Effects of Stripe Rust Infection on the Levels of Redox Balance and Photosynthetic Capacities in Wheat

• Main Authors: Yanger Chen, Haotian Mao, Nan Wu, Jie Ma, Ming Yuan, Zhongwei Zhang, Shu Yuan, Huaiyu Zhang
• Format: Article
• Language: English
• Published: MDPI AG 2019-12-01
• Series: International Journal of Molecular Sciences
• Subjects: stripe rust; antioxidant enzyme; chlorophyll fluorescence; photosystem; <i>triticum aestivum</i> l.
• Online Access: https://www.mdpi.com/1422-0067/21/1/268

Wheat stripe rust (<i>Puccinia striiformis</i> f. sp. <i>tritici</i>, <i>Pst</i>) is the most destructive wheat disease and a major problem for the productivity of wheat in the world. To obtain a better understanding about different effects of redox homeostasis and photosystem (PS) to <i>Pst</i> infection in wheat, we investigated the differences in photosynthesis and the antioxidant defense system in wheat cultivar Chuanmai42 (CM42) in response to two Chinese <i>Pst</i> races known as CYR32 and V26. The results showed that V26-infected wheat accumulated a higher reactive oxygen species (ROS), cell death, and energy dissipation than CYR32-infected wheat when compared with the control. Furthermore, we found that the activities of three antioxidant enzymes (APX, GR, and GPX) and four resistance-related enzymes in CYR32-infected wheat were significantly higher than that in V26-infected wheat. In addition, quantitative RT-PCR indicated that the expression levels of two genes associated with resistant stripe rust in CYR32-infected wheat were clearly higher than that in V26-infected wheat. Compared with CYR32-infected wheat, lower photochemical efficiencies were observed in V26-infected wheat at the adult stage. Meanwhile, only a marked decline in D1 protein was observed in V26-infected wheat. We therefore deduced that wheat with stripe rust resistance could maintain high resistance and photosynthetic capacity by regulating the antioxidant system, disease-resistant related enzymes and genes, and the levels of PSII reaction center proteins.