Identification of an alkaline phosphatase as a putative Cry1Ac binding protein in Ostrinia furnacalis (Guenée)
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- 作者：Tingting Jina ; 459891263@qq.com" class="auth_mail" title="E-mail the corresponding author ; Xiaoli Duana ; zishanhuhappy@126.com" class="auth_mail" title="E-mail the corresponding author ; Alejandra Bravob ; bravo@ibt.unam.mx" class="auth_mail" title="E-mail the corresponding author ; Mario Soberó ; nb ; mario@ibt.unam.mx" class="auth_mail" title="E-mail the corresponding author ; Zhenying Wanga ; wangzy61@163.com" class="auth_mail" title="E-mail the corresponding author ; Kanglai Hea ; klhe@ippcaas.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：ACB ; Asian corn borer ; Bt ; Bacillus thuringiensis ; ACB-BtS ; Bt-susceptible strain of ACB ; ACB-AcR ; Bt-Cry1Ac-resistant strain of ACB ; BBMV ; brush border membrane vesicles ; GPI ; glycosyl-phosphatidyl-inositol ; ALP ; alkaline-phosphatase ; APN ; aminopeptidase-N ; OfALP ; O. furnacalis ALP ; CAD ; cadherin-like protein ; qPCR ; Quantitative real-time PCR ; GalNAc ; N-acetylgalactosamine
- 刊名：Pesticide Biochemistry and Physiology
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：131
- 期：Complete
- 页码：80-86
- 全文大小：575 K
文摘
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An alkaline phosphatase protein from Ostrinia furnacalis (OfALP) was cloned and characterized.
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OfALP binds Cry1Ac in midgut membranes from young instar larvae and the binding interaction is GalNAc dependent.
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A recombinant OfALP fragment derived from Escherichia coli binds Cry1Ac toxin.
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