Characterization of Bacillus thuringiensis Cry toxin binding novel GPI anchored aminopeptidase from fat body of the moth Spodoptera litura

被引:16
|
作者
Budatha, Madhusudhan [1 ]
Meur, Gargi [1 ]
Kirti, P. B. [1 ]
Gupta, Aparna Dutta [1 ]
机构
[1] Univ Hyderabad, Sch Life Sci, Hyderabad 500046, Andhra Pradesh, India
关键词
aminopeptidase; Bacillus thuringiensis; cry toxin; fat body; GPI anchor; spodoptera litura;
D O I
10.1007/s10529-007-9453-z
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Aminopeptidase N (APN) isoforms were identified as candidate receptors for Bacillus thuringiensis Cry toxins from the midgut of several insect species. In this study a partial cDNA encoding aminopeptidase (slfbAPN) was cloned from fat body of the moth Spodoptera litura. In the deduced amino acid sequence the characteristic metallopeptidase sequences, HEXXHX18E and GAMENWG were conserved but the sequence showed only 33-39% identity to other insect APNs, which were also reported to be Cry toxin receptors. The presence of a putative GPI anchor signal sequence at the C-terminus indicated that it is a membrane-anchored protein. The slfbAPN expression was restricted to the fat body as suggested by northern blot analysis of different tissues. Biochemical analyses including immunoblotting, ligand blotting and lectin blotting, demonstrated that slfbAPN is a membrane-anchored glycoprotein in the fat body and it binds to Cry toxins.
引用
收藏
页码:1651 / 1657
页数:7
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