HSV-1 exploits host heterochromatin for egress [CUT&Tag]
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA858438 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR20142300_1.fastq.gz | Fastqsanger.gz | |||
| SRR20142300_2.fastq.gz | Fastqsanger.gz | |||
| SRR20142301_1.fastq.gz | Fastqsanger.gz | |||
| SRR20142301_2.fastq.gz | Fastqsanger.gz | |||
| SRR20142302_1.fastq.gz | Fastqsanger.gz |
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Project description:Herpes simplex virus replicates and forms progeny in the nucleus where it must overcome host chromatin to establish a successful infection. During lytic infection, newly formed viral capsids navigate through heterochromatin channels at the nuclear periphery to egress out of the nucleus. In uninfected cells, specific histone marks such as trimethylation on histone H3 lysine 27 (H3K27me3) and the histone variant macroH2A1 delineate heterochromatin regions, or repressed chromatin, that are predominantly located in the nuclear periphery. We examined these markers during HSV-1 lytic infection in primary cells and discovered a striking increase in the levels of macroH2A1 and H3K27me3. Here, we demonstrate that the loss of macroH2A1 results in significantly lower viral titers but does not impair viral transcription, protein production, or replication. By inhibiting the deposition of H3K27me3 by EZH2, we further show that reduction of H3K27me3 also leads to a significant decrease in viral titers. Through chromatin profiling via Cleavage Under Targets and tagmentation (CUT&Tag) of macroH2A1 and H3K27me3, we define the specific chromatin regions that change dynamically during HSV-1 lytic infection and show that regions with increased macroH2A1 and H3K27me3 correlate with decreased host transcription as measured by RNA-seq. Furthermore, we find by electron microscopy that loss of macroH2A1 results in reduced heterochromatin at the nuclear periphery and significantly more viral capsids trapped in the nuclear compartment. Using both high and low shedding clinical isolates of HSV-1, we similarly find that HSV-1 titers are significantly reduced in the absence of macroH2A1. Our work demonstrates that HSV-1 takes advantage of the dynamic nature of host heterochromatin formation during infection for efficient viral egress from the nuclear compartment.
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Project description:HSV-1 exploits host heterochromatin for nuclear egress
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Project description:HSV-1 exploits host heterochromatin for egress [RNA-seq]
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Project description:Herpes simplex virus replicates and forms progeny in the nucleus where it must overcome host chromatin to establish a successful infection. During lytic infection, newly formed viral capsids navigate through heterochromatin channels at the nuclear periphery to egress out of the nucleus. In uninfected cells, specific histone marks such as trimethylation on histone H3 lysine 27 (H3K27me3) and the histone variant macroH2A1 delineate heterochromatin regions, or repressed chromatin, that are predominantly located in the nuclear periphery. We examined these markers during HSV-1 lytic infection in primary cells and discovered a striking increase in the levels of macroH2A1 and H3K27me3. Here, we demonstrate that the loss of macroH2A1 results in significantly lower viral titers but does not impair viral transcription, protein production, or replication. By inhibiting the deposition of H3K27me3 by EZH2, we further show that reduction of H3K27me3 also leads to a significant decrease in viral titers. Through chromatin profiling via Cleavage Under Targets and tagmentation (CUT&Tag) of macroH2A1 and H3K27me3, we define the specific chromatin regions that change dynamically during HSV-1 lytic infection and show that regions with increased macroH2A1 and H3K27me3 correlate with decreased host transcription as measured by RNA-seq. Furthermore, we find by electron microscopy that loss of macroH2A1 results in reduced heterochromatin at the nuclear periphery and significantly more viral capsids trapped in the nuclear compartment. Using both high and low shedding clinical isolates of HSV-1, we similarly find that HSV-1 titers are significantly reduced in the absence of macroH2A1. Our work demonstrates that HSV-1 takes advantage of the dynamic nature of host heterochromatin formation during infection for efficient viral egress from the nuclear compartment.
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Project description:Herpes simplex virus (HSV-1) progeny form in the nucleus and exit to successfully infect other cells. Newly formed capsids navigate complex chromatin architecture to reach the inner nuclear membrane (INM) and egress. Here, we demonstrate by transmission electron microscopy (TEM) that HSV-1 capsids traverse heterochromatin associated with trimethylation on histone H3 lysine 27 (H3K27me3) and the histone variant macroH2A1. Through chromatin profiling during infection, we revealed global redistribution of these marks whereby massive host genomic regions bound by macroH2A1 and H3K27me3 correlate with decreased host transcription in active compartments. We found that the loss of these markers resulted in significantly lower viral titers but did not impact viral genome or protein accumulation. Strikingly, we discovered that loss of macroH2A1 or H3K27me3 resulted in nuclear trapping of capsids. Finally, by live-capsid tracking, we quantified this decreased capsid movement. Thus, our work demonstrates that HSV-1 takes advantage of the dynamic nature of host heterochromatin formation during infection for efficient nuclear egress.
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