Bacillus thuringiensis insecticidal Cry1Aa toxin binds to a highly conserved region of aminopeptidase N in the host insect leading to its evolutionary success

被引：21

作者：

Nakanishi, K

Yaoi, K

Shimada, N

Kadotani, T

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

[3] Ibaraki Agr Ctr, Inst Plant Biotechnol, Nishi Ibaraki 3190292, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1999年 / 1432卷 / 01期

关键词：

delta-endotoxin; aminopeptidase N; receptor; (Plutella xylostella); (Bacillus thuringiensis);

D O I：

10.1016/S0167-4838(99)00086-2

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 insecticidal protein, Cry1Aa toxin, binds to a specific receptor in insect midguts and has insecticidal activity. Therefore, the structure of the receptor molecule is probably a key factor in determining the binding affinity of the toxin and insect susceptibility. The cDNA fragment (PX frg1) encoding the Cry1Aa toxin-binding region of an aminopeptidase N (APN) or an APN family protein from diamondback moth, Plutella xylostella midgut was cloned and sequenced. A comparison between the deduced amino acid sequence of PXfrg1 and other insect APN sequences shows that Cry1Aa toxin binds to a highly conserved region of APN family protein. In this paper, we propose a model to explain the mechanism that causes B. thuringiensis evolutionary success and differing insect susceptibility to Cry1Aa toxin. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：57 / 63

页数：7

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