Open AccessAIP1/Alix Is a Binding Partner of Sendai Virus C Protein and Facilitates Virus Budding
Author(s) -
Takemasa Sakaguchi,
Atsushi Kato,
Fumihiro Sugahara,
Yukie Shimazu,
Makoto Inoue,
Katsuhiro Kiyotani,
Yoshinori Nagai,
Takemi Yoshida
Publication year - 2005
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.79.14.8933-8941.2005
Subject(s) - sendai virus , budding , vp40 , biology , virus , small interfering rna , escrt , rna , virology , endosome , viral matrix protein , microbiology and biotechnology , gene , biochemistry , intracellular
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.