Homo sapiens
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: PRJNA126155 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Proteomic analysis of cytokines in unstimulated oropharyngeal secretions. Epstein-barr virus (EBV) is a type 1 carcinogen which causes many cancers in humans. Here we explored the cytokine involvement of the EBV replication process in the oropharynx. Cytokine interactomic profiles were geneerated to understand the involved signalling pathways in HIV infected group and the healthy group. Proteome profilers were used to understand the major cytokine expression levels that are related to infection and immune regulation. We analyzed unstimulated oropharyngeal samples (UOPS) from 42 healthy subjects and 72 HIV positive subjects using the R & D Proteome Profiler array panels. No techinical replicates were performed. 14 samples in HIV group without therapy (NHAART group); 58 HIV patients with highly active antiretroviral therapy (HAART group); 42 samples in healthy group
2010-04-15 | E-GEOD-21339 | ArrayExpress
Project description:Proteomic analysis of cytokines in unstimulated oropharyngeal secretions. Epstein-barr virus (EBV) is a type 1 carcinogen which causes many cancers in humans. Here we explored the cytokine involvement of the EBV replication process in the oropharynx. Cytokine interactomic profiles were geneerated to understand the involved signalling pathways in HIV infected group and the healthy group. Proteome profilers were used to understand the major cytokine expression levels that are related to infection and immune regulation. Overall design: We analyzed unstimulated oropharyngeal samples (UOPS) from 42 healthy subjects and 72 HIV positive subjects using the R & D Proteome Profiler array panels. No techinical replicates were performed. 14 samples in HIV group without therapy (NHAART group); 58 HIV patients with highly active antiretroviral therapy (HAART group); 42 samples in healthy group
2010-04-15 | GSE21339 | GEO
Project description:MicroRNAs (miRNAs) are a class of small RNA molecules previously known to function as post-transcriptional regulators in multiple cellular processes. Here, we show that a human cellular miRNA, hsa-miR-155, can regulate the latent replication origin (oriP) of Epstein-Barr virus (EBV) by competing with Epstein-Barr nuclear antigen 1 (EBNA-1) for direct binding to the dyad symmetry (DS) sequence on the oriP, and thus regulate the function of the DNA replication origin. When this direct binding was abolished by introducing a mutation into the hsa-miR-155 or DS sequence, replication resumed. Furthermore, endogenous hsa-miR-155 could target specifically to the EBV genomic replication origin in EBV type I-latently infected cells and regulate the viral DNA replication. Our discovery represents a hitherto undiscovered and important function of miRNA for the control of DNA replication, and demonstrates a probable mechanism of how this can be achieved using the latent replication origin of EBV. Overall design: In this sequencing, miR-155, miR-3117 and miR-control (based on miR-67) were used to evaluate the targeting sequence in DS element of EBV.
| GSE89088 | GEO
Project description:The human gamma herpesvirus Epstein-Barr virus, infects most adults and is an important contributor to the development of many types of cancer. Essential contributions of viral genes to replication are known but the potential contributions of cell genes to viral replication are less well delineated. A key player is the viral protein Zta (BZLF1, ZEBRA, Z). This sequence-specific DNA-binding protein can disrupt viral latency by driving the transcription of target genes and by interacting with the EBV lytic origin of replication. Here we used an unbiased approach to identify the Zta-interactome in cells derived from a Burkitt’s lymphoma. Isolating Zta and associated proteins from Burkitt’s lymphoma cells undergoing EBV replication, followed by Tandem Mass Tag (TMT) mass spectrometry resulted in the identification of forty-four viral and cellular proteins in the Zta interactome. Of these two were known targets of Zta. The association of Zta with Hsc70 and the contribution that Hsc70 plays to EBV replication mirrors a contribution from HSP70 family members to the replication of other herpesviruses. Conversely, the association of Zta with NFATc2 has no known parallels for other herpesviruses. Zta attenuates the activity of an NFAT-dependent promoter, which shows a potential for dampening the expression of genes regulated by calcium-dependent signal transduction. Indeed, Zta has the ability to affect a feed-back loop limiting its own expression, which would aid viral replication by preventing the toxic effects of Zta overexpression.
