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The Influence of Site-direct Mutation on the Toxicity of Bacillus Thringiensis Cry1Ba3 Against Plutella Xylostella

Author: LinChengXi
Tutor: LinYi
School: Huaqiao University
Course: Biochemical Engineering
Keywords: Cry1Ba3 Site-directed mutagenesis Biological activity test Diamondback moth
CLC: TQ458
Type: Master's thesis
Year: 2011
Downloads: 17
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Abstract


Bacillus thuringiensis (Bacillus thuringiensis, referred to as Bt) to date research and the most widely used class of microbial pesticides. The Bt insecticidal activity mainly from parasporal crystal protein in the growth process, also known as insecticidal crystal proteins of ICPs (Insecticidal Crystal Proteins ICPs). ICPs insecticidal activity between the amino acids and the structure of the relationship is the focus of current research. Cry1Ba3 by the laboratory to explore the high virulence against Plutella insecticidal crystal proteins. In order to find the insecticidal activity of important amino acids, this study by the following steps Cry1Ba3 analysis: Swiss-Model database, homology modeling three-dimensional structure of Cry1Ba3 initially identified Cry1Ba3 three main structures the location of the domain: Domain Ⅰ located ~~ 270 Domain Ⅱ located of 280 ~~ 480 Domain Ⅲ located 500 to 630. Using the the BioEdit software analysis Cry1Ba3 the hydrophobic region, found in the 60 ~ 80, 260 ~ 263, 397 ~ 404 three hydrophobic region. Finally, Cry1Ba3 with Cry1Aa1 Cry2Aa1 Cry3Aa1 well Cry4Ba1 multiple sequence alignment, which identified 40 mutation sites. The use of semi-overlapping primer PCR method for Cry1Ba3 directed mutagenesis, to obtain 40 mutants (Ms to M39.) And inducible expression in E. coli (Escherichia coli, E. coli), BL21. The mutant protein using leaf dipping diamondback moth and ape leaf beetle bioassay, experimental results show that: the mutants M6 (R171L), M10 (W282A), M19 (H485G) against Plutella activity was significantly decreased, which The activity of the mutant protein M6 (R171L) complete loss of activity of the mutant protein M10 (W282A) reduced by 49 times, 44 times lower activity of the mutant protein M19 (H485G). All the mutant and wild-type protein sequence was submitted to the P? The NPS @ database SOPMA two institutions predict le Bio-Informatique Lyonnais site. Was found through the analysis of the results, the activity did not significantly change the mutations on protein structure generally does not affect, the activity changes apparent mutations were generated on the local structure of the protein irreversible change. This study identified a critical amino acids, three Cry1Ba3 insecticidal activity the mechanism research methods and theoretical aspects of the reference; while future synthesis of new high virulence broad-spectrum insecticidal protein theory basis, in order to increase agricultural production and save research resources to make some contribution.

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