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ABSTRACT: Human cytomegalovirus harnesses host L1 retrotransposon for efficient replication

PROVIDER: PRJNA1144403 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30131375_1.fastq.gz	Fastqsanger.gz
	SRR30131375_2.fastq.gz	Fastqsanger.gz
	SRR30131376_1.fastq.gz	Fastqsanger.gz
	SRR30131376_2.fastq.gz	Fastqsanger.gz
	SRR30131377_1.fastq.gz	Fastqsanger.gz

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Human cytomegalovirus hijacks L1 retrotransposon to fuel its heterogeneity

Project description:Human Cytomegalovirus (HCMV) causes severe morbidity and mortality in an immune-compromised or immune-naïve host. Among DNA viruses, the genetic diversity of HCMV is unexpectedly high and comparable to those of RNA viruses, which hinders the development of effective vaccines and causes the emergence of antiviral resistance. However, little is known about how HCMV acquires genetic variation. Here, we propose an evolution strategy of HCMV, that exploits host “jumping DNA” L1 retrotransposon as a mutagen. We found that HCMV infection switches on L1 expression by upregulating transcription factors YY1 and RUNX3. Furthermore, HCMV DNA processivity factor, UL44 recruits L1 ribonucleoproteins to viral replication compartments and induces DNA damage to its genome. Deep-sequencing analysis of cultured HCMV genome revealed that L1 retrotransposon facilitates mutation burden on the viral genome. Indeed, laboratory adaptation of HCMV to fibroblasts is only observed upon active L1 expression. These findings demonstrate the evolution mechanism and molecular insights of how HCMV acquires genetic fitness by the hijacking of host L1 retrotransposon.

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Human cytomegalovirus hijacks L1 retrotransposon to fuel its heterogeneity

Project description:Human cytomegalovirus hijacks L1 retrotransposon to fuel its heterogeneity

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Project description:Human Cytomegalovirus (HCMV) is a ubiquitous pathogen that has co-evolved with its host and in doing so, is highly efficient in undermining antiviral responses that limit successful infections. As a result, HCMV infections are highly problematic in individuals with weakened or underdeveloped immune systems including transplant recipients and newborns. Understanding how HCMV controls the microenvironment of an infected cell so as to favor productive replication is of critical importance. To this end, we took an unbiased proteomics approach to identify the highly reversible, stress induced, post-translational modification (PTM), protein S-nitrosylation, on viral proteins to determine the biological impact on viral replication. We identified protein S-nitrosylation of 13 viral proteins during infection of highly permissive fibroblasts. One of these proteins, pp71, is critical for efficient viral replication, as it undermines host antiviral responses, including STING activation. By exploiting site-directed mutagenesis of the specific amino acids we identified in pp71 as protein S-nitrosylated, we found this pp71 PTM diminishes its ability to undermine antiviral responses induced by the STING pathway. Our results suggest a model in which protein S-nitrosylation may function as a host response to viral infection that limits viral spread.

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