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A plant RNA virus hijacks endocytic proteins to establish its infection in plants

文献类型： 外文期刊

作者： Wu, Guanwei 1 ; Cui, Xiaoyan 2 ; Dai, Zhaoji 1 ; He, Rongrong 1 ; Li, Yinzi 1 ; Yu, Kangfu 4 ; Bernards, Mark 3 ; Chen, X 1 ;

作者机构： 1.Agr & Agri Food Canada, London Res & Dev Ctr, 1391 Sandford St, London, ON N5V 4T3, Canada

2.Jiangsu Acad Agr Sci, Inst Ind Crops, Jiangsu Key Lab Hort Crop Genet Improvement, Nanjing 210014, Jiangsu, Peoples R China

3.Univ Western Ontario, Dept Biol, 1151 Richmond ST, London, ON N6A 5B7, Canada

4.Agr & Agri Food Canada, Harrow Res & Dev Ctr, 2585 Cty Rd 20, Harrow, ON N0R 1G0, Canada

关键词： RNA virus; potyvirus; Turnip mosaic virus; Arabidopsis thaliana; Nicotiana benthamiana; dynamin; adaptor protein 2; endocytosis; virus replication complex; host factor

期刊名称：PLANT JOURNAL （ 影响因子：6.417； 五年影响因子：7.627 ）

ISSN： 0960-7412

年卷期： 2020 年 101 卷 2 期

页码：

收录情况： SCI

摘要： Endocytosis and endosomal trafficking play essential roles in diverse biological processes including responses to pathogen attack. It is well established that animal viruses enter host cells through receptor-mediated endocytosis for infection. However, the role of endocytosis in plant virus infection still largely remains unknown. Plant dynamin-related proteins 1 (DRP1) and 2 (DRP2) are the large, multidomain GTPases that participate together in endocytosis. Recently, we have discovered that DRP2 is co-opted by Turnip mosaic virus (TuMV) for infection in plants. We report here that DRP1 is also required for TuMV infection. We show that overexpression of DRP1 from Arabidopsis thaliana (AtDRP1A) promotes TuMV infection, and AtDRP1A interacts with several viral proteins including VPg and cylindrical inclusion (CI), which are the essential components of the virus replication complex (VRC). AtDRP1A colocalizes with the VRC in TuMV-infected cells. Transient expression of a dominant negative (DN) mutant of DRP1A disrupts DRP1-dependent endocytosis and supresses TuMV replication. As adaptor protein (AP) complexes mediate cargo selection for endocytosis, we further investigated the requirement of AP in TuMV infection. Our data suggest that the medium unit of the AP2 complex (AP2 beta) is responsible for recognizing the viral proteins as cargoes for endocytosis, and knockout of AP2 beta impairs intracellular endosomal trafficking of VPg and CI and inhibits TuMV replication. Collectively, our results demonstrate that DRP1 and AP2 beta are two proviral host factors of TuMV and shed light into the involvement of endocytosis and endosomal trafficking in plant virus infection.

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