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Journal of Virology, July 2005, p. 8933-8941, Vol. 79, No. 14
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.14.8933-8941.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

AIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding

Takemasa Sakaguchi,1* Atsushi Kato,2 Fumihiro Sugahara,1 Yukie Shimazu,1 Makoto Inoue,3 Katsuhiro Kiyotani,1 Yoshiyuki Nagai,4 and Tetsuya Yoshida1

Department of Virology, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8551,1 Department of Virology 3, National Institute of Infectious Diseases, Musashi-Murayama, Tokyo 208-0011,2 DNAVEC Corporation, Tsukuba, Ibaraki 305-0856,3 Toyama Institute of Health, Imizu-gun, Toyama 939-0363, Japan4

Received 26 January 2005/ Accepted 24 March 2005

The C protein, an accessory protein of Sendai virus (SeV), has anti-interferon capacity and suppresses viral RNA synthesis. In addition, it is thought that the C protein is involved in virus budding because of the low efficiency of release of progeny virions from C-knockout virus-infected cells and because of the requirement of the C protein for efficient release of virus-like particles. Here, we identified AIP1/Alix, a host protein involved in apoptosis and endosomal membrane trafficking, as an interacting partner of the C protein using a yeast two-hybrid system. The amino terminus of AIP1/Alix and the carboxyl terminus of the C protein are important for the interaction in mammalian cells. Mutant C proteins unable to bind AIP1/Alix failed to accelerate the release of virus-like particles from cells. Furthermore, overexpression of AIP1/Alix enhanced SeV budding from infected cells in a C-protein-dependent manner, while the release of nucleocapsid-free empty virions was also enhanced. Finally, AIP1/Alix depletion by small interfering RNA resulted in suppression of SeV budding. The results of this study suggest that AIP1/Alix plays a role in efficient SeV budding and that the SeV C protein facilitates virus budding through interaction with AIP1/Alix.

* Corresponding author. Mailing address: Department of Virology, Graduate School of Biomedical Sciences, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan. Phone: 81-82-257-5157. Fax: 81-82-257-5159. E-mail: tsaka{at}hiroshima-u.ac.jp.

Journal of Virology, July 2005, p. 8933-8941, Vol. 79, No. 14
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.14.8933-8941.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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