Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

RNA Sequencing of dendritic cells treated with glycan-costumed virus-like particles

ABSTRACT: RNA Sequencing of dendritic cells treated with glycan-costumed virus-like particles

PROVIDER: PRJNA1055489 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR27321663_1.fastq.gz	Fastqsanger.gz
	SRR27321663_2.fastq.gz	Fastqsanger.gz
	SRR27321664_1.fastq.gz	Fastqsanger.gz
	SRR27321664_2.fastq.gz	Fastqsanger.gz
	SRR27321665_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 30

Similar Datasets

RNA Sequencing of dendritic cells treated with glycan-costumed virus-like particles

Project description:We engineered a glycan-costumed virus-like particle (VLP) vaccine that delivers programmable peptide antigens to induce tumor-specific cellular immunity in vivo. VLPs encapsulating TLR7 agonists were decorated with a synthetic mannose-derived ligand (VLP-Man-OvaI/II) that selectively engages the lectin DC-SIGN. Lectin-TLR7 dual engagement induced robust DC activation and type 1 cellular immunity, whereas VLPs lacking this key DC-SIGN ligand (VLP-PE-OvaI/II) failed to promote DC-mediated cellular responses. We performed bulk RNA-seq experiments on moDCs treated with VLP-Man-OvaI/II and VLP-PE-OvaI/II or unstimulated control moDCs. A total of 486 genes were differentially expressed after treatment with VLP-Man-OvaI/II vs. VLP-PE-OvaI/II (log2FC >1.5 and p<0.05). The significantly upregulated genes included CXCL1, CXCL5, ISG15, IL6, CCL4, ISG20, and SOCS3, all of which are implicated in the TLR7 downstream signaling pathway, suggesting a higher extent of TLR7 activation with the VLP-Man-OvaI/II. Gene set enrichment analysis (GSEA) between VLP-Man-OvaI/II- and VLP-PE-OvaI/II-treated moDCs revealed that hallmark DC activation pathways were also upregulated in VLP-Man-OvaI/II-treated DCs, including pathways related to IFN-a, IFN-g, and TNF-a signaling via nuclear factor-κB (NF-kB). These data give insight into how lectin binding with glycan-costumed VLPs can be employed to reprogram immunity.

2024-09-06 | GSE251818 | GEO

Analysis of expression of genes involved in glycan and GBP synthesis in control and differentiated dendritic cells

Project description:Analysis of expression of genes involved in glycan and glycan-binding molecule synthesis in dendritic cells.

2011-04-29 | GSE28922 | GEO

GNPS - Mouse dendritic cell metabolome response to wild-type West Nile virus (WNV-NY)

Project description:Metabolomic data from 2x105 dendritic cells; West Nile Virus treated, Untreated, Mockulum treated; Time points 0, 4, 8, 12, 24; Two biological replicates

2015-06-11 | MSV000079149 | GNPS

GNPS - Mouse dendritic cell lipidome response to wild-type West Nile virus (WNV-NY)

Project description:Lipidomic data from 2x105 dendritic cells; West Nile Virus treated, Untreated, Mockulum treated; Time points 0, 4, 8, 12, 24; Two biological replicates

2015-06-11 | MSV000079150 | GNPS

Analysis of expression of genes involved in glycan and GBP synthesis in control and differentiated dendritic cells

Project description:Analysis of expression of genes involved in glycan and glycan-binding molecule synthesis in dendritic cells. Gene expression patterns for unstimulated dendritic cells, macrophages, and monocytes were compared. Also, gene expression patterns for dendritic cells and macrophages stimulated with LPS for 4 and 18 hours were compared to unstimulated cells. Three replicate samples of RNA were taken from human cells, one sample per donor. Samples were prepared and hybridized to the GLYCOv3 array.

