Effect of Mycotoxin Cytochalasin A on Photosystem II in Ageratina adenophora

• Published in: Plants (Basel) Vol. 11; no. 20; p. 2797
• Main Authors: Jiang, Mengyun, Yang, Qian, Wang, He, Luo, Zhi, Guo, Yanjing, Shi, Jiale, Wang, Xiaoxiong, Qiang, Sheng, Strasser, Reto Jörg, Chen, Shiguo
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 21.10.2022; MDPI
• Subjects: Ageratina adenophora; Binding sites; bioherbicide; Chlorophyll; chlorophyll a fluorescence; D1 protein; Diuron; Electron transfer; Evolution; Herbicides; Hydrogen bonding; Hydrogen bonds; Inactivation; Mode of action; Molecular docking; Molecular structure; Mycotoxins; natural product; Natural products; Photosynthesis; photosynthetic inhibitor; Photosystem II; Phytotoxicity; Plant resistance; Proteins; Reaction centers; Residues; Weeds
• ISSN: 2223-7747; 2223-7747
• DOI: 10.3390/plants11202797

Biological herbicides have received much attention due to their abundant resources, low development cost, unique targets and environmental friendliness. This study reveals some interesting effects of mycotoxin cytochalasin A (CA) on photosystem II (PSII). Our results suggested that CA causes leaf lesions on Ageratina adenophora due to its multiple effects on PSII. At a half-inhibitory concentration of 58.5 μΜ (I50, 58.5 μΜ), the rate of O2 evolution of PSII was significantly inhibited by CA. This indicates that CA possesses excellent phytotoxicity and exhibits potential herbicidal activity. Based on the increase in the J-step of the chlorophyll fluorescence rise OJIP curve and the analysis of some JIP-test parameters, similar to the classical herbicide diuron, CA interrupted PSII electron transfer beyond QA at the acceptor side, leading to damage to the PSII antenna structure and inactivation of reaction centers. Molecular docking model of CA and D1 protein of A. adenophora further suggests that CA directly targets the QB site of D1 protein. The potential hydrogen bonds are formed between CA and residues D1-His215, D1-Ala263 and D1-Ser264, respectively. The binding of CA to residue D1-Ala263 is novel. Thus, CA is a new natural PSII inhibitor. These results clarify the mode of action of CA in photosynthesis, providing valuable information and potential implications for the design of novel bioherbicides.