期刊
VIRUSES-BASEL
卷 14, 期 12, 页码 -出版社
MDPI
DOI: 10.3390/v14122672
关键词
virus; picornavirus; enterovirus; OSBP; PI4KB
类别
In this study, the essential domains of OSBP for poliovirus replication were identified. The pleckstrin homology domain and the ligand-binding domain were found to be crucial for viral replication, while other domains were not essential. These findings reveal the key role of OSBP in virus replication.
Oxysterol-binding protein (OSBP) is a host factor required for enterovirus (EV) replication. OSBP locates at membrane contact site and acts as a lipid exchanger of cholesterol and phosphatidylinositol 4-phosphate (PI4P) between cellular organelles; however, the essential domains required for the viral replication remain unknown. In this study, we define essential domains of OSBP for poliovirus (PV) replication by a functional dominance assay with a series of deletion variants of OSBP. We show that the pleckstrin homology domain (PHD) and the ligand-binding domain, but not the N-terminal intrinsically disordered domain, coiled-coil region, or the FFAT motif, are essential for PV replication. The PHD serves as the primary determinant of OSBP targeting to the replication organelle in the infected cells. These results suggest that not all the domains that support important biological functions of OSBP are essential for the viral replication.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据