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Journal of Virology, December 2002, p. 12683-12690, Vol. 76, No. 24
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.24.12683-12690.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

C-Terminal Region of STAT-1{alpha} Is Not Necessary for Its Ubiquitination and Degradation Caused by Mumps Virus V Protein

Noriko Yokosawa, Shin-ichi Yokota, Toru Kubota,{dagger} and Nobuhiro Fujii*

Department of Microbiology, School of Medicine, Sapporo Medical University, Chuo-ku, Sapporo 060-8556, Hokkaido, Japan

Received 17 May 2002/ Accepted 12 September 2002

Constitutive levels of production of STAT-1 were reduced by 10 h postinfection (p.i.) and significantly lost by 24 h p.i. in FL cells acutely infected with mumps virus (MuV). This result was consistent with that observed in previous studies and experiments with cells persistently infected with MuV (FLMT cells). There was a marked decrease in the amount of STAT-1 in cells expressing MuV accessory protein V (MuV-V). Furthermore, single amino acid substitutions in the Cys-rich region of V protein (Vc189a, Vc207a, and Vc214a) showed that each cysteine residue plays an important role in the decrease in STAT-1 production, but substitution of a histidine residue at amino acid position 203 had no effect. These events and the resultant suppression of the alpha interferon (IFN-{alpha}) response were confirmed by a luciferase reporter gene assay with five tandem repeats of the IFN-{alpha}-stimulated response element as an enhancer element of the firely luciferase gene. STAT-1 production was restored and detectable in FLMT cells treated with a proteosome inhibitor, such as MG132 or lactacystin. In the presence of MG132, ubiquitination of STAT-1 and the interaction of MuV-V with STAT-1 were demonstrated in FLMT cells by immunoprecipitation with anti-STAT-1 antibody. The same results for the interaction and ubiquitination were obtained in experiments with an expression vector for a C-terminal deletion mutant of STAT-1. The truncated STAT-1 molecules were degraded in the presence of MuV-V. Therefore, the C-terminal region (transcriptional activation and Src homology 2 domains) of STAT-1 is not necessary for its degradation caused by MuV-V. Our data suggest that MuV-V promotes ubiquitination and degradation of STAT-1.

* Corresponding author. Mailing address: Department of Microbiology, School of Medicine, Sapporo Medical University, South 1, West 17, Chuo-ku, Sapporo 060-8556, Hokkaido, Japan. Phone: 81-11-611-2111, ext. 2710. Fax: 81-11-612-5861. E-mail: fujii{at}sapmed.ac.jp.

{dagger} Present address: Department of Viral Diseases and Vaccine Control, Murayama Annex, National Institute of Infectious Diseases, Musashi-Murayama, Tokyo 208-0011, Japan

Journal of Virology, December 2002, p. 12683-12690, Vol. 76, No. 24
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.24.12683-12690.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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