Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Effect of CD154:CD11b blockade on antigen-specific CD8 T cell response to murine Epstein-Barr virus infection

ABSTRACT: Effect of CD154:CD11b blockade on antigen-specific CD8 T cell response to murine Epstein-Barr virus infection

PROVIDER: PRJNA1244744 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR32939936_1.fastq.gz	Fastqsanger.gz
	SRR32939936_2.fastq.gz	Fastqsanger.gz
	SRR32939937_1.fastq.gz	Fastqsanger.gz
	SRR32939937_2.fastq.gz	Fastqsanger.gz
	SRR32939938_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 20

Similar Datasets

Effect of CD154:CD11b blockade on antigen-specific CD8 T cell response to murine Epstein-Barr virus infection

Project description:CD154 is a promising target for immunosuppression in transplantation, autoimmunity, and inflammatory diseases. We previously identified CD11b as a novel alternate receptor for CD154 during alloimmunity. However, the impact of specific CD154:CD11b blockade on immune responses to infection has not been well characterized. Here, we have shown that in contrast to its immunosuppressive effect on graft-specific CD8+ T cells, CD154:CD11b blockade unexpectedly improved both the quantity and quality of murine herpesvirus-68 (MHV)-specific CD8+ T cells as measured by an increase in tetramer-positive KLRG1loCD127hi memory precursor effector cells (MPECs). RNAseq of antigen-specific CD8+ T cells identified using an MHV68-specific MHC tetramer reveals specific pathways altered following cM7 treatment during MHV68 infection, including transcripts associated with T cell activation and survival. The differential effect of CD154:CD11b blockade on graft-vs. virus-specific CD8+ T cells was underpinned by differences in phospho-S6 downstream of mTORC1, however differential expression of key transcription factors Eomes and TCF-1 was dictated by the type of antigen stimulus. These data demonstrate that priming conditions play an important role in determining the outcome of immunotherapy and suggest that specific inhibition of CD154:CD11b interactions could be effective for suppressing alloimmune responses while maintaining protective immunity to minimize infectious complications following transplantation.

2025-04-11 | GSE293467 | GEO

PLK1 phosphorylation of Epstein-Barr virus nuclear antigen 2

Project description:The Epstein-Barr virus nuclear antigen 2 (EBNA2) initiates and maintains the proliferation of infected B cells. In search of additional cellular strategies, that control EBNA2 function, we have performed a label-free mass spectrometry-based quantification of cellular proteins in EBNA2 immuno-precipitates and found polo-like kinase 1 (PLK1) to be bound to EBNA2. EBNA2/PLK1 complex formation is strongly enforced by EBNA2 S379 phosphorylation catalyzed by the mitotic CYCLIN B/CDK1 complex.

2021-08-22 | PXD022970 | Pride

Epstein Barr Virus Nuclear Antigen 3C binds to BATF/IRF4/SPI1 sites and represses CDKN2A by recruiting Sin3A

Project description:We report the application of ChIP Seq to study the Epstein Barr Virus Nuclear Antigen 3C, an essential transcriptional regulator involved in the transformation of Resting B Lymphocytes to the immortalized Lymphoblast Cell Lines Examination of viral and cellular transcription factors in 1 type of cell line

2013-12-22 | E-GEOD-52632 | biostudies-arrayexpress

Epstein Barr Virus Nuclear Antigen 3C binds to BATF/IRF4/SPI1 sites and represses CDKN2A by recruiting Sin3A

2013-12-22 | GSE52632 | GEO

Ganciclovir Plus Arginine Butyrate in Treating Patients With Cancer or Lymphoproliferative Disorders Associated With the Epstein Barr Virus

Project description:RATIONALE: The Epstein Barr virus can cause cancer and lymphoproliferative disorders. Ganciclovir is an antiviral drug that acts against the Epstein Barr virus. Arginine butyrate may make virus cells more sensitive to ganciclovir. Combining ganciclovir and arginine butyrate may kill more Epstein Barr virus cells and tumor cells. PURPOSE: Phase I trial to study the effectiveness of arginine butyrate plus ganciclovir in treating patients who have cancer or lymphoproliferative disorders that are associated with the Epstein Barr virus.

