Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

High definition analysis of host protein stability during human cytomegalovirus infection reveals antiviral factors and viral evasion mechanisms

ABSTRACT: High definition analysis of host protein stability during human cytomegalovirus infection reveals antiviral factors and viral evasion mechanisms

PROVIDER: PRJNA435668 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR6765790.fastq.gz	Fastqsanger.gz
	SRR6765782.fastq.gz	Fastqsanger.gz
	SRR6765783.fastq.gz	Fastqsanger.gz
	SRR6765784.fastq.gz	Fastqsanger.gz
	SRR6765785.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 9

Similar Datasets

High definition analysis of host protein stability during human cytomegalovirus infection reveals antiviral factors and viral evasion mechanisms

Project description:Human cytomegalovirus (HCMV) is an important pathogen with multiple immune evasion strategies, including virally facilitated degradation of host antiviral restriction factors. Here, we describe a multiplexed approach to discover proteins with innate immune function on the basis of active degradation by the proteasome or lysosome during early phase HCMV infection. Using three orthogonal proteomic/transcriptomic screens to quantify protein degradation, with high confidence we identified 35 proteins enriched in antiviral restriction factors. A final screen employed a comprehensive panel of viral mutants to predict viral genes that target >250 human proteins. This approach revealed Helicase-like Transcription Factor (HLTF), a DNA helicase important in DNA repair, potently inhibits early viral gene expression but is rapidly degraded during infection. The functionally unknown HCMV protein UL145 facilitates HLTF degradation by recruiting the Cullin4 E3 ligase complex. Our approach and data will enable further identifications of innate pathways targeted by HCMV and other viruses.

2018-08-16 | GSE111036 | GEO

High definition analysis of protein stability during cytomegalovirus infection informs on cellular restriction

Project description:Human cytomegalovirus (HCMV) is an important pathogen and a paradigm of viral immune evasion. Here, we describe a multiplexed approach to discover proteins with novel innate immune functions on the basis of their active proteasomal or lysosomal degradation during the early phase of HCMV infection. Using three orthogonal proteomic/transcriptomic screens to quantify protein degradation, we identified 35 proteins with high confidence that were enriched in known antiviral restriction factors. A final screen facilitated global analysis of the mechanism of viral immune-modulation by predicting which viral genes target >250 human proteins. Helicase-like Transcription Factor (HLTF), a DNA helicase important in error-free post-replication DNA repair, was rapidly degraded during infection and potently inhibited early viral gene expression. HCMV UL145, a protein of previously unknown function, recruits the Cullin 4 E3 ligase complex to degrade HLTF. Our approach and data will enable further identifications of innate pathways targeted by HCMV and other viruses.

2018-08-16 | PXD009945 | Pride

High-Definition Analysis of Host Protein Stability during Human Cytomegalovirus Infection Reveals Antiviral Factors and Viral Evasion Mechanisms.

Project description:Human cytomegalovirus (HCMV) is an important pathogen with multiple immune evasion strategies, including virally facilitated degradation of host antiviral restriction factors. Here, we describe a multiplexed approach to discover proteins with innate immune function on the basis of active degradation by the proteasome or lysosome during early-phase HCMV infection. Using three orthogonal proteomic/transcriptomic screens to quantify protein degradation, with high confidence we identified 35 proteins enriched in antiviral restriction factors. A final screen employed a comprehensive panel of viral mutants to predict viral genes that target >250 human proteins. This approach revealed that helicase-like transcription factor (HLTF), a DNA helicase important in DNA repair, potently inhibits early viral gene expression but is rapidly degraded during infection. The functionally unknown HCMV protein UL145 facilitates HLTF degradation by recruiting the Cullin4 E3 ligase complex. Our approach and data will enable further identifications of innate pathways targeted by HCMV and other viruses.

| S-EPMC6146656 | biostudies-literature

Human cytomegalovirus protein RL1 degrades the antiviral factor SLFN11 via recruitment of the CRL4 E3 ubiquitin ligase complex

