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Genome-wide analysis of gene expression in human macrophages in response to different stimuli

ABSTRACT: Analysis of gene expression in macrophages infected with influenza A virus or non-infected and treated with the saliphenylhalamide, obatoclax, expressing wild type NS1 protein or its mutant R38A, K41A. The hypothesis tested was that R38 and K41 residues within viral NS1 protein are essential for transctiptional control of cellluar gene expression. Cells were infected with influenza A/WSN/33 viruses expressing wild type NS1 protein (WT), its R38A, K41A mutant (RK/AA) or non-infected (Mock)

ORGANISM(S): Homo sapiens

PROVIDER: GSE66015 | GEO | 2015/02/18

SECONDARY ACCESSION(S): PRJNA275674

REPOSITORIES: GEO

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Genome-wide analysis of gene expression in human macrophages in response to different stimuli

Project description:Analysis of gene expression in macrophages infected with influenza A virus or non-infected and treated with the saliphenylhalamide, obatoclax, expressing wild type NS1 protein or its mutant R38A, K41A. The hypothesis tested was that R38 and K41 residues within viral NS1 protein are essential for transctiptional control of cellluar gene expression. Cells were infected with influenza A/WSN/33 viruses expressing wild type NS1 protein (WT), its R38A, K41A mutant (RK/AA) or non-infected (Mock) Total RNA isolated from macrophages 8 hours post stimuation.

2015-02-18 | E-GEOD-66015 | biostudies-arrayexpress

Genome-wide analysis of gene expression in human macrophages in response to infection with recombinant A/WSN/33 influenza A viruses expressing wild type NS1 protein or its mutant R38A, K41A. [macrophages]

Project description:Analysis of gene expression in human macrophages infected with influenza A viruses expressing wild type NS1 protein or its mutant R38A, K41A. The hypothesis tested was that R38 and K41 residues within viral NS1 protein are essential fro transctiptional control of cellluar gene expression. Cells were infected with influenza A/WSN/33 viruses expressing wild type NS1 protein (WT), its R38A, K41A mutant (RK/AA) or non-infected (Mock)

2015-02-07 | GSE65702 | GEO

Genome-wide analysis of gene expression in human macrophages in response to infection with recombinant A/WSN/33 influenza A viruses expressing wild type NS1 protein or its mutant R38A, K41A. [RPE]

Project description:Analysis of gene expression in human retinal pigment epithelium cell line (RPE) infected with influenza A viruses expressing wild type NS1 protein or its mutant R38A, K41A. The hypothesis tested was that R38 and K41 residues within viral NS1 protein are essential fro transctiptional control of cellluar gene expression. Cells were infected with influenza A/WSN/33 viruses expressing wild type NS1 protein (WT), its R38A, K41A mutant (RK/AA) or non-infected (Mock)

2015-02-07 | GSE65699 | GEO

2015-02-07 | E-GEOD-65702 | biostudies-arrayexpress

Genome-wide analysis of gene expression in human macrophages in response to infection with recombinant A/WSN/33 influenza A viruses expressing wild type NS1 protein or its mutant R38A, K41A. [RPE]

2015-02-07 | E-GEOD-65699 | biostudies-arrayexpress

Genome-wide analysis of gene expression in human macrophages in response to infection with influenza A viruses expressing full length or truncated non-structural protein NS1.

Project description:Analysis of gene expression in human macrophages infected with influenza A viruses expressing full length or truncated NS1 protein. The hypothesis tested was that C-terminal truncations of viral NS1 protein attenuate the capability of NS1 to limit activation of host antiviral and immune response genes. Cells were infected with influenza A/WSN/33 viruses expressing wild type NS1 protein (WSN-230), NS1 protein of 220 aa long (WSN-220) and NS1 protein of 202 aa long (WSN-202) on non-infected (Mock)

2014-10-08 | GSE62127 | GEO

Genome-wide analysis of gene expression in human macrophages in response to infection with influenza A viruses expressing full length or truncated non-structural protein NS1.

2014-10-08 | E-GEOD-62127 | biostudies-arrayexpress

The interaction of influenza A NS1 and cellular TRBP protein modulates the function of RNA interference machinery

Project description:Influenza A virus (IAV), one of the most prevalent respiratory diseases, causes pandemics around the world. The multifunctional non-structural protein 1 (NS1) of IAV is a viral antagonist that suppresses host antiviral response. However, the mechanism by which NS1 modulates the RNA interference (RNAi) pathway remains unclear. Here, we identified interactions between NS1 proteins of Influenza A/PR8/34 (H1N1; IAV-PR8) and Influenza A/WSN/1/33 (H1N1; IAV-WSN) and Dicer’s cofactor TAR-RNA binding protein (TRBP). We found that the N-terminal RNA binding domain (RBD) of NS1 and the first two domains of TRBP protein mediated this interaction. Furthermore, two amino acid residues (Arg at position 38 and Lys at position 41) in NS1 were essential for the interaction. We generated TRBP knockout cells and found that NS1 instead of NS1 mutants (two-point mutations within NS1, R38A/K41A) inhibited the process of microRNA (miRNA) maturation by binding with TRBP. PR8-infected cells showed masking of short hairpin RNA (shRNA)-mediated RNAi, which was not observed after mutant virus-containing NS1 mutation (R38A/K41A, termed PR8/3841) infection. Moreover, abundant viral small interfering RNAs (vsiRNAs) were detected in vitro and in vivo upon PR8/3841 infection. We identify, for the first time, the interaction between NS1 and TRBP that affects host RNAi machinery.

2022-04-15 | GSE189776 | GEO

mRNA display with library of even-distribution reveals cellular interactors of influenza virus NS1

Project description:The interactome of Influenza (A/WSN/33) NS1 protein (WT and D92Y mutant) was identifiedy by AP-MS.

2021-09-07 | PXD018377 | Pride

Suppression of the antiviral response by an influenza "histone mimic"

Project description:Viral infection is commonly associated with virus-driven hijacking of host proteins. We describe a novel mechanism by which influenza virus impacts host cells through the interaction of influenza NS1 protein with the infected cell epigenome. We show that the NS1 protein of influenza A H3N2 target the transcription elongation PAF1 complex (hPAF1C). We demonstrate that binding of NS1 to hPAF1C results in suppression of hPAF1C-mediated transcriptional elongation. In the following data sets, we show that NS1 colocalizes with hPAF1 on the chromatin of infected cells and that siRNA-mediated reduction of hPAF1 expression results in reduced recruitment of NS1 to the chromatin.

2013-07-01 | GSE35774 | GEO

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