Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Analysis of the early transcriptome signature of Nipah virus infection in primary endothelial cells

ABSTRACT: Nipah virus (NiV) is a recently emerged zoonotic Paramyxovirus that causes regular outbreaks in East Asia with mortality rate exceeding 75%. Major cellular targets of NiV infection are endothelial cells and neurons. To better understand virus-host interaction, we analysed the transcriptome profile of NiV infection in primary human umbilical vein endothelial cells. We found that NiV infection strongly induces genes involved in interferon response in endothelial cells. Among the top ten upregulated genes, we identified the chemokine CXCL10 (interferon-induced protein 10, IP-10), an important chemoattractant involved in the generation of inflammatory immune response and neurotoxicity.

ORGANISM(S): Homo sapiens

PROVIDER: GSE32902 | GEO | 2012/08/24

SECONDARY ACCESSION(S): PRJNA146579

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Analysis of the early transcriptome signature of Nipah virus infection in primary endothelial cells

Project description:Nipah virus (NiV) is a recently emerged zoonotic Paramyxovirus that causes regular outbreaks in East Asia with mortality rate exceeding 75%. Major cellular targets of NiV infection are endothelial cells and neurons. To better understand virus-host interaction, we analysed the transcriptome profile of NiV infection in primary human umbilical vein endothelial cells. We found that NiV infection strongly induces genes involved in interferon response in endothelial cells. Among the top ten upregulated genes, we identified the chemokine CXCL10 (interferon-induced protein 10, IP-10), an important chemoattractant involved in the generation of inflammatory immune response and neurotoxicity. We performed microarray gene expression profiling of NiV infected HUVEC cell (2 replicates) and of uninfected HUVEC cell (2 replicates).

2012-08-24 | E-GEOD-32902 | biostudies-arrayexpress

Analysis of the early transcriptome signature of infection of primary endothelial cells by Nipah virus vs. Nipah virus deleted for the expression of non-structural C protein

Project description:Nipah virus (NiV) is a highly pathogenic, negative strand RNA paramyxovirus that has recently emerged from flying foxes to cause serious human disease. To study the poorly-understood role of nonstructural NiV proteins in NiV pathogenesis, we generated recombinant viruse lacking the expression of accesory NiV C protein (NiVM-bM-^HM-^FC). To analyse the molecular basis of NiVM-bM-^HM-^FC attenuation we have used the gene microarray approach to study early changes of gene expression in infected primary human endothelial cells, which is a major cellular target of human NiV infection. We performed microarray gene expression profiling of NiV infected HUVEC cell (2 replicates), of uninfected HUVEC cell (2 replicates) and of NiVM-bM-^HM-^FC infected HUVEC cell (2 replicates).

2012-10-01 | E-GEOD-33133 | biostudies-arrayexpress

Analysis of the early transcriptome signature of infection of primary endothelial cells by Nipah virus vs. Nipah virus deleted for the expression of non-structural C protein

2012-10-01 | GSE33133 | GEO

ANTI-CD40 DENDRITIC CELL-TARGETING VACCINE INDUCES PROTECTIVE IMMUNITY AGAINST NIPAH DISEASE

Project description:Nipah virus (NiV) is an emerging paramyxovirus which causes severe respiratory illness and deathly encephalitis in humans.Improving the ability of vaccines to induce strong, cellular, and humoral immune responses, remains the challenge to respond to Nipah and future Henipavirus infections rapidly and efficiently. A CD40.NiV vaccine has been engineered by fusing to the anti-CD40 monoclonal Ab the ectodomain of the Nipah G protein (Bangladesh strain) and immunogenic and conserved NiV F and N peptides. In mice, CD40.NiV promotes poly-antigenic T cell responses and significantly improves anti-NiV G IgG responses compared to the non-targeted NiV G immunogenic protein, in terms of avidity and neutralization potency. Immunogenicity was confirmed in the AGM (African Green Monkey) model, with induction of cross-neutralizing sera against circulating NiV strains and Hendra virus (HeV). Challenge experiment using NiV-B strain demonstrated the high protective efficacy of the vaccine with 100% survival in vaccinated group as compared to 100% lethality in controls. Surviving animals did not exhibit NiV viral replication in the blood, organs and swabs suggesting a sterilizing immunity conferred by the CD40.NiV vaccine. Taken together, results obtained with CD40.NiV vaccine are highly promising in terms of breadth and viral efficacy against NiV.

