Activation of c-Jun N-terminal kinase by Akabane virus is required for apoptosis

被引：11

作者：

Mitomo, S. ^{[1
]}

Omatsu, T. ^{[1
]}

Tsuchiaka, S. ^{[1
]}

Nagai, M. ^{[1
]}

Furuya, T. ^{[1
]}

Mizutani, T. ^{[1
]}

机构：

[1] Tokyo Univ Agr & Technol, Res & Educ Ctr Prevent Global Infect Dis Anim, Saiwai Ku, Fuchu, Tokyo 1838509, Japan

来源：

RESEARCH IN VETERINARY SCIENCE | 2016年 / 107卷

关键词：

Akabane virus; Apoptosis; Mitogen-activated protein kinase (MAPK); SIGNALING PATHWAYS; PROTEIN-KINASES; SCHMALLENBERG VIRUS; INFECTION; JNK; REPLICATION; CELLS; STRESS; PHOSPHORYLATION; ARTHROGRYPOSIS;

D O I：

10.1016/j.rvsc.2016.06.007

中图分类号：

S85 [动物医学（兽医学）];

学科分类号：

0906 ;

摘要：

Akabane virus (AKAV) belongs to the Simbu serogroup of the genus Orthobunyavirus in the family Bunyaviridae. It has been shown that AKAV induces apoptosis in mammalian cells. It is necessary to understand the signaling pathways involved in AKAV-induced apoptosis to further elucidate the molecular virology of AKAV. c-Jun N-terminal kinase (INK) and p38 mitogen-activated protein kinase (MAPK) are mediators of apoptosis; therefore, we investigated the roles of JNK and p38 MAPK cascades in AKAV-infected cells. We found that JNK and p38 MAPK as well as their downstream substrates, c-Jun and heat shock protein 27 (HSP27), were phosphorylated in response to AKAV infection. A JNK inhibitor (SP600125) inhibited AKAV-mediated apoptosis whereas a p38 MAPK inhibitor (SB203580) did not. We conclude that AKAV infection activates the JNK and p38 MAPK signaling pathways, and the JNK cascade plays a crucial role in AKAV-induced apoptosis in vitro. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：147 / 151

页数：5

共 47 条

[1] Apoptosis induced by Oropouche virus infection in HeLa cells is dependent on virus protein expression [J].