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Journal of Virology, April 2005, p. 4451-4459, Vol. 79, No. 7
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.7.4451-4459.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mumps Virus V Protein Antagonizes Interferon without the Complete Degradation of STAT1

Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, Tokyo,¹ Department of Microbiology, School of Medicine, Sapporo Medical University, Sapporo, Hokkaido, Japan²

Received 5 September 2004/ Accepted 5 November 2004

Mumps virus (MuV) has been shown to antagonize the antiviral effects of interferon (IFN) through proteasome-mediated complete degradation of STAT1 by using the viral V protein (T. Kubota et al., Biochem. Biophys. Res. Commun. 283:255-259, 2001). However, we found that MuV could inhibit IFN signaling and the generation of a subsequent antiviral state long before the complete degradation of cellular STAT1 in infected cells. In MuV-infected cells, nuclear translocation and phosphorylation of STAT1 and STAT2 tyrosine residue (Y) at 701 and 689, respectively, by IFN-ß were significantly inhibited but the phosphorylation of Jak1 and Tyk2 was not inhibited. The transiently expressed MuV V protein also inhibited IFN-ß-induced Y⁷⁰¹-STAT1 and Y⁶⁸⁹-STAT2 phosphorylation, suggesting that the V protein could block IFN-ß-induced signal transduction without the aid of other viral components. Finally, a substitution of an alanine residue in place of a cysteine residue in the C-terminal V-unique region known to be required for STAT1 degradation and inhibition of anti-IFN signaling resulted in the loss of V protein function to inhibit the Y⁷⁰¹-STAT1 and Y⁶⁸⁹-STAT2 phosphorylation.

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