2011-04-29 | E-GEOD-28922 | biostudies-arrayexpress

Mouse dendritic cell proteome response to wild-type West Nile virus (WNV-NY)

Project description:Proteomics data from 2x105 dendritic cells; West Nile Virus treated, Untreated, Mockulum treated; Time points 0, 4, 8, 12, 24; Two biological replicates

2015-06-11 | MSV000079148 | MassIVE

Mouse dendritic cell metabolome response to wild-type West Nile virus (WNV-NY)

Project description:Metabolomic data from 2x105 dendritic cells; West Nile Virus treated, Untreated, Mockulum treated; Time points 0, 4, 8, 12, 24; Two biological replicates

2015-06-11 | MSV000079149 | MassIVE

Mass spectrometric characterization of HSV-1 L-particles from human dendritic cells and BHK21 cells and analysis of their functional role

Project description:Herpes simplex virus type 1 (HSV-1) is a very common human pathogenic virus among the world’s 12 population. The lytic replication cycle of HSV-1 is, amongst others, characterized by a tripartite viral 13 gene expression cascade, the assembly of nucleocapsids involving their subsequent nuclear egress, 14 tegumentation, re-envelopment and the final release of progeny viral particles. During productive 15 infection of a multitude of different cell types, HSV-1 generates not only infectious heavy (H-) 16 particles, but also non-infectious light (L-) particles, lacking the capsid. In monocyte-derived mature 17 dendritic cells (mDCs), HSV-1 causes a non-productive infection with the predominant release of L-18 particles. Until now, the generation and function of L-particles is not well understood, however, they 19 are described as factors transferring viral components to the cellular microenvironment. To obtain 20 deeper insights into the L-particle composition, we performed a mass-spectrometry-based analysis of 21 L-particles derived from HSV-1-infected mDCs or BHK21 cells and H-particles from the latter one. 22 In total, we detected 63 viral proteins in both H- and L-particle preparations derived from HSV-1-23 infected BHK21 cells. In L-particles from HSV-1-infected mDCs we identified 41 viral proteins 24 which are differentially distributed compared to L-particles from BHK21 cells. In this study, we 25 present data suggesting that L-particles modify mDCs and suppress their T cell stimulatory capacity. 26 Due to the plethora of specific viral proteins incorporated into and transmitted by L-particles, it is 27 tempting to speculate that L-particles manipulate non-infected bystander cells for the benefit of the 28 virus.

2021-09-09 | PXD020845 | Pride

Mass spectrometric characterization of HSV-1 L-particles from human dendritic cells and BHK21 cells and analysis of their functional role Part B

2021-09-09 | PXD020846 | Pride

Targeting host O-linked glycan biosynthesis affects Ebola virus replication efficiency and reveals differential GalNAc-T acceptor site preferences on the Ebola virus glycoprotein

Project description:Ebola virus glycoprotein is one of the most heavily O-glycosylated viral envelope glycoproteins. The glycoprotein possesses a large mucin-like domain responsible for the cytopathic effect on infected cells, yet its structure or potential role in early entry events is poorly defined. To understand the importance of O-glycans and the individual O-glycosylation sites for viral infectivity, we performed a comprehensive characterization of site-specific glycosylation governed by the three key GalNAc-transferases, GalNAc-T1, -T2, and -T3, initiating O-glycan biosynthesis. Using TMT isobaric labelling we performed quantitative differential O-glycoproteomics on proteins produced in wild type HEK293 cells and cell lines ablated for each of the three GalNAc-Ts, as well as compared it to patterns on wild type virus-like particles. In total we found 38 and 41 O-glycosites on virus like particle-derived and recombinant GP, respectively, with well correlated sites and site-specific structures. Examination of the isoform-specific glycosylation demonstrate selective initiation of a subset of O-glycosites by each enzyme, with GalNAc-T1 having the largest contribution. We next demonstrate that O-linked glycan truncation and perturbed initiation retarded the production of viral particles and decreased infectivity of progeny virus. This work represents a comprehensive site-specific analysis of EBOV GP and sheds light on differential regulation of EBOV GP glycosylation initiated by host GalNAc-Ts. Together with the effect on viral propagation it opens prospective avenues for tailored intervention approaches and means for modulating immunogen O-glycan density.

2024-04-29 | PXD036213 | 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