Aminopeptidase N isoforms from the midgut of Bombyx mori and Plutella xylostella – their classification and the factors that determine their binding specificity to Bacillus thuringiensis Cry1A toxin

FEBS Letters

Nakanishi, Kazuko²  Atsumi, Shogo²  Miura, Nami²  Sato, Ryoichi²  Yaoi, Katsuro¹  Hara, Hirotaka²  Nagino, Yasushi²  Kitami, Madoka² 

[1] Research Institute of Biological Resources, National Institute of Advanced Industrial Science and Technology (AIST), AIST Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan;Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

关键词: Aminopeptidase N;    Cry1A toxin;    Receptor;    Bombyx mori;    Plutella xylostella;    Bacillus thuringiensis;   

DOI  :  10.1016/S0014-5793(02)02708-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Novel aminopeptidase N (APN) isoform cDNAs, BmAPN3 and PxAPN3, from the midguts of Bombyx mori and Plutella xylostella, respectively, were cloned, and a total of eight APN isoforms cloned from B. mori and P. xylostella were classified into four classes. Bacillus thuringiensis Cry1Aa and Cry1Ab toxins were found to bind to specific APN isoforms from the midguts of B. mori and P. xylostella, and binding occurred with fragments that corresponded to the BmAPN1 Cry1Aa toxin-binding region of each APN isoform. The results suggest that APN isoforms have a common toxin-binding region, and that the apparent specificity of Cry1Aa toxin binding to each intact APN isoform seen in SDS–PAGE is determined by factors such as expression level in conjunction with differences in binding affinity.

【 授权许可】

Unknown