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A Sialylated Voltage-Dependent Ca2+ Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into Mammalian Cells

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/74619

Title: A Sialylated Voltage-Dependent Ca2+ Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into Mammalian Cells
Authors: Fujioka, Yoichiro Browse this author
Nishide, Shinya Browse this author →KAKEN DB
Ose, Toyoyuki Browse this author →KAKEN DB
Suzuki, Tadaki Browse this author →KAKEN DB
Kato, Izumi Browse this author
Fukuhara, Hideo Browse this author
Fujioka, Mari Browse this author
Horiuchi, Kosui Browse this author
Satoh, Aya O. Browse this author
Nepal, Prabha Browse this author
Kashiwagi, Sayaka Browse this author
Wang, Jing Browse this author
Horiguchi, Mika Browse this author
Sato, Yuko Browse this author
Paudel, Sarad Browse this author
Nanbo, Asuka Browse this author →KAKEN DB
Miyazaki, Tadaaki Browse this author →KAKEN DB
Hasegawa, Hideki Browse this author
Maenaka, Katsumi Browse this author →KAKEN DB
Ohba, Yusuke Browse this author →KAKEN DB
Keywords: influenza A virus
virus entry
calcium ion
calcium channel
calcium channel blockers
hemagglutinin
sialylation
virus-host cell interaction
Issue Date: 13-Jun-2018
Publisher: Cell Press
Journal Title: Cell host & microbe
Volume: 23
Issue: 6
Start Page: 809
End Page: 818
Publisher DOI: 10.1016/j.chom.2018.04.015
Abstract: Influenza A virus (IAV) infection is initiated by the attachment of the viral glycoprotein hemagglutinin (HA) to sialic acid on the host cell surface. However, the sialic acid-containing receptor crucial for IAV infection has remained unidentified. Here, we show that HA binds to the voltage-dependent Ca2+ channel Cav1.2 to trigger intracellular Ca2+ oscillations and subsequent IAV entry and replication. IAV entry was inhibited by Ca2+ channel blockers (CCBs) or by knockdown of Cav1.2. The CCB diltiazem also inhibited virus replication in vivo. Reintroduction of wild-type but not the glycosylation-deficient mutants of Cav1.2 restored Ca2+ oscillations and virus infection in Cav1.2-depleted cells, demonstrating the significance of Cav1.2 sialylation. Taken together, we identify Cav1.2 as a sialylated host cell surface receptor that binds HA and is critical for IAV entry.
Rights: © 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
http://creativecommons.org/licenses/by-nc-nd/4.0/
Type: article (author version)
URI: http://hdl.handle.net/2115/74619
Appears in Collections:医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 大場 雄介

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