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Journal of Virology, November 2009, p. 11624-11634, Vol. 83, No. 22
0022-538X/09/$08.00+0     doi:10.1128/JVI.00993-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Differences in the Regulatory and Functional Effects of the Us3 Protein Kinase Activities of Herpes Simplex Virus 1 and 2{triangledown}

Tomomi Morimoto,1 Jun Arii,1,2 Michiko Tanaka,3 Tetsutaro Sata,3 Hiroomi Akashi,2 Masao Yamada,4 Yukihiro Nishiyama,5 Masashi Uema,1 and Yasushi Kawaguchi1*

Division of Viral Infection, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108-8639,1 Department of Veterinary Microbiology, Graduate School of Agricultural and Life Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657,2 Department of Pathology, National Institute of Infectious Disease, Shinjuku-ku, Tokyo 162-8640,3 Department of Virology, Okayama University Medical School, Okayama, 700-8558,4 Department of Virology, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550, Japan5

Received 16 May 2009/ Accepted 28 August 2009

Us3 protein kinases encoded by herpes simplex virus 1 (HSV-1) and 2 (HSV-2) are serine/threonine protein kinases and play critical roles in viral replication and pathogenicity in vivo. In the present study, we investigated differences in the biological properties of HSV-1 and HSV-2 Us3 protein kinases and demonstrated that HSV-2 Us3 did not have some of the HSV-1 Us3 kinase functions, including control of nuclear egress of nucleocapsids, localization of UL31 and UL34, and cell surface expression of viral envelope glycoprotein B. In agreement with the observations that HSV-2 Us3 was less important for these functions, the effect of HSV-2 Us3 kinase activity on virulence in mice following intracerebral inoculation was much lower than that of HSV-1 Us3. Furthermore, we showed that alanine substitution in HSV-2 Us3 at a site (aspartic acid at position 147) corresponding to one that can be autophosphorylated in HSV-1 Us3 abolished HSV-2 Us3 kinase activity. Thus, the regulatory and functional effects of Us3 kinase activity are different between HSV-1 and HSV-2.

* Corresponding author. Mailing address: Division 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. Phone: 81-3-6409-2070. Fax: 81-3-6409-2072. E-mail: ykawagu{at}ims.u-tokyo.ac.jp

{triangledown} Published ahead of print on 9 September 2009.

Journal of Virology, November 2009, p. 11624-11634, Vol. 83, No. 22
0022-538X/09/$08.00+0     doi:10.1128/JVI.00993-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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