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NS1-binding protein abrogates the elevation of cell viability by the influenza A virus NS1 protein in association with CRKL

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Biochem Biophys Res Commun_441(4)_953-957.pdf443.5 kBPDF見る/開く
この文献へのリンクには次のURLを使用してください:http://hdl.handle.net/2115/54561

タイトル: NS1-binding protein abrogates the elevation of cell viability by the influenza A virus NS1 protein in association with CRKL
著者: Miyazaki, Masaya 著作を一覧する
Nishihara, Hiroshi 著作を一覧する
Hasegawa, Hideki 著作を一覧する
Tashiro, Masato 著作を一覧する
Wang, Lei 著作を一覧する
Kimura, Taichi 著作を一覧する
Tanino, Mishie 著作を一覧する
Tsuda, Masumi 著作を一覧する
Tanaka, Shinya 著作を一覧する
キーワード: NS1
CrkL
CrkII
NS1-BP
Cell proliferation
ERK
発行日: 2013年11月29日
出版者: Academic press inc elsevier science
誌名: Biochemical and biophysical research communications
巻: 441
号: 4
開始ページ: 953
終了ページ: 957
出版社 DOI: 10.1016/j.bbrc.2013.11.011
抄録: The influenza A virus non-structural protein 1 (NS1) is a multifunctional virulence factor consisting of an RNA binding domain and several Src-homology (SH) 2 and SH3 binding motifs, which promotes virus replication in the host cell and helps to evade antiviral immunity. NS1 modulates general host cell physiology in association with various cellular molecules including NS1-binding protein (NS1-BP) and signaling adapter protein CRK-like (CRKL), while the physiological role of NS1-BP during influenza A virus infection especially in association with NS1 remains unclear. In this study, we analyzed the intracellular association of NS1-BP, NS1 and CRKL to elucidate the physiological roles of these molecules in the host cell. In HEK293T cells, enforced expression of NS1 of A/Beijing (H1N1) and A/Indonesia (H5N1) significantly induced excessive phosphorylation of ERR and elevated cell viability, while the over-expression of NS1-BP and the abrogation of CRKL using siRNA abolished such survival effect of NS1. The pull-down assay using GST-fusion CRKL revealed the formation of intracellular complexes of NS1-BP, NS1 and CRKL. In addition, we identified that the N-terminus SH3 domain of CRKL was essential for binding to NS1-BP using GST-fusion CRKL-truncate mutants. This is the first report to elucidate the novel function of NS1-BP collaborating with viral protein NS1 in modulation of host cell physiology. In addition, an alternative role of adaptor protein CRKL in association with NS1 and NS1-BP during influenza A virus infection is demonstrated. (C) 2013 Elsevier Inc. All rights reserved.
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/54561
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 西原 広史

 

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