Activation of c-Jun N-terminal kinase by Akabane virus is required for apoptosis. (August 2016)

• Record Type: Journal Article
• Authors: Mitomo, S.; Omatsu, T.; Tsuchiaka, S.; Nagai, M.; Furuya, T.; Mizutani, T.
• Is Part Of: Research in veterinary science. Volume 107(2016)
• Page Start: 147
• Page End: 151
• Publication Date: 2016-08
• Subjects: Akabane virus -- Apoptosis -- Mitogen-activated protein kinase (MAPK); Veterinary medicine -- Periodicals; Veterinary Medicine -- Periodicals; Médecine vétérinaire -- Périodiques; Médecine vétérinaire -- Recherche -- Périodiques; Diergeneeskunde; 636.089
• DOI: 10.1016/j.rvsc.2016.06.007
• Languages: English
• ISSNs: 0034-5288

Abstract

Abstract: 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 (JNK) 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. Highlights: JNK and p38 MAPK were phosphorylated in response to Akabane virus infection. Downstream substrates, c-Jun and heat shock protein 27, were also phosphorylated by viral infection. JNK inhibitor (SP600125) inhibited AKAV-mediated apoptosis whereas a p38 MAPK inhibitor (SB203580) did not.