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Toxicity and binding analyses of Bacillus thuringiensis toxin Vip3A in Cry1Ac-resistant and -susceptible strains of Helicoverpa armigera (Hubner)

文献类型： 外文期刊

作者： Zhang Qian 2 ; Chen Li-zhen 3 ; Lu Qiong 1 ; Zhang Yan 1 ; Liang Ge-mei 1 ;

作者机构： 1.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China

2.Hebei Acad Agr & Forestry Sci, Inst Cotton Res, Shijiazhuang 050051, Peoples R China

3.Huazhong Agr Univ, Coll Plant Sci & Technol, Wuhan 430070, Peoples R China

关键词： vegetative insecticidal proteins (Vip3Aa);Bacillus thuringiensis;Helicoverpa armigera;cross-resistance;binding affinity

期刊名称：JOURNAL OF INTEGRATIVE AGRICULTURE （ 影响因子：2.848； 五年影响因子：2.979 ）

ISSN： 2095-3119

年卷期： 2015 年 14 卷 2 期

页码：

收录情况： SCI

摘要： The Bacillus thuringiensis vegetative insecticidal protein, Vip3A, represents a new family of Bt toxin and is currently applied to commercial transgenic cotton. To determine whether the Cry1Ac-resistant Helicoverpa armigera is cross-resistant to Vip3Aa protein, insecticidal activities, proteolytic activations and binding properties of Vip3Aa toxin were investigated using Cry1Ac-susceptible (96S) and Cry1Ac-resistant H. armigera strain (Cry1Ac-R). The toxicity of Vip3Aa in Cry1Ac-R slightly reduced compared with 96S, the resistance ratio was only 1.7-fold. The digestion rate of full-length Vip3Aa by gut juice extracts from 96S was little faster than that from Cry1Ac-R. Surface plasmon resonance (SPR) showed there was no significant difference between the binding affinity of Vip3Aa and BBMVs between 96S and Cry1Ac-R strains, and there was no significant competitive binding between Vip3Aa and Cry1Ac in susceptible or resistant strains. So there had little cross-resistance between Vip3Aa and Cry1Ac,Vip3A+Cry proteins maybe the suitable pyramid strategy to control H. armigera in China in the future.

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