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N-linked glycan in tick-borne encephalitis virus envelope protein affects viral secretion in mammalian cells, but not in tick cells

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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/2115/56524

タイトル: N-linked glycan in tick-borne encephalitis virus envelope protein affects viral secretion in mammalian cells, but not in tick cells
著者: Yoshii, Kentaro 著作を一覧する
Yanagihara, Natsumi 著作を一覧する
Ishizuka, Mariko 著作を一覧する
Sakai, Mizuki 著作を一覧する
Kariwa, Hiroaki 著作を一覧する
発行日: 2013年10月
出版者: Society for General Microbiology
誌名: Journal of General Virology
巻: 94
開始ページ: 2249
終了ページ: 2258
出版社 DOI: 10.1099/vir.0.055269-0
抄録: Tick-borne encephalitis virus (TBEV) is a zoonotic disease agent that causes severe encephalitis in humans. The envelope protein E of TBEV has one N-linked glycosylation consensus sequence, but little is known about the biological function of the N-linked glycan. In this study, the function of protein E glycosylation was investigated using recombinant TBEV with or without the protein E N-linked glycan. Virion infectivity was not affected after removing the N-linked glycans using N-glycosidase F. In mammalian cells, loss of glycosylation affected the conformation of protein E during secretion, reducing the infectivity of secreted virions. Mice subcutaneously infected with TBEV lacking protein E glycosylation showed no signs of disease, and viral multiplication in peripheral organs was reduced relative to that with the parental virus. In contrast, loss of glycosylation did not affect the secretory process of infectious virions in tick cells. Furthermore, inhibition of transport to the Golgi apparatus affected TBEV secretion in mammalian cells, but not in tick cells, indicating that TBEV was secreted through an unidentified pathway after synthesis in endoplasmic reticulum in tick cells. These results increase our understanding of the molecular mechanisms of TBEV maturation.
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/56524
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 好井 健太朗

 

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