Journal
JOURNAL OF VIROLOGY
Volume 80, Issue 12, Pages 5740-5746Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00169-06
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Funding
- NIAID NIH HHS [T32 AI007324, T32 AI-073244] Funding Source: Medline
- NINDS NIH HHS [P01 NS33768, P50 NS033768, P01 NS033768] Funding Source: Medline
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Human herpes simplex virus 1 (HSV-1) is a double-stranded DNA virus that causes facial, ocular, and encephalitic disease in humans. Previous work showed that the genome of HSV-1 is associated with acetylated and methyllated histones during lytic infection. However, the physiological role of histone modifications in lytic infection of HSV-1 is unclear. We examined the role of protein methylation in lytic infection of HSV-1 using a protein methylation inhibitor, 5'-deoxy-5'-methylthioadenosine (MTA). We found that MTA strongly reduces the transcription and replication of HSV-1. Moreover, MTA treatment decreases the level of trimethylation of lysine 4 in histone H3 (H3K4me3) on the HSV-1 genome. These results suggest that protein methylation, and in particular, histone methylation, is involved in the lytic infection of HSV-1. To delineate the underlying mechanism, we investigated the role of two H3K4 methyltransferases, Sell and Set7/9, in the lytic infection of HSV-1. Using small interference RNA, we found that the reduction of Sell, but not Set7/9, reduces the transcription and replication of HSV-1 and specifically decreases H3K4me3 on the virus genome. These results indicate that H3K4me3 mediated by Sett is required for optimal gene expression and replication of HSV-1 during lytic infection and suggest that this pathway could be a potential point of pharmacological intervention during HSV-1 infection.
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