TY - JOUR
T1 - Pathogenesis-related protein 1 suppresses oomycete pathogen by targeting against AMPK kinase complex
AU - Luo, Xiumei
AU - Tian, Tingting
AU - Feng, Li
AU - Yang, Xingyong
AU - Li, Linxuan
AU - Tan, Xue
AU - Wu, Wenxian
AU - Li, Zhengguo
AU - Treves, Haim
AU - Serneels, Francois
AU - Ng, I. Son
AU - Tanaka, Kan
AU - Ren, Maozhi
N1 - Publisher Copyright:
© 2022
PY - 2023/1
Y1 - 2023/1
N2 - Introduction: During the arms race between plants and pathogens, pathogenesis-related proteins (PR) in host plants play a crucial role in disease resistance, especially PR1. PR1 constitute a secretory peptide family, and their role in plant defense has been widely demonstrated in both hosts and in vitro. However, the mechanisms by which they control host-pathogen interactions and the nature of their targets within the pathogen remain poorly understood. Objectives: The present study was aimed to investigate the anti-oomycete activity of secretory PR1 proteins and elaborate their underlying mechanisms. Methods: This study was conducted in the potato-Phytophthora infestans pathosystem. After being induced by the pathogen infection, the cross-kingdom translocation of secretory PR1 was demonstrated by histochemical assays and western blot, and their targets in P. infestans were identified by yeast-two-hybrid assays, bimolecular fluorescence complementation assays, and co-immunoprecipitation assay. Results: The results showed that the expression of secretory PR1-encoding genes was induced during pathogen infection, and the host could deliver PR1 into P. infestans to inhibit its vegetative growth and pathogenicity. The translocated secretory PR1 targeted the subunits of the AMPK kinase complex in P. infestans, thus affecting the AMPK-driven phosphorylation of downstream target proteins, preventing ROS homeostasis, and down-regulating the expression of RxLR effectors. Conclusion: The results provide novel insights into the molecular function of PR1 in protecting plants against pathogen infection, and uncover a potential target for preventing pre- and post-harvest late blight.
AB - Introduction: During the arms race between plants and pathogens, pathogenesis-related proteins (PR) in host plants play a crucial role in disease resistance, especially PR1. PR1 constitute a secretory peptide family, and their role in plant defense has been widely demonstrated in both hosts and in vitro. However, the mechanisms by which they control host-pathogen interactions and the nature of their targets within the pathogen remain poorly understood. Objectives: The present study was aimed to investigate the anti-oomycete activity of secretory PR1 proteins and elaborate their underlying mechanisms. Methods: This study was conducted in the potato-Phytophthora infestans pathosystem. After being induced by the pathogen infection, the cross-kingdom translocation of secretory PR1 was demonstrated by histochemical assays and western blot, and their targets in P. infestans were identified by yeast-two-hybrid assays, bimolecular fluorescence complementation assays, and co-immunoprecipitation assay. Results: The results showed that the expression of secretory PR1-encoding genes was induced during pathogen infection, and the host could deliver PR1 into P. infestans to inhibit its vegetative growth and pathogenicity. The translocated secretory PR1 targeted the subunits of the AMPK kinase complex in P. infestans, thus affecting the AMPK-driven phosphorylation of downstream target proteins, preventing ROS homeostasis, and down-regulating the expression of RxLR effectors. Conclusion: The results provide novel insights into the molecular function of PR1 in protecting plants against pathogen infection, and uncover a potential target for preventing pre- and post-harvest late blight.
KW - AMPK kinase complex
KW - Cross-kingdom translocation
KW - Host-pathogen interaction
KW - Pathogenesis-related protein 1
KW - Phytophthora infestans
KW - Potato late blight
UR - http://www.scopus.com/inward/record.url?scp=85124668073&partnerID=8YFLogxK
U2 - 10.1016/j.jare.2022.02.002
DO - 10.1016/j.jare.2022.02.002
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C2 - 36585103
AN - SCOPUS:85124668073
SN - 2090-1232
VL - 43
SP - 13
EP - 26
JO - Journal of Advanced Research
JF - Journal of Advanced Research
ER -