Project description:Human cytomegalovirus (HCMV) is an important human pathogen and a paradigm of viral immune evasion, targeting intrinsic, innate and adaptive immunity. We have employed two novel, orthogonal multiplexed tandem mass tag-based proteomic screens to identify host proteins downregulated by viral factors expressed during the latest phases of viral infection. This approach revealed that the HIV-1 restriction factor Schlafen-11 (SLFN11) was degraded by the poorly characterised, late-expressed HCMV protein RL1, via recruitment of the Cullin4-RING E3 Ubiquitin Ligase (CRL4) complex. SLFN11 potently restricted HCMV infection, inhibiting the formation and spread of viral plaques. Overall, we show that a restriction factor previously thought only to inhibit RNA viruses additionally restricts HCMV. We define the mechanism of viral antagonism and also describe an important resource for revealing additional molecules of importance in antiviral innate immunity and viral immune evasion.

2022-02-22 | PXD026785 | Pride

Evasion of antiviral bacterial immunity by phage tRNAs

Project description:Evasion of antiviral bacterial immunity by phage tRNAs

| PRJNA953969 | ENA

Strain Dependent Restriction of Human Cytomegalovirus by Zinc Finger Antiviral Proteins

Project description:Strain Dependent Restriction of Human Cytomegalovirus by Zinc Finger Antiviral Proteins

| PRJEB58764 | ENA

The zinc finger antiviral protein ZAP destabilises viral transcripts and restricts human cytomegalovirus

Project description:Interferon-stimulated gene products (ISGs) play a crucial role in early infection control. The ISG zinc finger CCCH-type antiviral protein 1 (ZAP/ZC3HAV1) antagonises several RNA viruses by binding to CG-rich RNA sequences, whereas its effect on DNA viruses is largely unknown. Here, we decipher the role of ZAP in the context of human cytomegalovirus (HCMV) infection, a β-herpesvirus that is associated with high morbidity in immunosuppressed individuals and newborns. We show that expression of the two major isoforms of ZAP, the long (ZAP-L) and short (ZAP-S), is induced during HCMV infection and that both negatively affect HCMV replication. Transcriptome and proteome analyses demonstrated that the expression of ZAP decelerates the progression of HCMV infection. SLAM-sequencing revealed that ZAP restricts HCMV at early stages of infection by destabilising a distinct subset of viral transcripts with low CG content. In summary, this report provides evidence of an important antiviral role for ZAP in host defense against HCMV infection and highlights its differentiated function during DNA virus infection.

2021-04-22 | PXD023559 | Pride

Human Cytomegalovirus long non-coding RNA counteracts nuclear cGAS to facilitate immune evasion

Project description:Viruses have evolved diverse immune evasion strategies including targeting host pattern recognition receptors. The role of viral non-coding RNAs in modulating PRR activity is unclear. Here, we show that human cytomegalovirus (HCMV) produces long non-coding RNA4.9 that counteracts nuclear cyclic GMP-AMP synthase (cGAS)-mediated immune response to facilitate viral infection in primary human foreskin fibroblasts (HFFs). RNA4.9 interacts with host cGAS via its 75-nucleotide (nt) RNA region with predicted hairpin loops. Binding of RNA4.9 to cGAS inhibits cGAS enzymatic activity and downstream interferon response, and facilitates productive viral replication. Sterically blocking the folding of 75-nt region with antisense oligonucleotides during HCMV infection restores cGAS activity and impairs viral replication. We also found that the specific localization of RNA4.9, which concentrates near HCMV DNA, is correlated with its efficient binding to cGAS and subsequent immune suppression. Our findings demonstrate viral non-coding RNAs as critical cGAS regulators and potential therapeutic targets.

2025-06-12 | GSE270524 | GEO

Human Cytomegalovirus long non-coding RNA counteracts nuclear cGAS to facilitate immune evasion

2025-06-11 | GSE268887 | GEO

Human Cytomegalovirus long non-coding RNA counteracts nuclear cGAS to facilitate immune evasion

Project description:Human Cytomegalovirus long non-coding RNA counteracts nuclear cGAS to facilitate immune evasion

| PRJNA1119399 | ENA