Decoy engineering of the receptor-like cytoplasmic kinase StPBS1 to defend against virus infection in potato |
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Authors: | Runyao Bai Huanhuan Li Wenjia Du Niu Niu Wenxia Li Qican Gao Chongyang Yao Zikai Zhou Wenhua Bao Mingjia Che Yongxiu Zhao Bin Zhou Yaohui Wang Hada Wuriyanghan |
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Affiliation: | 1. Key Laboratory of Forage and Endemic Crop Biotechnology, Ministry of Education, School of Life Sciences, Inner Mongolia University, Hohhot, China;2. Crop Research Institute of Anhui Academy of Agricultural Sciences, Hefei, China;3. School of Biological Science and Technology, Baotou Teachers College, Baotou, China |
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Abstract: | Potato virus Y (PVY) is an important pathogen of potato (Solanum tuberosum). Although the PBS1–RPS5 immune system is well documented in Arabidopsis thaliana, it has not been reported in potato. In Arabidopsis, the bacterial effector AvrPphB cleaves AtPBS1 to trigger an immune response. Here, we show that the AvrPphB-triggered immune response is mediated by StPBS1, a close homologue of AtPBS1 in potato. However, downstream signalling of StPBS1 was mediated by unknown resistance (R) proteins other than potato orthologues of AtRPS5 and HvPBR1, which is important for HvPBS1 signalling in barley. Immune signalling of StPBS1 is mediated by the AvrPphB C-terminal cleavage domain and an STKPQ motif, in contrast to AtPBS1-mediated immunity in which both AvrPphB cleavage fragments and an SEMPH motif are essential. The cleavage sequence of AvrPphB in StPBS1 was replaced with that of the PVY NIa-Pro protease to obtain StPBS1NIa. StPBS1NIa overexpression potato displayed stronger immunity to PVY infection than did the StPBS1 transgenic lines. StPBS1NIa was cleaved at the expected target site by NIa-Pro protease from PVY. Thus, we characterized the function of StPBS1 in potato immunity and provide a biotechnology control method for PVY via transformation of decoy-engineered StPBS1NIa. |
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Keywords: | AvrPphB decoy engineering immune signalling potato virus Y resistance protein StPBS1 transgenic potato |
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