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Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1
Risa Asai1, Takashi Ohno, Akihisa Kato
1Division of Viral Infection, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Abstract:
Herpes simplex virus 1 (HSV-1) UL13 is a viral protein kinase that regulates optimal viral replication in cell cultures. Identification of substrates of protein kinases is a crucial step to elucidate the mechanism by which they function. Using our developed system to analyze the specific protein kinase activity of UL13, we have shown that UL13 protein kinase directly phosphorylates the viral proteins ICP22 and UL49 previously reported to be putative substrates. We also identified UL41 as a previously unreported and novel substrate of UL13. These data will serve as a basis to clarify the mechanism by which UL13 influences viral replication.
Insights
Herpes simplex virus 1 UL13 protein kinase phosphorylates viral proteins ICP22 and UL49. It also newly phosphorylates UL41, aiding understanding of viral replication mechanisms.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Herpes simplex virus 1 (HSV-1) UL13 is a viral protein kinase.
- Understanding protein kinase substrates is key to elucidating their function.
- HSV-1 UL13 regulates viral replication in cell cultures.
Purpose of the Study:
- To identify the direct substrates of the HSV-1 UL13 protein kinase.
- To further elucidate the mechanism of HSV-1 replication.
- To characterize the specific protein kinase activity of UL13.
Main Methods:
- Utilized a developed system to analyze UL13 protein kinase activity.
- Investigated direct phosphorylation of viral proteins by UL13.
- Identified novel and known substrates.
Main Results:
- HSV-1 UL13 directly phosphorylates ICP22 and UL49.
- UL41 was identified as a novel substrate of UL13.
- Confirmed ICP22 and UL49 as direct targets of UL13.
Conclusions:
- The study identifies UL41 as a new substrate for HSV-1 UL13.
- These findings provide a basis for understanding UL13's role in viral replication.
- Direct phosphorylation of ICP22, UL49, and UL41 by UL13 is demonstrated.
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