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

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.

journal_name

Cell Host Microbe

journal_title

Cell host & microbe

authors

Fujioka Y,Nishide S,Ose T,Suzuki T,Kato I,Fukuhara H,Fujioka M,Horiuchi K,Satoh AO,Nepal P,Kashiwagi S,Wang J,Horiguchi M,Sato Y,Paudel S,Nanbo A,Miyazaki T,Hasegawa H,Maenaka K,Ohba Y

doi

10.1016/j.chom.2018.04.015

subject

Has Abstract

pub_date

2018-06-13 00:00:00

pages

809-818.e5

issue

6

eissn

1931-3128

issn

1934-6069

pii

S1931-3128(18)30216-6

journal_volume

23

pub_type

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