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ID 20596
本文ファイル
著者
Shimazu, Yukie
Yoshida, Tetsuya
NDC
医学
抄録(英)
For many enveloped viruses, cellular multivesicular body (MVB) sorting machinery has been reported to be utilized for efficient viral budding. Matrix and Gag proteins have been shown to contain one or two L-domain motifs (PPxY, PT/SAP, YPDL, and FPIV), some of which interact specifically with host cellular proteins involved in multivesicular body sorting, which are recruited to the viral budding site. However, for many enveloped viruses, L-domain motifs have not yet been identified, and the involvement of MVB sorting machinery in viral budding is still unknown. Here we show that both Sendai virus (SeV) matrix protein M and accessory protein C contribute to virus budding by physically interacting with Alix/AIP1. A YLDL sequence within the M protein showed L-domain activity, and its specific interaction with the N-terminus of Alix/AIP1 (1-211) was important for the budding of virus-like particles (VLPs) of M protein. In addition, M-VLP budding was inhibited by the overexpression of some deletion mutants of Alix/AIP1 and depletion of endogenous Alix/AIP1 using specific siRNAs. The YLDL sequence was not replaceable by other L-domain motifs, such as PPxY and PT/SAP, and even YPxL. C protein was also able to physically interact with the N-terminus of Alix/AIP1 (212-357) and enhanced M-VLP budding independently of M-Alix/AIP1 interaction, although it was not released from the transfected cells itself. Our results suggest that the interaction of multiple viral proteins with Alix/AIP1 may enhance the efficiency of the utilization of cellular MVB sorting machinery for efficient SeV budding.
掲載誌名
Journal of Virology
81巻
5号
開始ページ
2263
終了ページ
2273
出版年月日
2007-03
出版者
American Society for Microbiology
ISSN
0022-538X
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
Copyright (c) 2007 American Society for Microbiology
関連情報URL
部局名
医歯薬学総合研究科