The P2 of Wheat yellow mosaic virus rearranges the endoplasmic reticulum and recruits other viral proteins into replication-associated inclusion bodies

文献类型： 外文期刊

第一作者： Sun, Liying

作者： Sun, Liying;Andika, Ida Bagus;Chen, Jianping;Shen, Jiangfeng;Yang, Di

作者机构：

关键词： endoplasmic reticulum;Wheat yellow mosaic virus;protein localization;replication-associated inclusion bodies;rearrange

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：5.663； 五年影响因子：5.626 ）

ISSN： 1464-6722

年卷期： 2014 年 15 卷 5 期

页码：

收录情况： SCI

摘要： Viruses commonly modify host endomembranes to facilitate biological processes in the viral life cycle. Infection by viruses belonging to the genus Bymovirus (family Potyviridae) has long been known to induce the formation of large membranous inclusion bodies in host cells, but their assembly and biological roles are still unclear. Immunoelectron microscopy of cells infected with the bymovirus Wheat yellow mosaic virus (WYMV) showed that P1, P2 and P3 are the major viral protein constituents of the membranous inclusions, whereas NIa-Pro (nuclear inclusion-a protease) and VPg (viral protein genome-linked) are probable minor components. P1, P2 and P3 associated with the endoplasmic reticulum (ER), but only P2 was able to rearrange ER and form large aggregate structures. Bioinformatic analyses and chemical experiments showed that P2 is an integral membrane protein and depends on the active secretory pathway to form aggregates of ER membranes. In planta and in vitro assays demonstrated that P2 interacts with P1, P3, NIa-Pro or VPg and recruits these proteins into the aggregates. In vivo RNA labelling using WYMV-infected wheat protoplasts showed that the synthesis of viral RNAs occurs in the P2-associated inclusions. Our results suggest that P2 plays a major role in the formation of membranous compartments that house the genomic replication of WYMV.

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