An article A fungal effector and a rice NLR protein have antagonistic effects on a Bowman-Birk trypsin inhibitor WOS:000545116200001 published article about BLAST RESISTANCE; PHYTOPHTHORA-INFESTANS; PROTEASES; DEFENSE; IMMUNITY; TARGETS; BBI; PATHOGENS; TRIGGERS; ENCODES in [Zhang, Chongyang; Fang, Hong; Shi, Xuetao; He, Feng; Wang, Ruyi; Fan, Jiangbo; Wang, Jiyang; Zhou, Xueping; Ning, Yuese] Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China; [Zhang, Chongyang; Fan, Jiangbo; Bai, Pengfei; Park, Chan-Ho; Bellizzi, Maria; Wang, Guo-Liang] Ohio State Univ, Dept Plant Pathol, Columbus, OH 43210 USA in 2020.0, Cited 47.0. The Name is 1H-1,2,4-Triazol-5-amine. Through research, I have a further understanding and discovery of 61-82-5. Computed Properties of C2H4N4
Bowman-Birk trypsin inhibitors (BBIs) play important roles in animal and plant immunity, but how these protease inhibitors are involved in the immune system remains unclear. Here, we show that the rice (Oryza sativa) BBI protein APIP4 is a common target of a fungal effector and an NLR receptor for innate immunity. APIP4 exhibited trypsin inhibitor activityin vitroandin vivo. Knockout ofAPIP4in rice enhanced susceptibility, and overexpression ofAPIP4increased resistance to the fungal pathogenMagnaporthe oryzae. TheM. oryzaeeffector AvrPiz-t interacted with APIP4 and suppressed APIP4 trypsin inhibitor activity. By contrast, the rice NLR protein Piz-t interacted with APIP4, enhancing APIP4 transcript and protein levels, and protease inhibitor activity. Our findings reveal a novel host defence mechanism in which a host protease inhibitor targeted by a fungal pathogen is protected by an NLR receptor.
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Reference:
Article; Safari, Niloufar; Shirini, Farhad; Tajik, Hassan; Journal of Molecular Structure; vol. 1201; (2020);,
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