A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resista
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ORIGINAL PAPER
A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resistance to Cry1Ab Lina Xu • Natalie Ferry • Zhenying Wang Jie Zhang • Martin G. Edwards • Angharad M. R. Gatehouse • Kanglai He
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Received: 9 May 2013 / Accepted: 28 May 2013 Ó Springer Science+Business Media Dordrecht 2013
Abstract 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 crossresistance 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 proteomicbased approach was used to identify proteins from brush border membrane vesicles (isolated from both resistant and susceptible Ostrinia furnacalis larvae)
L. Xu Z. Wang J. Zhang K. He (&) The State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 West Yuanmingyuan Road, Beijing 100193, People’s Republic of China e-mail: [email protected] L. Xu N. Ferry M. G. Edwards A. M. R. Gatehouse (&) Newcastle Institute for Research on Environment and Sustainability, School of Biology, Newcastle University, Newcastle upon Tyne NE1 7RU, UK e-mail: [email protected]; [email protected] L. Xu Institute of Plant Protection and Agro-Products Safety, Anhui Academy of Agricultural Sciences, No. 40 South Nongke Road, Hefei 230031, People’s Republic of China
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 ACBBtS larvae. The biotinylated Cry toxins showed markedly stronger interactions with proteins in the resistant compared to the susceptible larvae, suggesting an upregulation 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. Keywords Bacillus thuringiensis Ostrinia furnacalis (Guene´e) Proteomics Resistance V-type proton ATPase catalytic subunit A Heat shock 70 kDa proteins
Introduction Transgenic maize expressing the Cry1Ab protein from Bacillus thuringiensis (Bt) Berliner has been continuously planted in the USA since 1996 and has provided successful control of the European corn borer Ostrinia nubilalis (Hu¨bner) and other lepidopteran herbivores on maize (Archer et al. 2001; Shelton
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Transgenic Res
et al. 2002; Hari et al. 2008). Howeve
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