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Resistance mechanism of Fusarium fujikuroi to phenamacril in the field

Author:
Hou, Yi‐Ping, Qu, Xiang‐Pu, Mao, Xue‐Wei, Kuang, Jing, Duan, Ya‐Bing, Song, Xiu‐shi, Wang, Jian‐Xin, Chen, Chang‐Jun, Zhou, Ming‐Guo
Source:
Pest management science 2018 v.74 no.3 pp. 607-616
ISSN:
1526-498X
Subject:
Fusarium fujikuroi, amino acids, cross resistance, disease control, fungicides, hydrogen bonding, mycelium, pathogenicity, point mutation, rice, sporulation, China
Abstract:
BACKGROUND: Rice bakanae disease, mainly caused by Fusarium fujikuroi, is an important disease of rice. Phenamacril has been used to control the disease for a few years in China. In 2016, nine phenamacril‐resistant strains were found in the field in Zhejiang Province. The aim of the study was to clarify the mechanism of resistance of F. fujikuroi to phenamacril and the fitness of resistant strains. RESULTS: The nine F. fujikuroi strains examined were highly resistant to phenamacril. Eight of them had the point mutation TCA (Ser) → CCA (Pro) at codon 219 in the Myosin‐5 protein, while the other had the point mutation TCA (Ser) → TTA (Leu) at codon 219. Myosin‐5 replacement between resistant and sensitive strains confirmed that the point mutation in Myosin‐5 caused the resistance of F. fujikuroi to phenamacril. Docking of phenamacril into the modeled binding pocket of Myosin‐5 showed that the affinity between phenamacril and Myosin‐5 decreased and a hydrogen bond could not be formed between phenamacril and the amino acid at codon 219 after it changed to Pro or Leu. There was no cross‐resistance between phenamacril and other fungicides. The eight resistant strains containing the point mutation S219P had almost the same fitness as the sensitive strains, while the one resistant strain containing the point mutation S219 L showed decreased mycelial growth, sporulation and pathogenicity. CONCLUSION: In the field, the point mutation S219P or S219 L in Myosin‐5 conferred high resistance to phenamacril in F. fujikuroi. The point mutation S219P did not affect the fitness of F. fujikuroi, while the point mutation S219 L decreased its fitness. © 2017 Society of Chemical Industry
Agid:
5890615