2024-02-02 | GSE245374 | GEO

Analysis of Nipah virus replication and host proteome response patterns in differentiated porcine airway epithelial cells cultured at the air-liquid interface

Project description:Respiratory tract epithelium infection is considered crucial for airborne transmission of Nipah virus (NiV). Knowledge about infection dynamics and host responses to NiV infection in respiratory tract epithelia is scarce. Various studies in non-differentiated primary respiratory tract cells or cell lines indicate limitations in interferon responses. However, comprehensive studies determining complex reaction patterns in differentiated respiratory tract epithelia to understand efficient NiV replication and spread in swine populations are lacking. Here we characterized infection and spread of NiV in differentiated primary porcine bronchial epithelial cells (PBEC) cultivated at the air-liquid-interface (ALI). After initial infection of only a few apical cells, lateral spread for 12 days with disruption of the epithelium was observed without releasing substantial amounts of infectious virus from the apical or basal sides. Deep time course proteomics revealed pronounced upregulation of genes related to type I/II interferon (IFN), immunoproteasomal subunits, TAP-mediated peptide transport and MHC I antigen presentation, whereas spliceosomal factors were downregulated. We deduce a model in which NiV replication in pig bronchial epithelia is slowed by a potent and broad type I/II interferon host response with concurrent conversion from 26S proteasomal to immunoproteasomal antigen processing and improved MHC I presentation as a crucial step in adaptive immunity priming. Moreover, strong cytopathic effects observed in infected areas could reflect focal release of cell-associated NiV. Cell-associated NiV may translate into the source of efficient airborne viral spread in vivo with a high local infectious dose leading to high and fast spread of NiV throughout pig herds.

2023-05-10 | PXD032673 | Pride

Structure and antigenicity of divergent Henipavirus fusion glycoproteins

Project description:A novel henipavirus (HNV) named Langya virus (LayV) was isolated in human patients in China in August 2022. It is closely related to Mòjiāng virus (MojV) and represents the first instance of HNV zoonosis to humans outside of Nipah virus (NiV) and Hendra viruses (HeV). Within this work, mass spectrometry glycoproteomic analysis revealed that although the LayV F protein has reduced glycosylation compared to its NiV and HeV counterparts, a unique glycan was identified positioned at the DIII apex, shielding a previously identified site of vulnerability in NiV F.

2023-05-03 | PXD039898 | Pride

A proximity interactome assay for interaction of nipah virus F and G protein with the cellular protein

Project description:Nipah virus (NiV) is a highly lethal zoonotic virus with a potential large-scale outbreak, which poses a great threat to world health and security. Cell entry is the first step in viral infection, and the entry of NiV into host cells is inseparable from the attachment (G) and fusion (F) glycoproteins. To discover the host factors potentially involved in the entry of NiV into host cells, we systematically studied the interaction of NiV F and G proteins with host proteins using proximity labeling methods.

2023-12-22 | PXD048109 |

The Sequence Basis for Selectivity of Ephrin-B2 for Eph Receptors and Pathogenic Henipavirus G Glycoproteins [EFNB2-D62Q DEEP MUTAGENESIS]

Project description:Ephrin-B2 (EFNB2) is a ligand for six Eph receptors in humans and also functions as a cell entry receptor for several henipaviruses, which are zoonotic viruses with pandemic potential. Two such viruses, Nipah (NiV) and Hendra (HeV), are highly pathogenic in humans yet do not have any widely approved virus-specific therapeutics or vaccines. Soluble Fc-fusions of EFNB2 (sEFNB2-Fc) are known to bind the attachment glycoprotein G of both viruses and inhibit viral infection of cells. However, the potential of sEFNB2-Fc as a neutralizing agent in vivo is hindered by its binding activity to native Eph receptors. Therefore, using deep mutagenesis, variants of EFNB2 at cell surface are identified with increased binding to the soluble head domain of NiV-G over soluble Fc-fusions of the extracellular domains of Eph receptors. Specificity mutations for NiV-G are found primarily at the binding interface, especially around the G-H binding loop. The mutational landscape offers a preliminary blueprint for engineering sEFNB2-Fc variants with high specificity and affinity for potent neutralization of henipaviruses.

2023-06-12 | GSE234214 | GEO

The Sequence Basis for Selectivity of Ephrin-B2 for Eph Receptors and Pathogenic Henipavirus G Glycoproteins [EFNB2 DEEP MUTAGENESIS]

2023-06-12 | GSE234213 | GEO

Interferon-γ inhibition of Ebola virus infection [Alveolar macrophage]

Project description:Episodic Ebola virus (EBOV) outbreaks, such as the current one in West Africa, emphasize the critical need for novel antivirals against this highly pathogenic virus. Here, we demonstrate that interferon gamma (IFNγ) prevents morbidity and mortality associated with EBOV infection when administered to mice either 24 hours prior to or 2 hours following EBOV infection. Microarray studies with IFNγ-stimulated human macrophages identified novel interferon-stimulated genes (ISGs) that inhibit EBOV infection upon ectopic expression. IFNγ treatment reduced viral RNA levels in macrophages to a similar degree as cells treated with the protein synthesis inhibitor, cycloheximide, suggesting that IFNγ treatment inhibits genome replication. As IFNγ treatment robustly protects mice against EBOV infection, we propose that this FDA-approved drug may serve as a useful prophylactic or therapeutic strategy during EBOV outbreaks, contributing to the currently limited arsenal of filovirus antivirals.

2015-10-20 | GSE64995 | GEO

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