Bacillus thuringiensis Cry1Aa toxin‐binding region of Bombyx mori aminopeptidase N

FEBS Letters

Nakanishi, Kazuko¹  Imamura, Morikazu²  Koizumi, Nobuo²  Sato, Ryoichi¹  Yaoi, Katsuro¹  Iwahana, Hidenori²  Kadotani, Tomoyuki² 

[1] Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-0012, Japan;Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Tokyo 183-0054, Japan

关键词: Aminopeptidase N;    δ-Endotoxin;    Bacillus thuringiensis;    Bombyx mori;   

DOI  :  10.1016/S0014-5793(99)01626-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Bacillus thuringiensis Cry1Aa toxin-binding region of Bombyx mori aminopeptidase N (APN) was analyzed, to better understand the molecular mechanism of susceptibility to the toxin and the development of resistance in insects. APN was digested with lysylendopeptidase and the ability of the resulting fragments to bind to Cry1Aa and 1Ac toxins was examined. The binding abilities of the two toxins to these fragments were different. The Cry1Aa toxin bound to the fragment containing 40-Asp to 313-Lys, suggesting that the Cry1Aa toxin-binding site is located in the region between 40-Asp and 313-Lys, while Cry1Ac toxin bound exclusively to mature APN. Next, recombinant APN of various lengths was expressed in Escherichia coli cells and its ability to bind to Cry1Aa toxin was examined. The results localized the Cry1Aa toxin binding to the region between 135-Ile and 198-Pro.

【 授权许可】

Unknown