RH3 enhances antiviral defense by facilitating small RNA loading into Argonaute 2 at endoplasmic reticulum–chloroplast membrane contact sites

Juan Huang, Juan Du, Yan Liu, Lu Lu, Yanzhuo Xu, Jianfei Shi, Qing Liu, Qi Li, Yang Liu, Yaqiu Chen, Meng Du, Yiming Zhao, Liangxiao Huo, Weiran Wang, Chenxi Ding, Liya Wei, Jianguo Wu, Yao-Wu Yuan, Jinfeng Chen, Ruixi Li, Feng Cui () and Xiaoming Zhang ()
Additional contact information
Juan Huang: Chinese Academy of Sciences
Juan Du: Chinese Academy of Sciences
Yan Liu: Chinese Academy of Sciences
Lu Lu: Chinese Academy of Sciences
Yanzhuo Xu: Chinese Academy of Sciences
Jianfei Shi: Chinese Academy of Sciences
Qing Liu: Chinese Academy of Sciences
Qi Li: Chinese Academy of Sciences
Yang Liu: Chinese Academy of Sciences
Yaqiu Chen: Chinese Academy of Sciences
Meng Du: Chinese Academy of Sciences
Yiming Zhao: Chinese Academy of Sciences
Liangxiao Huo: Baoding
Weiran Wang: Baoding
Chenxi Ding: Baoding
Liya Wei: Baoding
Jianguo Wu: Fujian Agriculture and Forestry University
Yao-Wu Yuan: Unit 3043
Jinfeng Chen: Chinese Academy of Sciences
Ruixi Li: Shenzhen
Feng Cui: Chinese Academy of Sciences
Xiaoming Zhang: Chinese Academy of Sciences

Nature Communications, 2025, vol. 16, issue 1, 1-17

Abstract: Abstract While RNA silencing is crucial for plant resistance against viruses, the cellular connections between RNA silencing and antiviral responses in plants remain poorly understood. In this study, we aim to investigate this relationship by examining the subcellular localization of small RNA loading and viral replication in Arabidopsis. Our findings reveal that Argonaute 2 (AGO2), a key component of RNA silencing, loads small RNAs at the endoplasmic reticulum (ER)–chloroplast membrane contact sites (MCSs). We identify a chloroplast-localized protein, RNA helicase 3 (RH3), which interacts with AGO2 and facilitates the loading of small RNAs into AGO2 at these MCSs. Furthermore, we discover that MCSs serve as replication sites for certain plant viruses. RH3 also promotes the loading of viral-derived small RNAs into AGO2, thereby enhancing plant antiviral resistance. Overall, our study sheds light on the roles of RH3 in RNA silencing and plant antiviral defenses, providing valuable insights into the cytobiological connections between RNA silencing, viral replication, and antiviral immunity.

Date: 2025
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DOI: 10.1038/s41467-025-57296-6

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