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作 者:Meng-Yao Wang Xin-Yang Liu Li Shi Jia-Lu Liu Guang-Mao Shen Ping Zhang Wen-Cai Lu Lin He
机构地区:[1]Key Laboratory of Entomology and Pest Control Engineering,College of Plant Protection,Southwest University,Chongqing,China [2]Academy o f Agricultural Sciences,Southwest University,Chongqing,China
出 处:《Insect Science》2020年第2期276-291,共16页昆虫科学(英文版)
基 金:by Chongqing Research Program of Basic Research and Frontier Technology(No.cstc2017jcyjBX0061);the National Natural Science Foundation of China(31672085).
摘 要:Uridine diphosphate(UDP)-glycosyltransferases(UGTS)are widely distributed within living organisms and share roles in biotransformation of various lipophilic endo-and xenobiotics with activated UDP sugars.In this study,it was found that the activity of UGTs in abamectin-resistant(AbR)strain was significantly higher(2.3-fod)than that in susceptible strain(SS)of Tetramychus cinnabarinus.Further analysis showed that 5-nitrouracil,the inhibitor ofUGTs,could enhance the lethal effect of abamectin on mites.From the previous microarray results,we found an UGT gene(UGT201D3)overexpressed in AbR strain.Quantitative PCR analysis showed that UGT20ID3 was highly expressed and more inducible with abamectin exposure in the AbR strain.After silencing the tran-scription of UGT201D3,the activity of UGTs was decreased and the susceptibility to abamectin was increased in AbR strain whereas it was not in sS.Furthermore,UGT201D3 gene was then succefully expressed in Escherichia coli.The recombinant UGT20ID3 exhibited a-naphthol activity(2.810.43 nmol mg protein/min),and the enzyme activity could be inhibited by abamectin(inhibitory concentration at 50%:57.50±3.54 μmol/L).High-performance liquid chromatography analysis demonstrated that the recombinant UGT201D3 could efctively deplete abamectin(15.77%±3.72%)incubating with 150 ug protein for 6 h.These results provided direct evidence that UGT201D3 was involved in abamectin resistance in T cinnabarinus.
关 键 词:abamectin resistance prokaryotic expression RNA interference Tetrumychus cimnabarins UDP-glycosy ltransferases
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