Respirovirus C protein inhibits activation of type I interferon receptor-associated kinases to block JAK-STAT signaling

被引：12
|
作者：
Kitagawa, Yoshinori [1 ]
Yamaguchi, Mayu [1 ]
Kohno, Miki [1 ,2 ]
Sakai, Madoka [1 ,2 ]
Itoh, Masae [2 ]
Gotoh, Bin [1 ]
机构：
[1] Shiga Univ Med Sci, Dept Pathol, Div Microbiol & Infect Dis, Seta Tsukinowa Cho, Otsu, Shiga 5202192, Japan
[2] Nagahama Inst Biosci & Technol, Nagahama, Japan
来源：
FEBS LETTERS | 2020年 / 594卷 / 05期
关键词：
C protein; interferon; JAK1; JAK-STAT pathway; respirovirus; Sendai virus; TYK2; VIRUS-V-PROTEIN; SENDAI-VIRUS; ALPHA-INTERFERON; PREVENTING STAT1; WILD-TYPE; P/C GENE; REPLICATION; ANTIINTERFERON; INDUCTION; IFN;
D O I：
10.1002/1873-3468.13670
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Respirovirus C protein blocks the type I interferon (IFN)-stimulated activation of the JAK-STAT pathway. It has been reported that C protein inhibits IFN-alpha-stimulated tyrosine phosphorylation of STATs, but the underlying mechanism is poorly understood. Here, we show that the C protein of Sendai virus (SeV), a member of the Respirovirus genus, binds to the IFN receptor subunit IFN-alpha/beta receptor subunit (IFNAR)2 and inhibits IFN-alpha-stimulated tyrosine phosphorylation of the upstream receptor-associated kinases, JAK1 and TYK2. Analysis of various SeV C mutant (Cm) proteins demonstrates the importance of the inhibitory effect on receptor-associated kinase phosphorylation for blockade of JAK-STAT signaling. Furthermore, this inhibitory effect and the IFNAR2 binding capacity are observed for all the respirovirus C proteins examined. Our results suggest that respirovirus C protein inhibits activation of the receptor-associated kinases JAK1 and TYK2 possibly through interaction with IFNAR2.
引用
收藏
页码：864 / 877
页数：14
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