequencing (ChIP-seq) analysis revealed that PIAS1 is enriched at the viral origin of plasmid replication (oriP), where it physically associates with EBNA1 and catalyzes its SUMOylation. Using mutational analysis, we identified three lysine residues on EBNA1 (K17, K75, and K241) as major SUMOylation sites. Disruption of these sites compromises EBNA1’s ability to restrict EBV lytic replication. In addition, both PIAS1 depletion and the disruption of EBNA1 SUMOylation lead to reduced retention of EBNA1-OriP-based EBV mini-replicon, indicating the importance of EBNA1 SUMOylation in viral episome maintenance. Together, these results uncover a conserved post-translational mechanism by which PIAS1-mediated SUMOylation modulates EBNA1 function and EBV episome maintenance and suggests a broader role for SUMOylation in viral latency, lytic replication and persistence.
2025-12-01 | GSE306456 | GEO
Project description:Most humans are infected with Epstein-Barr virus (EBV), a cancer-causing virus. While EBV generally persists silently in B lymphocytes, periodic lytic (re-)activation of latent virus is central to its life cycle and to most EBV-related diseases. However, a substantial fraction of EBV-infected B cells and tumor cells in a population is refractory to lytic activation. This resistance to lytic activation directly and profoundly impacts viral persistence and effectiveness of oncolytic therapy for EBV+ cancers. To identify the mechanisms that underlie susceptibility to EBV-lytic activation, we used host protein-expression profiling of separated-lytic and -refractory cells.
2016-04-27 | PXD001838 | Pride
Project description:To understand the changes in global transcriptomic landscape during the EBV lytic cycle reactivation from lymphoblastoid cell lines (LCLs), RNA-seq was performed. By examining the transcriptomic changes, we obtained valuable insights into the molecular events and regulatory mechanisms involved in EBV reactivation into lytic cycle replication. The study also enhances our knowledge of the complex interplay between EBV and the host cells during its lytic cycle.
2023-08-03 | GSE237484 | GEO
Project description:Infection with Epstein-Barr virus (EBV) usually results in asymptomatic infection in the pediatric population. In some pediatric patients, it can lead to infectious mononucleosis (IM) and may be complicated by malignant diseases such as hemophagocytic lymphohistiocytosis (HLH) and chronic active EBV infection (CAEBV). The traditional Chinese medicine (TCM) Sanyang Toujie Decoction (SYTJ) exerts a favorable therapeutic effect on IM associated with EBV infection. However, its active components and underlying mechanisms of action remain unclear. ObjectiveTo clarify the mechanisms of SYTJ against EBV infection in the treatment of pediatric IM by integrating multi-omics and molecular biology approaches. Study DesignWe collected serum samples from healthy children undergoing routine physical examinations, pediatric patients with IM, and pediatric IM patients after SYTJ treatment. An innovative strategy combining proteomics, metabolomics, and molecular biology was adopted to investigate the active components and mechanisms of action of SYTJ. We explored the anti-EBV targets, biological processes, and pathways of SYTJ at the metabolite and protein levels, and established an EBV lytic infection model for validation. ResultsA total of 1,424 chemical components were identified in the fingerprint of SYTJ. Multi-omics and systems biology analyses revealed that the pharmacological mechanisms of SYTJ involve 34 core proteins and 6 core differential metabolites, which are enriched in EBV infection-related key pathways including the Toll-like receptor signaling pathway, glycerophospholipid metabolism, and pentose phosphate pathway. Validation experiments demonstrated that SYTJ could inhibit the proliferation of RAJI and B95-8 cells, promote cell apoptosis, reduce the expression of EBV-EA in RAJI cells and EBV-VCA in B95-8 cells, and suppress EBV-DNA replication. In addition, SYTJ downregulated the mRNA and protein expression of BZLF1 and BMRF1 in B95-8 cells, inhibited EBV lytic replication, upregulated the expression of TOLLIP protein, and suppressed the TLR9/MYD88/NF-κB pathway. ConclusionSYTJ can reduce EBV lytic replication, upregulate TOLLIP protein expression, inhibit the TLR9/MYD88/NF-κB pathway, and alleviate the immune-inflammatory response in the body.