2019-06-06 | PXD013727 | Pride
Project description:Epstein Barr virus (EBV) replication contributes to multiple human diseases, including infectious mononucleosis, nasopharyngeal carcinoma, B-cell lymphomas, and oral hairy leukoplakia. We performed systematic quantitative analyses of temporal changes in host and EBV proteins during lytic replication to gain novel insights into virus-host interactions, using conditional Burkitt lymphoma models of type I and II EBV infection. We quantified profiles of >8000 cellular and 69 EBV proteins, including >500 plasma membrane proteins, providing temporal views of the lytic B-cell proteome and EBV virome. Our approach revealed EBV-induced remodelling of cell cycle, innate and adaptive immune pathways, including upregulation of the complement cascade and proteasomal degradation of the B-cell receptor complex, conserved between EBV types I and II. Cross-comparison with proteomic analyses of human cytomegalovirus infection and of a Kaposi sarcoma associated herpesvirus immunoevasin identified host factors targeted by multiple herpesviruses. Our results provide an important resource for studies of EBV replication.
2018-10-19 | PXD008752 | Pride
Project description:Epstein Barr virus (EBV) replication contributes to multiple human diseases, including infectious mononucleosis, nasopharyngeal carcinoma, B-cell lymphomas, and oral hairy leukoplakia. We performed systematic quantitative analyses of temporal changes in host and EBV proteins during lytic replication to gain novel insights into virus-host interactions, using conditional Burkitt lymphoma models of type I and II EBV infection. We quantified profiles of >8000 cellular and 69 EBV proteins, including >500 plasma membrane proteins, providing temporal views of the lytic B-cell proteome and EBV virome. Our approach revealed EBV-induced remodelling of cell cycle, innate and adaptive immune pathways, including upregulation of the complement cascade and proteasomal degradation of the B-cell receptor complex, conserved between EBV types I and II. Cross-comparison with proteomic analyses of human cytomegalovirus infection and of a Kaposi sarcoma associated herpesvirus immunoevasin identified host factors targeted by multiple herpesviruses. Our results provide an important resource for studies of EBV replication.
2017-05-19 | PXD006317 | Pride
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. Overall design: ChIP-seq and input from untreated and JQ1 treated MutuI cells
| 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 ChIP-seq data below show that the BET proteins bind to both EBV lytic origins of replication. Overall design: Brd4 ChIP-seq in latent LGNFR- and reactivated LGNFR+ Akata-ZTA cells pre-treated with acyclovir and either JQ1 or vehicle
| GSE98773 | GEO
Project description:Epstein-Barr virus (EBV) reactivation in latently infected B cells is essential for persistent infection and B cell receptor (BCR) activation is a physiologically relevant stimulus for EBV reactivation. Post-translational modifications, such as phosphorylation and ubiquitination, are known to be regulated by antigen binding to BCR within minutes. However, a detailed understanding of the signaling alterations at later time when EBV is being actively replicated remains elusive. To gain insights into BCR activation-mediated reprogramming of the cellular environment in both Akata-BX1 (EBV+) and Akata-4E3 (EBV-) B cells, we utilized a 3-plex stable isotope labeling by amino acid in cell culture (SILAC)-based quantitative proteomic approach to monitor the dynamic changes of protein ubiquitination during the course of immunoglobulin G (IgG) cross-linking of BCRs. We observed temporal alterations in the level of ubiquitination on approximately 150 sites in both Akata-BX1 (EBV+) and Akata-4E3 (EBV-) B cells post-IgG cross-linking compared with no cross-linking controls, with the majority of protein ubiquitination down-regulated. Our analysis revealed that IgG cross-linking plays a major role in the regulation of protein ubiquitination in both EBV+ and EBV- B cells. Bioinformatic analyses of up-regulated ubiquitination events revealed significant enrichment of proteins involved in RNA processing. Among the down-regulated ubiquitination events are proteins enriched in apoptosis and the ubiquitin-proteasome pathway. The comparative and quantitative studies provide a foundation for further understanding how BCR activation regulates cellular protein ubiquitination and how EBV utilizes or subverts BCR engagement-mediated changes to facilitate viral replication.
2017-02-02 | PXD004562 | Pride