Title: Expression and Antimicrobiotic Activity of aiiA Gene from Different Strains of Bacillus thuringiensis
Abstract:The enzyme encoded by aiiA gene was involved in the degradation of N-acyl-homoserine lactones (AHLs), decreasing the virulence of bacterial pathogens. After the aiiA genes from 6 different strains of ...The enzyme encoded by aiiA gene was involved in the degradation of N-acyl-homoserine lactones (AHLs), decreasing the virulence of bacterial pathogens. After the aiiA genes from 6 different strains of Bacillus thuringiensis were cloned, the aiiA genes from bryopsida (LLB15) and soil (LLS9) were analyzed. The deduced isoelectric point of AiiA-B15 was about 4.59 with a theoretical molecular weight of 27.97×103, while the deduced isoelectric point of AiiA-S9 was about 4.32 with a theoretical molecular weight of 28.14×103. They were both hydrophilic proteins. AiiA proteins were highly conserved with the homology of 90 % between AiiA-B15 and AiiA-S9. Phylogenetic analysis showed AiiA-B15 was closest to the AiiA from B. thuringiensis subsp. kyushuensis, while AiiA-S9 was closest to those of B. cereus. The aiiA-B15 genes from B. thuringiensis isolated from bryopsida were subcloned and inserted into the expression vector pGEX-4T-3.The recombinant plasmid pGEXaiiA-B15 was induced by IPTG. Large amounts of fusion protein were obtained by optimizing the expression conditions. The highest expression level of fusion protein was obtained by adding 0.6 mmol/L IPTG and inducing for 3 hours at 30 ℃. The fusion protein greatly alleviated the pathogenesis of Eriwinia carotovora causing soft rot for carota. Fig 13, Tab 4, Ref 23Read More
Publication Year: 2007
Publication Date: 2007-01-01
Language: en
Type: article
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