2025-12-07 | PXD071703 |
Project description:Lytic infection by the Epstein-Barr virus (EBV) poses numerous health risks, such as infectious mononucleosis and lymphoproliferative disorder. We demonstrate that JQ1 and other BET inhibitors block two different steps in the sequential cascade of the EBV life cycle: expression of the immediate-early gene BZLF1 and lytic genome replication. This represents a novel mode of action for antiviral drugs that may increase efficacy and decrease emergence of resistance. The ChIP-seq data below show that the BET proteins bind to both EBV lytic origins of replication.
2017-06-30 | GSE84213 | GEO
Project description:Lytic infection by the Epstein-Barr virus (EBV) poses numerous health risks, such as infectious mononucleosis and lymphoproliferative disorder. We demonstrate that JQ1 and other BET inhibitors block two different steps in the sequential cascade of the EBV life cycle: expression of the immediate-early gene BZLF1 and lytic genome replication. This represents a novel mode of action for antiviral drugs that may increase efficacy and decrease emergence of resistance. The sequenced total DNA data below show that JQ1 and I-BET cause a decrease in EBV genome replication after induction.
2017-06-30 | GSE84212 | GEO
Project description:Most humans are infected with Epstein-Barr virus (EBV), a cancer-causing virus. While EBV generally persists silently in B lymphocytes, periodic lytic (re-)activation of latent virus is central to its life cycle and to most EBV-related diseases. However, a substantial fraction of EBV-infected B cells and tumor cells in a population is refractory to lytic activation. This resistance to lytic activation directly and profoundly impacts viral persistence and effectiveness of oncolytic therapy for EBV+ cancers. To identify the mechanisms that underlie susceptibility to EBV-lytic activation, we used host protein-expression profiling of separated-lytic and -refractory cells.
2016-07-22 | MSV000079993 | MassIVE
Project description:Lytic infection by the Epstein-Barr virus (EBV) poses numerous health risks, such as infectious mononucleosis and lymphoproliferative disorder. We demonstrate that JQ1 and other BET inhibitors block two different steps in the sequential cascade of the EBV life cycle: expression of the immediate-early gene BZLF1 and lytic genome replication. This represents a novel mode of action for antiviral drugs that may increase efficacy and decrease emergence of resistance. The ChIP-seq data below show that the BET proteins bind to both EBV lytic origins of replication.
2017-06-30 | GSE98772 | GEO
Project description:Epstein-Barr virus (EBV) has a lifelong latency period after initial infection. Rarely, however, when the EBV immediate early gene BZLF1 is expressed by a specific stimulus, the virus switches to the lytic cycle to produce progeny viruses. We found that EBV infection reduced levels of various ceramide species in gastric cancer cells. As ceramide is a bioactive lipid implicated in the infection of various viruses, we assessed the effect of ceramide on the EBV lytic cycle. Treatment with C6-ceramide (C6-Cer) induced an increase in the endogenous ceramide pool and increased production of the viral product as well as BZLF1 expression. Treatment with the ceramidase inhibitor ceranib-2 induced EBV lytic replication with an increase in the endogenous ceramide pool. The glucosylceramide synthase inhibitor Genz-123346 inhibited C6-Cer-induced lytic replication. C6-Cer induced ERK1/2 and CREB phosphorylation, c-JUN expression, and accumulation of the autophagosome marker LC3B. Treatment with MEK1/2 inhibitor U0126 or autophagy initiation inhibitor 3-MA suppressed C6-Cer-induced EBV lytic replication. In contrast, the autophagosome-lysosome fusion inhibitor chloroquine induced BZLF1 expression. Transfection with siCREB reduced ERK1/2 phosphorylation and C6-Cer-induced BZLF1 expression. On the other hand, siJUN transfection did not affect BZLF1 expression. Our results show that increased endogenous ceramide and glycosyl ceramide (GlyCer) following C6-Cer treatment induce EBV lytic replication in gastric cancer cells via ERK1/2 and CREB phosphorylation and autophagosome accumulation.
2023-12-20 | MTBLS7649 | MetaboLights