Expression and characterization of inhA gene from Bacillus thuringiensis 8010

被引:7
作者
Yu, Xiaomin
Huang, Tianpei
Huang, Zhipeng
Powell, Charles A.
Guan, Xiong [1 ]
机构
[1] Minist Educ, Fujian Agr & Forestry Univ, Key Lab Bbiopesticide & Chem Biol, Fujian 350002, Peoples R China
[2] Univ Florida, Indian River Res & Educ Ctr, Ft Pierce, FL 34945 USA
基金
中国国家自然科学基金; 高等学校博士学科点专项科研基金;
关键词
Bacillus thuringiensis; bioassay; expression; inhA gene; sequence analysis;
D O I
10.1007/s11274-007-9408-5
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
InhA, a zinc metalloprotease secreted by Bacillus thuringiensis, specifically hydrolyzes antibacterial peptides produced by insect hosts. In this study, the inhA gene was cloned from B. thuringiensis 8010 using a pair of degenerate primers and the deduced 796 amino acid sequence showed a high degree of similarity with other InhA proteins in the Bacillus cereus group. The deduced amino acid sequence contained the zinc-binding motif (HEXXH), which is characteristic of the zinc-metalloprotease family. Additionally, the inhA gene was expressed in Escherichia coli BL21 (DE3). The expressed InhA protein was shown to be toxic to the third larvae of Plutella xylostella, contrary to preliminary study concerning the effect of InhA on Bombyx mori. This study provided insights into the potential of InhA for the biological control of certain lepidopteran insects.
引用
收藏
页码:1621 / 1625
页数:5
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