cDNA cloning and expression of Bacillus thuringiensis Cry1Aa toxin binding 120 kDa amninopeptidase N from Bombyx mori

被引：35

作者：

Yaoi, K

Nakanishi, K

Kadotani, T

Imamura, M

Koizumi, N

Iwahana, H

Sato, R ^{[1
]}

机构：

[1] Tokyo Univ Agr & Technol, Grad Sch Bioapplicat & Syst Engn, Tokyo 1840012, Japan

[2] Tokyo Univ Agr & Technol, Fac Agr, Dept Appl Biol Sci, Tokyo 1830054, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1999年 / 1444卷 / 01期

关键词：

D O I：

10.1016/S0167-4781(98)00250-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Bacillus thuringiensis Cry1Aa toxin binds to a 120 kDa putative receptor protein in the Bombyx mori midgut. Recently, this protein was purified and identified as glycosyl-phosphatidylinositol (GPI) anchored aminopeptidase N (APN). In this study, a full-length cDNA thought to encode this 120 kDa APN was isolated and sequenced. It has a 2958 bp ORF encoding 986 amino acids. In the deduced amino acid sequence, we identified GPI-anchor and zinc-metallopeptidase signals, which are the same as those of APNs of other insects that are reported to be putative Cry1 toxin receptors. The B. mori APN amino acid sequence also has a high similarity with those of the other APNs. Subsequently, the recombinant APN was expressed by Escherichia coli and its Cry1Aa toxin binding ability was analyzed. Ligand blotting showed that Cry1Aa toxin bound to the recombinant APN. (C) 1999 Elsevier Science B.V. All rights reserved.

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页码：131 / 137

页数：7

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