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A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resistance to Cry1Ab

文献类型： 外文期刊

作者： Xu, Lina 1 ; Ferry, Natalie 2 ; Wang, Zhenying 1 ; Zhang, Jie 1 ; Edwards, Martin G. 2 ; Gatehouse, Angharad M. R.; 1 ;

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

2.Newcastle Univ, Newcastle Inst Res Environm & Sustainabil, Sch Biol, Newcastle Upon Tyne NE1 7RU, Tyne & Wear, England

3.Anhui Acad Agr Sci, Inst Plant Protect & Agroprod Safety, Hefei

关键词： Bacillus thuringiensis;Ostrinia furnacalis (Gueneve);Proteomics;Resistance;V-type proton ATPase catalytic;subunit A;Heat shock 70 kDa proteins

期刊名称：TRANSGENIC RESEARCH （ 影响因子：2.788； 五年影响因子：2.377 ）

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收录情况： SCI

摘要： A Cry1Ab-resistant population of Asian corn borer (ACB-AbR) exhibiting approximately 100 times greater resistance to activated Cry1Ab than a susceptible population (Ostrinia furnacalis; ACB-BtS), was previously shown to exhibit high levels of cross-resistance to Cry1Ah (131-fold), but no cross-resistance to Cry1Ie. It was suggested that the proposed mechanism of resistance was due to the alteration of specific receptors for Cry toxins in the midgut brush border membrane. In the present study a proteomic-based approach was used to identify proteins from brush border membrane vesicles (isolated from both resistant and susceptible Ostrinia furnacalis larvae) interacting with biotinylated Cry1Ab, Cry1Ah, and Cry1Ie. 2D-Electrophoresis in combination with ligand blots were employed and putative protein identities obtained using MALDI-ToF/ToF mass spectrometry. The V-type proton ATPase catalytic subunit A and heat shock 70 kDa proteins were identified as interacting with the Cry toxins tested in the ACB-AbR and ACB-BtS larvae. The biotinylated Cry toxins showed markedly stronger interactions with proteins in the resistant compared to the susceptible larvae, suggesting an up-regulation of the V-type proton ATPase catalytic subunit A and heat shock 70 kDa proteins in the resistant (ACB-AbR) larvae. Interestingly, Cry1Ie interactions with the V-type proton ATPase catalytic subunit A in the ACB-BtS larvae appeared to be absent.

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