HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Matsuzaki, A. Articles by Nishiyama, Y. Search for Related Content PubMed PubMed Citation Articles by Matsuzaki, A. Articles by Nishiyama, Y. Agricola Articles by Matsuzaki, A. Articles by Nishiyama, Y.

US3 protein kinase of herpes simplex virus type 2 is required for the stability of the UL46-encoded tegument protein and its association with virus particles

Akio Matsuzaki

Yohei Yamauchi

Department of Virology, Nagoya University Graduate School of Medicine, Tsurumai-cho, Showa-ku, Nagoya 466-8550, Japan

Correspondence
Yukihiro Nishiyama
ynishiya{at}med.nagoya-u.ac.jp

The herpes simplex virus (HSV) US3 gene encodes a serine/threonine protein kinase (PK). Although US3 PK is not essential for virus replication in cell culture, it plays an important role in the regulation of apoptosis in infected cells. However, the role of US3 PK in virus replication and pathogenicity is not well understood. The UL46 gene encodes virion tegument phosphoproteins, the properties and functions of which are poorly understood. In this study, it is shown that the UL46 protein of HSV type 2 (HSV-2) is affected strikingly by the presence of US3 PK. In the absence of US3 PK, UL46 protein was quite unstable, being much more susceptible to degradation. UL46 protein was undetectable in the extracellular virions of US3-deficient virus. Moreover, in vitro kinase assays using recombinant US3 PK show that UL46 protein is phosphorylated by the US3 PK, suggesting that UL46 can be a direct substrate for US3 PK in infected cells. Together, these findings shed new light on the physiological functions of US3 PK.

These authors contributed equally to this work.

This article has been cited by other articles:

				S. L. Labiuk, L. A. Babiuk, and S. van Drunen Littel-van den Hurk Major tegument protein VP8 of bovine herpesvirus 1 is phosphorylated by viral US3 and cellular CK2 protein kinases J. Gen. Virol., December 1, 2009; 90(12): 2829 - 2839. [Abstract] [Full Text] [PDF]

				A. Kato, M. Tanaka, M. Yamamoto, R. Asai, T. Sata, Y. Nishiyama, and Y. Kawaguchi Identification of a Physiological Phosphorylation Site of the Herpes Simplex Virus 1-Encoded Protein Kinase Us3 Which Regulates Its Optimal Catalytic Activity In Vitro and Influences Its Function in Infected Cells J. Virol., July 1, 2008; 82(13): 6172 - 6189. [Abstract] [Full Text] [PDF]

				G. Zahariadis, M. J. Wagner, R. C. Doepker, J. M. Maciejko, C. M. Crider, K. R. Jerome, and J. R. Smiley Cell-Type-Specific Tyrosine Phosphorylation of the Herpes Simplex Virus Tegument Protein VP11/12 Encoded by Gene UL46 J. Virol., July 1, 2008; 82(13): 6098 - 6108. [Abstract] [Full Text] [PDF]

				K. Michael, B. G. Klupp, A. Karger, and T. C. Mettenleiter Efficient Incorporation of Tegument Proteins pUL46, pUL49, and pUS3 into Pseudorabies Virus Particles Depends on the Presence of pUL21 J. Virol., January 15, 2007; 81(2): 1048 - 1051. [Abstract] [Full Text] [PDF]

				A. Schaap-Nutt, M. Sommer, X. Che, L. Zerboni, and A. M. Arvin ORF66 Protein Kinase Function Is Required for T-Cell Tropism of Varicella-Zoster Virus In Vivo J. Virol., December 1, 2006; 80(23): 11806 - 11816. [Abstract] [Full Text] [PDF]

				K. Michael, B. G. Klupp, T. C. Mettenleiter, and A. Karger Composition of Pseudorabies Virus Particles Lacking Tegument Protein US3, UL47, or UL49 or Envelope Glycoprotein E J. Virol., February 1, 2006; 80(3): 1332 - 1339. [Abstract] [Full Text] [PDF]