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タイトル	en Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles
作成者	en Nanbo, Asuka NRID 1000060359487 en Maruyama, Junki en Imai, Masaki en Ujie, Michiko en Fujioka, Yoichiro en Nishide, Shinya NRID 1000040451398 en Takada, Ayato NRID 1000010292062 en Ohba, Yusuke NRID 1000030333503 en Kawaoka, Yoshihiro NRID 1000070135838
アクセス権	open access
権利情報	http://creativecommons.org/licenses/by/4.0/ en Creative Commons Attribution 4.0 International
主題	NDC 490
内容注記	Abstract en Cell surface receptors for phosphatidylserine contribute to the entry of Ebola virus (EBOV) particles, indicating that the presence of phosphatidylserine in the envelope of EBOV is important for the internalization of EBOV particles. Phosphatidylserine is typically distributed in the inner layer of the plasma membrane in normal cells. Progeny virions bud from the plasma membrane of infected cells, suggesting that phosphatidylserine is likely flipped to the outer leaflet of the plasma membrane in infected cells for EBOV virions to acquire it. Currently, the intracellular dynamics of phosphatidylserine during EBOV infection are poorly understood. Here, we explored the role of XK-related protein (Xkr) 8, which is a scramblase responsible for exposure of phosphatidylserine in the plasma membrane of apoptotic cells, to understand its significance in phosphatidylserine-dependent entry of EBOV. We found that Xkr8 and transiently expressed EBOV glycoprotein GP often co-localized in intracellular vesicles and the plasma membrane. We also found that co-expression of GP and viral major matrix protein VP40 promoted incorporation of Xkr8 into ebolavirus-like particles (VLPs) and exposure of phosphatidylserine on their surface, although only a limited amount of phosphatidylserine was exposed on the surface of the cells expressing GP and/or VP40. Downregulating Xkr8 or blocking caspase-mediated Xkr8 activation did not affect VLP production, but they reduced the amount of phosphatidylserine on the VLPs and their uptake in recipient cells. Taken together, our findings indicate that Xkr8 is trafficked to budding sites via GP-containing vesicles, is incorporated into VLPs, and then promote the entry of the released EBOV to cells in a phosphatidylserine-dependent manner.
出版者	en PLOS
日付	Issued2018-01
言語	eng
資源タイプ	journal article
出版タイプ	VoR
資源識別子	HDL http://hdl.handle.net/2115/68604
関連	isIdenticalTo DOI https://doi.org/10.1371/journal.ppat.1006848
収録誌情報	PISSN 1553-7366 en PLOS pathogens 巻14 号1 開始ページe1006848
ファイル	fulltext journal.ppat.1006848.pdf 2.5 MB (application/pdf) Issued2018-01 fulltext journal.ppat.1006848.s001.tiff 149.75 KB (image/tiff) Issued2018-01 fulltext journal.ppat.1006848.s002.tiff 199.11 KB (image/tiff) Issued2018-01 fulltext journal.ppat.1006848.s003.pdf 3.62 MB (application/pdf) Issued2018-01 fulltext journal.ppat.1006848.s004.tiff 2.14 MB (image/tiff) Issued2018-01 fulltext journal.ppat.1006848.s005.tiff 1000.66 KB (image/tiff) Issued2018-01
コンテンツ更新日時	2023-07-26