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Published on: December 21, 2019
Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin
1State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei 430072, China.
Journal of Virology
|September 16, 2011
Summary
Human cytomegalovirus (HCMV) UL70 protein interacts with Snapin, a host factor. Snapin regulates UL70
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Genomic DNA synthesis is crucial for herpesviruses like human cytomegalovirus (HCMV).
- HCMV UL70 is hypothesized to be the primase, essential for viral DNA replication.
- No host factors interacting with UL70 have been previously identified.
Purpose of the Study:
- To identify host factors interacting with HCMV UL70.
- To investigate the functional role of identified host factors in HCMV replication.
Main Methods:
- Yeast two-hybrid screening to detect protein-protein interactions.
- Coimmunoprecipitation assays in human cells to confirm interactions.
- Small interfering RNA (siRNA) mediated gene silencing to modulate host factor expression.
- Assessment of viral DNA synthesis and progeny production.
Main Results:
- Direct interaction between HCMV UL70 and human Snapin was confirmed.
- Snapin predominantly localizes to the cytoplasm and is associated with cellular vesicles.
- Overexpression of Snapin decreased nuclear import of UL70, viral DNA synthesis, and progeny production.
- Downregulation of Snapin using siRNA increased nuclear import of UL70, viral DNA synthesis, and progeny production.
Conclusions:
- Snapin is a novel host factor that interacts with HCMV UL70.
- Snapin plays a significant role in regulating the nuclear localization of UL70.
- Modulation of Snapin affects HCMV DNA synthesis and viral progeny production, suggesting a key regulatory role in the viral life cycle.
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