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The NS1 protein of influenza A virus suppresses interferon-regulated activation of antigen-presentation and immune-proteasome pathways

ABSTRACT: The NS1 protein of influenza virus counters host antiviral defences primarily by antagonizing the type I interferon (IFN) response. Both the N-terminal dsRNA-binding domain and the C-terminal effector domain are required for optimal suppression of host responses during infection. To better understand the regulatory role of the NS1 effector domain, we used an NS1-truncated mutant virus derived from human H1N1 influenza isolate A/Texas/36/91 (Tx/91) and assessed global transcriptional profiles from two independent human lung cell-culture models.

ORGANISM(S): Homo sapiens

PROVIDER: GSE39200 | GEO | 2012/07/10

SECONDARY ACCESSION(S): PRJNA170197

REPOSITORIES: GEO

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The NS1 protein of influenza A virus suppresses interferon-regulated activation of antigen-presentation and immune-proteasome pathways

Project description:The NS1 protein of influenza virus counters host antiviral defences primarily by antagonizing the type I interferon (IFN) response. Both the N-terminal dsRNA-binding domain and the C-terminal effector domain are required for optimal suppression of host responses during infection. To better understand the regulatory role of the NS1 effector domain, we used an NS1-truncated mutant virus derived from human H1N1 influenza isolate A/Texas/36/91 (Tx/91) and assessed global transcriptional profiles from two independent human lung cell-culture models. Primary human tracheobronchial epithelial (HTBE) cells were washed and infected with 4×10^6 p.f.u. Tx/91 or Tx/91 NS1 : 1–126 viruses per filter (m.o.i. of 20) for 1 h at 37 °C. Three replicate wells were infected for each condition per time point. Allantoic fluid was used for mock treatments. At 9.5 and 25 h p.i., cells were collected and resuspended in TRIzol reagent (Invitrogen) for total RNA extraction. A549 cells were infected with Tx/91 or Tx/91 NS1 : 1–126 viruses at an m.o.i. of 2 for 1 h at 4 °C. Three replicate wells were infected for each condition per time point. Allantoic fluid was used for mock treatments. A549 cells were collected and lysed in solution D (4 M guanidinium thiocyanate, 25 mM sodium citrate, 0.5 % sarcosyl, 0.1 M β-mercaptoethanol) at 12 and 24 h p.i. for total RNA extraction.

2012-07-09 | E-GEOD-39200 | biostudies-arrayexpress

Acute host transcriptonal response to r1918 influenza and r1918 influenza containing the NS1 gene from A/Texas/36/91 in A549 cells

Project description:The “Spanish influenza” of 1918 claimed an unprecedented number of lives, yet the determinants of virulence for this virus are still not fully understood. Here, we used functional genomics and an in vitro human lung epithelial cell infection model to define the global host transcriptional response to the eight-gene 1918 virus. To better understand the role of the 1918 virus NS1 gene, we also evaluated the host response to fully reconstructed 1918 and reassortant 1918 virus containing the NS1 gene from A/Texas/36/91 (a seasonal isolate of human influenza virus). A549 cells were infected with either recombinant 1918 influenza, a chimeric virus that contained seven genes from recombinant 1918 and the NS1 from A/Texas/36/91 (Tx/91), or mock. Cells were harvested for microarray analysis at 2, 6, and 24hr following infection.

2012-05-13 | E-GEOD-37951 | biostudies-arrayexpress

Acute host transcriptonal response to A/Texas/36/91 influenza and A/Texas/36/91 influenza containing the NS1 gene from r1918 in A549 cells

2012-05-14 | GSE37829 | GEO

Acute host transcriptonal response to r1918 influenza and r1918 influenza containing the NS1 gene from A/Texas/36/91 in A549 cells

2012-05-14 | GSE37951 | GEO

Acute host transcriptonal response to A/Texas/36/91 influenza and A/Texas/36/91 influenza containing the NS1 gene from r1918 in A549 cells

Project description:The M-bM-^@M-^\Spanish influenzaM-bM-^@M-^] of 1918 claimed an unprecedented number of lives, yet the determinants of virulence for this virus are still not fully understood. Here, we used functional genomics and an in vitro human lung epithelial cell infection model to define the global host transcriptional response to the eight-gene 1918 virus. To better understand the role of the 1918 virus NS1 gene, we evaluated the host response to A/Texas/36/91 (a seasonal isolate of human influenza virus) and a reassortant of A/Texas/36/91 containing the 1918 NS1 gene. A549 cells were infected at a MOI=2 with either A/Texas/36/91 (Tx/91) or A/Texas/36/91 (Tx/91) containing the NS1 gene from r1918 influenza. Virus was allowed to bind to cells for 1 h at 4M-BM-0C in serum-free infection medium supplemented with trypsin (1 g/ml). Mock-infected cells were treated with allantoic fluid instead of virus. Three replicate wells were used for each infection condition at each time point. Cells were harvested for array analysis at 2, 6, and 24hr post-infection. Cells from three individual cultures were pooled for each condition for microarray.

2012-05-13 | E-GEOD-37829 | 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

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) Total RNA isolated from macrophages after 8 hours of infection with wild type or mutant influenza A virus (multiplicity of infection = 2)

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

Influenza non-structural protein 1 (NS1) localization plays a key role in the anatagonism of host antiviral processes.

Project description:The influenza virus is opportunistic by nature and is capable of subverting cellular signalling pathways for the benefit of viral replication. The function of non-structural protein 1 (NS1) as a core component for the influenza virus to interfere with host antiviral activity has been well cited in literature. However, the mechanism as to how NS1 is capble of subverting the host's innate immune system is unknown. NS1 has a unique capability to migrate between both the cytoplasm and nucleus of infected cells. To assess if NS1 interference operates a stratagy pertaining to a mechanism involved with nuclear-located signalling processes we designed two mutant virsus; WSNdelNS1 which encodes a deletion to prevent complete NS1 expression and WSN3M which encodes a NS1-variant that is defective in NS1 nuclear-translocation, thus preventing NS1 from entering the nuclus of infected cells.

2020-08-12 | GSE156060 | 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 | GSE62127 | GEO

The Influenza non-structural protein 1 (NS1) operates targeted mechanisms to suppress immune gene expression.

Project description:Influenza non-structural protein 1 (NS1) has been well cited to ellicit an inhibitory effect of immune gene expression thus resulting in the curtailment of efficient antiviral immunity. However the mechanisms and gene networks subjected to this immuno-suppression are unclear. We designed an RNA-Seq study to explore this viral trait and characterize the induced gene expression in response to wildtype (native) Influenza A infection. We have also developed an Influenza mutant virus that is deficient in its ability to expression NS1 (WSNdelNS1), thus our study incorporates a virus that will enable induced transcriptomic comparison between wildtype and mutant viral infections.

2020-08-13 | GSE156152 | GEO

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