| 2005372 | ecrin-mdr-crc

Identifying Sites Bound by Epstein Barr Nuclear Antigen 1 (EBNA1) in the Human Genome

2009-01-01 | GSE13315 | GEO

Identifying Sites Bound by Epstein Barr Nuclear Antigen 1 (EBNA1) in the Human Genome

Project description:Epstein-Barr virus (EBV) is a ubiquitous gammaherpes virus that establishes a life-long latency in over 90% of the world's population. Epstein Barr Nuclear Antigen 1, EBNA1, is the only viral protein consistently detected in all viral latency programs, as well as in all forms of EBV-associated malignancies. EBNA1 plays critical roles in the viral life cycle by fostering the replication and maintenance of the extrachromosomal viral genome as well as enhancing transcription from multiple viral promoters. Using chromatin immunoprecipitation and human promoter microarrays (an analysis termed ChIP-chip) we found that EBNA1 binds site specifically within multiple human promoters. To determine whether EBNA1â??s binding to these promoters perturbed gene expression, we measured the levels of cellular mRNAs by microarrays when EBNA1 was inhibited by a dominant negative derivative of EBNA1 (DomNeg1). Keywords: viral regulation of cellular genes We analysed mRNA expression from the EBV-positive lymphoblastoid cell line 721 transduced with either a control (empty) retroviral vector or a DomNeg1-encoding retroviral vector. For ChIP-chip, DNA from immunoprecipitated chromatin using a anti-EBNA1 antibody (IH4) along with total chromatin was hybridized to a Nimblegen human promoter arrays (CHAR0150-HP2). A single ChIP-chip experiment was performed with DNAs pooled equally from three independent ChIP experiments.

2010-05-14 | E-GEOD-13315 | biostudies-arrayexpress

The Epstein Barr virus circleRNAome

Project description:The Epstein Barr virus circleRNAome

| PRJNA479852 | ENA

Genome-Wide Analysis of Host-Chromosome Binding Sites for Epstein-Barr Virus Nuclear Antigen 1 (EBNA1)

Project description:The Epstein-Barr Virus (EBV) Nuclear Antigen 1 (EBNA1) protein is required for the establishment of EBV latent infection in proliferating B-lymphocytes. EBNA1 is a multifunctional DNA-binding protein that stimulates DNA replication at the viral origin of plasmid replication (OriP), regulates transcription of viral and cellular genes, and tethers the viral episome to the cellular chromosome. EBNA1 also provides a survival function to B-lymphocytes, potentially through its ability to alter cellular gene expression. Chromatin-immunoprecipitation (ChIP) combined with massively parallel deep-sequencing (ChIP-Seq) was used to identify cellular sites bound by EBNA1. Sites identified by ChIP-Seq were validated by conventional real-time PCR, and ChIP-Seq provided quantitative, high-resolution detection of the known EBNA1 binding sites on the EBV genome at OriP and Qp. We identified at least one cluster of unusually high-affinity EBNA1 binding sites on chromosome 11, between the divergent FAM55D and FAM55B genes. A consensus for all cellular EBNA1 binding sites is distinct from those derived from the known viral binding sites, suggesting that some of these sites are indirectly bound by EBNA1. We conclude that EBNA1 can interact with a large number of cellular genes and chromosomal loci in latently infected cells, but that these sites are likely to represent a complex ensemble of direct and indirect EBNA1 binding sites. Study of Epstein-Barr virus (EBV)

2011-07-16 | E-GEOD-30709 | biostudies-arrayexpress

Antibodies against the mono-methylated Arginine-Glycine repeat (MMA-RG) of the Epstein-Barr virus nuclear antigen 1 (EBNA1) identify potential cellular proteins targeted in viral transformation

Project description:The viral nuclear antigen 1 (EBNA1) of Epstein Barr (EBV) features two functionally redundant Arginine-Glycine (RG) repeats that contain symmetrically and asymmetrically di-methylated (SDMA/ADMA) and also mono-methylated (MMA) Arginine residues. We generated mouse monoclonal antibodies against the mono-methylated RG-repeat between aa 328-377. In addition to detect MMA-EBNA1, we aimed at the identification of cellular proteins that are bound to MMA-modified EBNA1 in EBV-positive Raji cells.

2025-03-05 | PXD051181 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data