A viral protein activates the MAPK pathway to promote viral infection by downregulating callose deposition in plants

Lixiao Feng, Xiangwen Luo, Liping Huang, Yu Zhang, Fangfang Li, Shijun Li, Zhanhong Zhang, Xiao Yang, Xin Wang, Xian OuYang, Xiaobin Shi, Deyong Zhang, Xiaorong Tao, Jianping Chen, Jian Yang (), Songbai Zhang () and Yong Liu ()
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Lixiao Feng: Biology College of Hunan University
Xiangwen Luo: Institute of Plant Protection of Hunan Academy of Agricultural Science
Liping Huang: Institute of Plant Protection of Hunan Academy of Agricultural Science
Yu Zhang: Institute of Plant Protection of Hunan Academy of Agricultural Science
Fangfang Li: Chinese Academy of Agricultural Sciences
Shijun Li: Hunan Agricultural University
Zhanhong Zhang: Biology College of Hunan University
Xiao Yang: Biology College of Hunan University
Xin Wang: Biology College of Hunan University
Xian OuYang: Institute of Plant Protection of Hunan Academy of Agricultural Science
Xiaobin Shi: Biology College of Hunan University
Deyong Zhang: Biology College of Hunan University
Xiaorong Tao: Nanjing Agricultural University
Jianping Chen: Ningbo University
Jian Yang: Ningbo University
Songbai Zhang: Biology College of Hunan University
Yong Liu: Biology College of Hunan University

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Mitogen-activated protein kinase (MAPK) cascades are evolutionarily conserved in both plants and animals and play critical roles in activating innate immunity to defend against various pathogens. However, the role of MAPK cascades in positively regulating or enhancing viral infections in plants is unclear. In this study, we investigate the involvement of MAPK cascades in infection by the positive-strand RNA virus tomato chlorosis virus (ToCV). Our findings reveal that ToCV infection activates MAPK cascades, promoting virus spread within plants. Specifically, ToCV P7, a pathogenicity determinant protein, localizes to the plasma membrane and recruits NbMPK3/6 from the nucleus. Subsequently, P7 is directly phosphorylated on serine 59 by NbMPK3/6. Phosphorylated P7 interacts with NbREM1.1 and inhibits its ability to induce callose deposition at plasmodesmata. These results demonstrate that NbMPK3/6 directly phosphorylate ToCV P7, modulating antiviral defence mechanisms by downregulating callose deposition at plasmodesmata and thereby enhancing ToCV transmission in N. benthamiana. This study sheds light on the intricate arms race between host defence and viral counter-defence strategies.

Date: 2024
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DOI: 10.1038/s41467-024-54467-9

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