Journal of Integrative Agriculture ›› 2015, Vol. 14 ›› Issue (2): 347-354.DOI: 10.1016/S2095-3119(14)60770-X

• 论文 • 上一篇    下一篇

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

 ZHANG Qian, CHEN Li-zhen, LU Qiong, ZHANG Yan, LIANG Ge-mei   

  1. 1、State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of
    Agricultural Sciences, 100193 Beijing, P.R.China
    2、Institute of Cotton Research, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, P.R.China
    3、College of Plant Science and Technology, Huazhong Agricultural University, 430070 Wuhan, P.R.China
  • 收稿日期:2013-12-04 出版日期:2015-02-01 发布日期:2015-02-11
  • 通讯作者: LIANG Ge-mei, Tel: +86-10-62815929,E-mail: gmliang@ippcaas.cn
  • 作者简介:* These authors contributed equally to this study.
  • 基金资助:

    This research was supported by the Key Project for Breeding Genetically Modified Organisms, China (2014ZX08011-002) and the National Natural Science Foundation of China (30971921, 31321004).

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

 ZHANG Qian, CHEN Li-zhen, LU Qiong, ZHANG Yan, LIANG Ge-mei   

  1. 1、State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of
    Agricultural Sciences, 100193 Beijing, P.R.China
    2、Institute of Cotton Research, Hebei Academy of Agriculture and Forestry Sciences, Shijiazhuang 050051, P.R.China
    3、College of Plant Science and Technology, Huazhong Agricultural University, 430070 Wuhan, P.R.China
  • Received:2013-12-04 Online:2015-02-01 Published:2015-02-11
  • Contact: LIANG Ge-mei, Tel: +86-10-62815929,E-mail: gmliang@ippcaas.cn
  • About author:* These authors contributed equally to this study.
  • Supported by:

    This research was supported by the Key Project for Breeding Genetically Modified Organisms, China (2014ZX08011-002) and the National Natural Science Foundation of China (30971921, 31321004).

PDF

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.

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

Abstract: 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.

Key words: vegetative insecticidal proteins (Vip3Aa) , Bacillus thuringiensis , Helicoverpa armigera , cross-resistance , binding affinity