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Two plant membrane-shaping reticulon-like proteins play contrasting complex roles in turnip mosaic virus infection

文献类型： 外文期刊

作者： Wu, Guanwei 1 ; Wang, Liping 1 ; He, Rongrong 1 ; Cui, Xiaoyan 2 ; Chen, Xin 2 ; Wang, Aiming 1 ;

作者机构： 1.Agr & Agrifood Canada, London Res & Dev Ctr, London, ON, Canada

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

3.Ningbo Univ, Inst Plant Virol, State Key Lab Managing Biot & Chem Threats Qual &, Ningbo, Peoples R China

4.Huazhong Agr Univ, State Key Lab Agr Microbiol, Wuhan, Peoples R China

5.Western Univ, Dept Biol, London, ON, Canada

关键词： antiviral factor; cell-to-cell movement; Potyvirus; proviral factor; reticulon; virus replication complex

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：4.9； 五年影响因子：5.6 ）

ISSN： 1464-6722

年卷期： 2024 年 25 卷 10 期

页码：

收录情况： SCI

摘要： Positive-sense RNA viruses remodel cellular cytoplasmic membranes as the membranous sources for the formation of viral replication organelles (VROs) for viral genome replication. In plants, they traffic through plasmodesmata (PD), plasma membrane-lined pores enabling cytoplasmic connections between cells for intercellular movement and systemic infection. In this study, we employed turnip mosaic virus (TuMV), a plant RNA virus to investigate the involvement of RTNLB3 and RTNLB6, two ER (endoplasmic reticulum) membrane-bending, PD-located reticulon-like (RTNL) non-metazoan group B proteins (RTNLBs) in viral infection. We show that RTNLB3 interacts with TuMV 6K2 integral membrane protein and RTNLB6 binds to TuMV coat protein (CP). Knockdown of RTNLB3 promoted viral infection, whereas downregulation of RTNLB6 restricted viral infection, suggesting that these two RTNLs play contrasting roles in TuMV infection. We further demonstrate that RTNLB3 targets the alpha-helix motif (LRKSM46)-L-42 of 6K2 to interrupt 6K2 self-interactions and compromise 6K2-induced VRO formation. Moreover, overexpression of AtRTNLB3 apparently promoted the selective degradation of the ER and ER-associated protein calnexin, but not 6K2. Intriguingly, mutation of the alpha-helix motif of 6K2 that is required for induction of VROs severely affected 6K2 stability and abolished TuMV infection. Thus, RTNLB3 attenuates TuMV replication, probably through the suppression of 6K2 function. We also show that RTNLB6 promotes viral intercellular movement but does not affect viral replication. Therefore, the proviral role of RTNLB6 is probably by enhancing viral cell-to-cell trafficking. Taken together, our data demonstrate that RTNL family proteins may play diverse complex, even opposite, roles in viral infection in plants.

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