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Adenovirus prevents dsRNA formation by promoting efficient splicing of viral RNA

ABSTRACT: Adenovirus prevents dsRNA formation by promoting efficient splicing of viral RNA

PROVIDER: PRJNA743528 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15035100.fastq.gz	Fastqsanger.gz
	SRR15035101.fastq.gz	Fastqsanger.gz
	SRR15035102.fastq.gz	Fastqsanger.gz
	SRR15035103.fastq.gz	Fastqsanger.gz
	SRR15035104.fastq.gz	Fastqsanger.gz

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Adenovirus prevents dsRNA formation by promoting efficient splicing of viral RNA

Project description:Eukaryotic cells recognize intracellular pathogens through pattern recognition receptors, including sensors of aberrant nucleic acid structures. Sensors of double-stranded RNA (dsRNA) are known to detect replication intermediates of RNA viruses. It has been suggested that annealing of mRNA from symmetrical transcription of both top and bottom strands of DNA virus genomes can produce dsRNA during infection. Supporting this hypothesis, nearly all DNA viruses encode inhibitors of dsRNA-recognition pathways. However, direct evidence that DNA viruses produce dsRNA is lacking. Contrary to dogma, we show that the nuclear-replicating DNA virus adenovirus (AdV) does not produce detectable levels of dsRNA during infection. In contrast, abundant dsRNA is detected within the nucleus of cells infected with AdV mutants that lack the virus-directed ubiquitin ligase required for efficient processing of viral RNA. In the presence of nuclear dsRNA, the cytoplasmic dsRNA sensor PKR is relocalized and activated within the nucleus. Accumulation of viral dsRNA occurs in the late phase of infection, when unspliced viral transcripts form intron/exon base pairs between top and bottom strand transcripts. We propose that DNA viruses actively promote efficient splicing and mRNA processing to limit dsRNA formation, thus avoiding detection and restriction by host nucleic acid sensors.

2021-07-15 | GSE179388 | GEO

Adenovirus prevents dsRNA formation by promoting efficient splicing of viral RNA.

Project description:Eukaryotic cells recognize intracellular pathogens through pattern recognition receptors, including sensors of aberrant nucleic acid structures. Sensors of double-stranded RNA (dsRNA) are known to detect replication intermediates of RNA viruses. It has long been suggested that annealing of mRNA from symmetrical transcription of both top and bottom strands of DNA virus genomes can produce dsRNA during infection. Supporting this hypothesis, nearly all DNA viruses encode inhibitors of dsRNA-recognition pathways. However, direct evidence that DNA viruses produce dsRNA is lacking. Contrary to dogma, we show that the nuclear-replicating DNA virus adenovirus (AdV) does not produce detectable levels of dsRNA during infection. In contrast, abundant dsRNA is detected within the nucleus of cells infected with AdV mutants defective for viral RNA processing. In the presence of nuclear dsRNA, the cytoplasmic dsRNA sensor PKR is relocalized and activated within the nucleus. Accumulation of viral dsRNA occurs in the late phase of infection, when unspliced viral transcripts form intron/exon base pairs between top and bottom strand transcripts. We propose that DNA viruses actively limit dsRNA formation by promoting efficient splicing and mRNA processing, thus avoiding detection and restriction by host innate immune sensors of pathogenic nucleic acids.

| S-EPMC8860579 | biostudies-literature

Efficient in vivo genome editing prevents hypertrophic cardiomyopathy in mice

Project description:Efficient in vivo genome editing prevents hypertrophic cardiomyopathy in mice

| PRJNA911761 | ENA

Efficient in vivo genome editing prevents hypertrophic cardiomyopathy in mice [genomicDNA]

Project description:Efficient in vivo genome editing prevents hypertrophic cardiomyopathy in mice [genomicDNA]

| PRJNA911928 | ENA

Efficient in vivo Genome Editing Prevents Hypertrophic Cardiomyopathy in Mice [Amplified_cDNA]

Project description:Efficient in vivo Genome Editing Prevents Hypertrophic Cardiomyopathy in Mice [Amplified_cDNA]

| PRJNA911609 | ENA

unclassified dsRNA viruses

Project description:unclassified dsRNA viruses

| PRJNA16954 | ENA

Efficient in vivo Genome Editing Prevents Hypertrophic Cardiomyopathy in Mice [Nuc-Seq]

Project description:Efficient in vivo Genome Editing Prevents Hypertrophic Cardiomyopathy in Mice [Nuc-Seq]

| PRJNA911594 | ENA

Efficient in vivo Genome Editing Prevents Hypertrophic Cardiomyopathy in Mice [RNA-seq]

Project description:Efficient in vivo Genome Editing Prevents Hypertrophic Cardiomyopathy in Mice [RNA-seq]

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Efficient mRNA processing prevents gene gating-associated replication stress in mammalian cells

Project description:Efficient mRNA processing prevents gene gating-associated replication stress in mammalian cells

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Structural insights into dsRNA processing by Drosophila Dicer-2/Loqs-PD

Project description:Small interfering RNAs (siRNAs) are the key components for RNA interference (RNAi), a conserved RNA silencing mechanism in many eukaryotes. In Drosophila, an RNase III enzyme Dicer-2 (Dcr-2), aided by its cofactor Loquacious-PD (Loqs-PD), plays major role in generating 21 base-pair (bp) siRNA duplexes from long double-stranded RNAs (dsRNAs). The ATP hydrolysis by the helicase domain of Dcr-2 is critical to the successful processing of a long dsRNA into consecutive siRNA duplexes. Here we report the cryo-EM structures of Dcr-2/Loqs-PD in the apo state and in multiple processing states of a 50-bp dsRNA substrate. The structures elucidated interactions between Dcr-2 and Loqs-PD, and significant conformational changes of Dcr-2 during a dsRNA processing cycle. The N-terminal helicase and DUF283 domains undergo conformational change upon initial dsRNA binding, forming an ATP binding pocket and a 5’-phosphate binding pocket. The overall conformation of Dcr-2/Loqs-PD is relatively rigid during translocating along the dsRNA in the presence of ATP, while the interaction between DUF283 and RIIIDb domains prevents non-specific cleavage during translocation by blocking the access of dsRNA to the RNase active center. Additional ATP-dependent conformational changes are required to form an active-dicing state and precisely cleave the dsRNA into 21-bp siRNA duplex confirmed by the structure in the post-dicing state. Collectively, this study revealed the molecular mechanism for the full-cycle of ATP-dependent dsRNA processing by Dcr-2/Loqs-PD.

2022-04-21 | PXD033365 |

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