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
收藏
页码：57 / 63
页数：7
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