Integrin-Linked Kinase Reduces H3K9 Trimethylation to Enhance Herpes Simplex Virus 1 Replication
Lytic cycle
Integrin-linked kinase
DOI:
10.3389/fcimb.2022.814307
Publication Date:
2022-03-08T07:36:22Z
AUTHORS (5)
ABSTRACT
Histone modifications control the lytic gene expression of herpes simplex virus 1 (HSV-1). The heterochromatin mark, trimethylation histone H3 on lysine (K) 9 (H3K9me3), is detected HSV-1 genomes at early phases infection to repress viral transcription. However, components and mechanisms involved in process are mostly unknown. Integrin-linked kinase (ILK) activated by PI3K phosphorylate Akt promote several RNA infections. has been shown enhance infection, suggesting a pro-viral role ILK that not addressed before. Here, we reveal enhances replication an Akt-independent manner. reduces accumulation H3K9me3 promoters compartments. Notably, manner independent ICP0. Instead, show increased binding H3K9 methyltransferase SUV39H1 corepressor TRIM28 knockdown cells. Knocking down or increases transcription These results antagonizes SVU39H1- TRIM28-mediated repression We further demonstrate phosphorylation serine 473 824 HSV-1-infected cells, facilitates abrogate its inhibition OSU-T315, inhibitor, suppresses cells mice. In conclusion, decreases DNA reducing binding. Moreover, our suggest targeting could be broad-spectrum antiviral strategy for infections, especially viruses controlled modifications.
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