中国农业科学院机构知识库

The Y123H substitution perturbs FvCYP51B function and confers prochloraz resistance in laboratory mutants of Fusarium verticillioides

文献类型：外文期刊

作者： Fan, J. ² ; Chen, F. ¹ ; Diao, Y. ¹ ; Cools, H. J. ⁴ ; Kelly, S. L. ⁵ ; Liu, X. ¹ ;

作者机构： 1.China Agr Univ, Dept Plant Pathol, Beijing 100193, Peoples R China

2.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China

3.Fujian Agr & Forestry Univ, Inst Plant Virol, Key Lab Plant Virol Fujian Prov, Fuzhou 350002, Peoples R China

4.Rothamsted Res, Dept Biol Chem & Crop Protect, Harpenden AL5 2JQ, Herts, England

5.Swansea Univ, Inst Life Sci, Swansea SA2 8PP, W Glam, Wales

6.Swansea Univ, Coll Med, Swansea SA2 8PP, W Glam, Wales

关键词： azole fungicide;CYP51;resistance mechanism;site mutation;yeast expression

期刊名称：PLANT PATHOLOGY （影响因子：2.59；五年影响因子：2.924 ）

ISSN： 0032-0862

年卷期： 2014 年 63 卷 4 期

页码：

收录情况： SCI

摘要： Fusarium verticillioides reduces corn yield and contaminates infected kernels with the toxin fumonisin, which is harmful to humans and animals. Previous research has demonstrated that F. verticillioides can be controlled by the azole fungicide prochloraz. Currently, prochloraz is used as a foliar spray to control maize disease in China, which will increase the risk of resistance. Although F. verticillioides resistance to prochloraz has not been reported in the field, possible resistance risk and mechanisms resulting in prochloraz resistance were explored in the laboratory. Four prochloraz-resistant strains of F. verticillioides were generated by successive selection on fungicide-amended media. The mycelial growth rates of the mutants were inversely related to the level of resistance. All four mutants were cross-resistant to the triazole fungicides triadimefon, tebuconazole and difenoconazole, but not to the multisite fungicide chlorothalonil or to the MAP/histidine-kinase inhibitor fungicide fludioxonil. Based on the Y123H mutation in FvCYP51B, the four resistant mutants were subdivided into two genotypes: PCZ-R1 mutants with wildtype FvCYP51B and PCZ-R2 mutants with substitution Y123H in FvCYP51B. Wildtype FvCYP51B complemented the function of native ScCYP51 in Saccharomyces cerevisiae YUG37::erg11, whereas Y123H-mutated FvCYP51B did not. For the PCZ-R1 mutants, induced expression of FvCYP51A increased resistance to prochloraz. For the PCZ-R2 mutants, disruption of FvCYP51B function by the Y123H substitution caused constitutive up-regulation of FvCYP51A expression and thus resistance to prochloraz.

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