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The YLDL sequence within Sendai virus m protein is critical for budding of virus-like particles and interacts with Alix/AIP1 independently of C protein

https://hiroshima.repo.nii.ac.jp/records/2007572
https://hiroshima.repo.nii.ac.jp/records/2007572
ebd865fa-f372-41ef-9247-9ba9e1cc0565
名前 / ファイル ライセンス アクション
JVI_81-5_2263.pdf JVI_81-5_2263.pdf (248.0 KB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル The YLDL sequence within Sendai virus m protein is critical for budding of virus-like particles and interacts with Alix/AIP1 independently of C protein
言語 en
作成者 Irie, Takashi

× Irie, Takashi

en Irie, Takashi

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Shimazu, Yukie

× Shimazu, Yukie

en Shimazu, Yukie

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Yoshida, Tetsuya

× Yoshida, Tetsuya

en Yoshida, Tetsuya

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Sakaguchi, Takemasa

× Sakaguchi, Takemasa

en Sakaguchi, Takemasa

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 Copyright (c) 2007 American Society for Microbiology
主題
主題Scheme NDC
主題 490
内容記述
内容記述 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.
言語 en
出版者
出版者 American Society for Microbiology
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
出版タイプ
出版タイプ AO
出版タイプResource http://purl.org/coar/version/c_b1a7d7d4d402bcce
関連情報
識別子タイプ DOI
関連識別子 10.1128/JVI.02218-06
関連情報
識別子タイプ DOI
関連識別子 http://dx.doi.org/10.1128/JVI.02218-06
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0022-538X
収録物識別子
収録物識別子タイプ NCID
収録物識別子 AA00708779
開始ページ
開始ページ 2263
書誌情報 Journal of Virology
Journal of Virology

巻 81, 号 5, p. 2263-2273, 発行日 2007-03
旧ID 20596
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