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Journal of Virology, July 2005, p. 9325-9331, Vol. 79, No. 14
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.14.9325-9331.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Identification of Proteins Phosphorylated Directly by the Us3 Protein Kinase Encoded by Herpes Simplex Virus 1

Akihisa Kato,1 Mayuko Yamamoto,1 Takashi Ohno,1 Hiroshi Kodaira,2 Yukihiro Nishiyama,1 and Yasushi Kawaguchi1,3*

Department of Virology, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550,1 Development Planning and Coordination, Pharmaceutical Department, Yakult Honsha Co., LTD., Chuo-ku, Tokyo 104-0061,2 PRESTO, Japan Science and Technology Agency, Kawaguchi, Saitama, 332-0012, Japan3

Received 14 February 2005/ Accepted 23 March 2005

We have developed a system to analyze the specific protein kinase activity of herpes simplex virus 1 Us3 in vitro and shown that Us3 directly phosphorylates viral proteins UL34, ICP22, and Us9 and the cellular protein Bad, previously reported to be putative substrates. Using this system, we determined the phosphorylation sites of UL34 and identified UL31 as a previously unreported, novel substrate of Us3. This system will be useful for further identification of Us3 substrates and their phosphorylation sites, clarification of the role of Us3 in viral replication, and identification of additional Us3 function(s).

* Corresponding author. Mailing address: Department of Virology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan. Phone: 81-52-744-2207. Fax: 81-52-744-2452. E-mail: ykawagu{at}med.nagoya-u.ac.jp.

Journal of Virology, July 2005, p. 9325-9331, Vol. 79, No. 14
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.14.9325-9331.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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