A new point mutation in β 2 -tubulin confers resistance to carbendazim in Fusarium asiaticum

Resistance to benzimidazole fungicides in many phytopathogenic fungi is caused by specific point mutations in the β-tubulin gene (β-tubulin). However, the mutated locus and genotype of β-tubulin differ among phytopathogenic fungi. To validate the point mutation in Fusarium asiaticum β -tubulin that...

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Bibliographic Details
Published in:Pesticide biochemistry and physiology 2018-02, Vol.145, p.15
Main Authors: Yang, Ying, Li, Mei-Xia, Duan, Ya-Bing, Li, Tao, Shi, Yi-Yuan, Zhao, Dong-Lei, Zhou, Ze-Hua, Xin, Wen-Jing, Wu, Jian, Pan, Xia-Yan, Li, Yan-Jun, Zhu, Yuan-Ye, Zhou, Ming-Guo
Format: Article
Language:English
Subjects:
Benzimidazoles - pharmacology
Binding Sites
Carbamates - pharmacology
Drug Resistance, Fungal - genetics
Fungicides, Industrial - pharmacology
Fusarium - drug effects
Fusarium - genetics
Genes, Plant
Microbial Sensitivity Tests
Molecular Docking Simulation
Mutagenesis, Site-Directed
Point Mutation
Reverse Transcriptase Polymerase Chain Reaction
Tubulin - genetics
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Summary:Resistance to benzimidazole fungicides in many phytopathogenic fungi is caused by specific point mutations in the β-tubulin gene (β-tubulin). However, the mutated locus and genotype of β-tubulin differ among phytopathogenic fungi. To validate the point mutation in Fusarium asiaticum β -tubulin that confers resistance to carbendazim and to analyze the molecular interaction between carbendazim and F. asiaticum β -tubulin. In this study, a new point mutation (GAG→GCG, E198A) at codon 198 of β -tubulin in a wild-type F. asiaticum strain was constructed by site-directed mutagenesis followed by a split marker strategy. The site-directed mutants were verified and exhibited a high level of resistance to carbendazim. In the absence of fungicide treatment, the biological characteristics did not differ between the site-directed mutants and the wild-type strain. Molecular docking between carbendazim and β -tubulin was carried out using the Surflex-Dock program in Sybyl X-2.0 version and the results indicated that the E198A mutation altered the configuration of β -tubulin, resulting in the change of the bonding sites and docking scores. We concluded that the point mutation of F. asiaticum β -tubulin conferring carbendazim resistance may not always be the bonding site for carbendazim.
ISSN:1095-9939
DOI:10.1016/j.pestbp.2017.12.006