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Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription (ChIP-seq)

ABSTRACT: Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription (ChIP-seq)

PROVIDER: PRJNA648861 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12329643.fastq.gz	Fastqsanger.gz
	SRR12329644.fastq.gz	Fastqsanger.gz
	SRR12329645.fastq.gz	Fastqsanger.gz
	SRR12329646.fastq.gz	Fastqsanger.gz
	SRR12329647.fastq.gz	Fastqsanger.gz

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Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription (RNA-seq)

Project description:Human respiratory syncytial virus (RSV) is a common cause of lower respiratory tract infections in young children, the elderly, and immunocompromised individuals. Prior exposure to RSV affords little protection and many are susceptible to reinfection throughout life. Virally encoded non-structural (NS) protein 1 (NS1) is thought to modulate host responses in the cytosol. Here, we describe the nuclear localization of NS1 during RSV infection and a corresponding nuclear role in modulating host transcription. In support, we show that a significant proportion of NS1 is partitions to the nucleus and that NS1 alone is necessary and sufficient to translocate into the nucleus. NS1 co-localizes with exportin XPO1 and inhibition of XPO1 results in NS1 accumulation in the nucleus. Furthermore, nuclear NS1 is chromatin-associated and co-immunoprecipitates with Mediator complex proteins. Chromatin-immunoprecipitation demonstrates enrichment of NS1 binding overlapping Mediator and interferon-stimulated transcription factor binding sites that lie within regulatory elements of genes differentially expressed during RSV infection. Mutation of the unique alpha helix in NS1 enhances its repressive effect on host gene expression. Together, these data suggest that nuclear NS1 may alter host responses to RSV infection by binding at the promoters and enhancers of host immune response genes and disrupting host transcriptional regulators. Our study identifies yet another regulatory layer of interactions with RSV proteins that shapes host response to RSV and potentially impacts long-term immunity to RSV.

2021-10-12 | GSE155151 | GEO

Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription (ChIP-seq)

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Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription

Project description:Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription

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Structural basis for human respiratory syncytial virus NS1-mediated modulation of host responses

Project description:Human respiratory syncytial virus (hRSV) is a major cause of morbidity and mortality in the pediatric, elderly, and immune compromised populations. A gap in our understanding of hRSVdisease pathology is the interplay between virally encoded immune antagonists and host components that limit hRSV replication. hRSV encodes for non-structural (NS) proteins that are important immune antagonists; however, the role of these proteins in viral pathogenesis is incompletely understood. Here we report the crystal structure of hRSV NS1 protein, which suggests that NS1 is a structural paralog of hRSV matrix (M) protein. Comparative analysis of the shared structural fold with M revealed regions unique to NS1. Studies on NS1 WT or mutant alone or in recombinant RSVs demonstrate that structural regions unique to NS1 contribute to modulation of host responses, including inhibition of type I IFN responses, suppression of dendritic cell maturation, and promotion of inflammatory responses. Transcriptional profiles of A549 cells infected with recombinant RSVs show significant differences in multiple host pathways, suggesting that NS1 may have a greater role in regulating host responses than previously appreciated. These results provide a framework to target NS1 for therapeutic development to limit hRSV associated morbidity and mortality.

2017-06-15 | GSE99298 | GEO

Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription (RNA-seq)

Project description:Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription (RNA-seq)

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Human Respiratory Syncytial Virus Non-Structural Protein NS1 enters the nucleus to disrupt gene transcription

Project description:This SuperSeries is composed of the SubSeries listed below.

2021-10-12 | GSE155152 | GEO

An Unexpected Encounter: Respiratory Syncytial Virus Non-Structural Protein 1 Interacts With Mediator Subunit MED25

Project description:Human respiratory syncytial virus (RSV) is the leading cause of severe acute lower respiratory tract infections in infants worldwide. Non-structural protein NS1 of RSV modulates the host innate immune response by acting as an antagonist of type I and type III interferon (IFN) production and signaling in multiple ways. It is likely that NS1 performs this function by interacting with different host proteins. In order to obtain a comprehensive overview of NS1 interaction partners, we performed three complementary protein-protein interaction screens i.e. BioID, MAPPIT and KISS. The BioID proximity screen was performed during an RSV infection in A549 cells. MED25, a subunit of the Mediator complex, was identified in all 3 performed screening methods as a potential NS1 interacting protein. We confirmed the interaction between MED25 and RSV NS1 by co-immunoprecipitation, not only upon overexpression of NS1, but also with endogenous NS1 during RSV infection. We also demonstrate that the replication of RSV is enhanced in MED25 knockout A549 cells, suggesting a potential antiviral role of MED25 during RSV infection. Mediator subunits function as transcriptional coactivators and are involved in transcriptional regulation of their target genes. Therefore, the interaction between RSV NS1 and cellular MED25 might be beneficial during an RSV infection as this can affect host transcription and the host immune response to infection.

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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

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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