Document Type
Article
Publication Date
6-11-2025
Publication Title
Plant Cell
Abstract
Fungi secrete effector proteins, including extracellular redox enzymes, to inhibit host immunity. Redox enzymes have been hypothesized to inhibit host reactive oxygen species (ROS); however, how they suppress host immunity remains unknown. We characterized an extracellular ascorbate peroxidase (MoApx1) that is secreted into rice chloroplasts by the rice blast fungus Magnaporthe oryzae. MoApx1 displays multifunctional capabilities that significantly contribute to fungal virulence. Firstly, MoApx1 neutralizes host-derived H2O2 within the chloroplast through its peroxidase activity, thereby inhibiting chloroplast ROS (cROS)-mediated defense responses. Secondly, MoApx1 targets the photosystem I subunit OsPsaD, disrupting photosynthetic electron transport to further suppress cROS production. Most importantly, MoApx1 has evolved a fungal-specific starch-binding domain that binds host starch, inhibiting its degradation and disrupting the energy supply required for host resistance. Our findings underscore the importance of a novel multifaceted strategy, potentially widely employed by other fungal pathogens, in suppressing host immunity during host–microbe interactions.
PubMed ID
40497787
Volume
37
Issue
7
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Liu, Muxing; Guo, Ziqian; Hu, Jiexiong; Chen, Yuke; Chen, Fang; Chen, Weizhong; Wang, Wenya; Ye, Boyang; Yang, Zhixiang; Li, Gang; Liu, Xinyu; Zhang, Haifeng; Wang, Ping; and Zhang, Zhengguang, "The multifunctional ascorbate peroxidase MoApx1 secreted by Magnaporthe oryzae mediates the suppression of rice immunity" (2025). School of Graduate Studies Faculty Publications. 377.
https://digitalscholar.lsuhsc.edu/sogs_facpubs/377
10.1093/plcell/koaf146
Included in
Amino Acids, Peptides, and Proteins Commons, Enzymes and Coenzymes Commons, Fungi Commons, Medical Immunology Commons, Plants Commons