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Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25

ABSTRACT: Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25

PROVIDER: PRJNA1126678 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29493803_1.fastq.gz	Fastqsanger.gz
	SRR29493803_2.fastq.gz	Fastqsanger.gz
	SRR29493804_1.fastq.gz	Fastqsanger.gz
	SRR29493804_2.fastq.gz	Fastqsanger.gz
	SRR29493805_1.fastq.gz	Fastqsanger.gz

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Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25

Project description:Human Respiratory Syncytial Virus (hRSV) is a prevalent pathogen posing significant risks to infants and older adults. While the roles of RSV non-structural proteins NS1 protein in modulating host immune responses remains poorly defined, its potential impact on viral pathogenicity is critical. We employed CUT&RUN of NS1, Mediator, and ATF3 in WT NS1 and mutant NS1 expressing A549 cells and bulk RNA sequencing of WT and mutant NS1-expressing A549 (GSE155151) and RSV infection in human lung air-liquid interface (ALI) cultures to elucidate the perterbations of transcriptional regulatory control induced by NS1. Coupled with our earlier work, these epigenomic and transcriptomic profiling datasets provides deeper insights into the molecular mechanisms through which RSV NS1 protein disrupts host immune functions.

2025-03-09 | GSE270463 | 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.

2022-09-09 | PXD034627 | Pride

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 (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.

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shRNA-mediated knockdown of ETV4 and MED25 in the prostate cell line PC3 reveals set of genes potentially coregulated by MED25 and ETV4

Project description:Our in vitro binding studies support a model whereby MED25 exhibits multivalent interactions with a subset of related ETS factors, ETV1/4/5. We hypothesize that the interaction would allow for coregulation of genes by ETV1/4/5 and MED25, acting perhaps to link the ETVs to the Mediator complex. To explore this possibility, we compared the genome occupancy for FLAG-tagged MED25 and ETV4 in the prostate cancer cell line PC3, which overexpresses ETV4. We also tested for relevance of MED25 and ETV4 binding to for gene expression in PC3s. We found a high degree of overlap in the FLAG-MED25 and ETV4 ChIPs datasets consistent with our model, and also identified a subset of target genes co-dependent on Med25 and ETV4.

2019-06-28 | GSE133447 | GEO

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