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The E420K mutation in myosin5 confers field resistance to phenamacril in Fusarium asiaticum

文献类型： 外文期刊

作者： Zhang, Ziyang 1 ; Song, Xinhao 1 ; Qiu, Hui 1 ; Guo, Yu 1 ; Xu, Chao 2 ; Zhang, Haibo 3 ; Cai, Yiqiang 1 ; Zhang, Jie 1 ; Zhu, Feng 4 ; Yang, Hongfu 2 ; Tian, Zihua 3 ; Zhang, Shuai 5 ; Zhou, Mingguo 1 ; Duan, Yabing 1 ;

作者机构： 1.Nanjing Agr Univ, Coll Plant Protect, State Key Lab Agr & Forestry Biosecur, Nanjing 210095, Peoples R China

2.Jiangsu Acad Agr Sci, Jiangsu Hilly Area Zhenjiang Inst Agr Sci, Jurong 212400, Peoples R China

3.Plant Protect & Quarantine Stn Jiangsu Prov, Nanjing 210036, Peoples R China

4.Jiangsu Prov Off Green Food, Nanjing 210036, Peoples R China

5.Natl Agrotech Extens & Serv Ctr, Beijing 100125, Peoples R China

关键词： Fusarium asiaticum; Phenamacril; Myosin5; Field resistance

期刊名称：PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：4.0； 五年影响因子：4.5 ）

ISSN： 0048-3575

年卷期： 2025 年 213 卷

页码：

收录情况： SCI

摘要： Fusarium head blight (FHB), primarily caused by the Fusarium graminearum species complex (FGSC), is a devastating fungal disease that threatens global wheat production and endangers worldwide food security. Phenamacril, a myosin5 inhibitor, is widely recognized as an effective fungicide against FGSC. Since 2007, phenamacril has been registered in China for the control of FHB. While the resistance mechanisms in laboratoryinduced phenamacril-resistant mutants of FGSC have been documented, the field resistance mechanisms remain poorly understood. In this study, we identified six F. asiaticum isolates with high resistance to phenamacril from a collection of 5163 FGSC isolates. Sequence alignment analysis revealed these resistant isolates harbor an E420K point mutation in myosin5. Site-directed mutagenesis experiments confirmed that the E420K mutation in myosin5 confers high resistance to phenamacril in F. asiaticum. No cross-resistance was observed between phenamacril and pyraclostrobin, pydiflumetofen, or tebuconazole. Additionally, the mycelial growth, spore production, and pathogenicity of phenamacril-resistant isolates were diminished, indicating a reduced fitness of these resistant isolates. Molecular docking results further indicated that the E420K mutation in FaMyosin5 decreases its binding affinity for phenamacril compared to the wild-type FaMyosin5. Collectively, this study provides the first evidence that E420K mutation in myosin5 confers field resistance to phenamacril in F. asiaticum. These findings provide critical insights for monitoring and managing phenamacril resistance in FGSC.

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