In silicoStructure-Based Investigation of Key Residues of Insecticidal Activity of Sip1Aa Protein

文献类型： 外文期刊

第一作者： Wang, Jing

作者： Wang, Jing;Ding, Ming-Yue;Wang, Jian;Liu, Rong-Mei;Li, Hai-Tao;Gao, Ji-Guo;Wang, Jian;Li, Hai-Tao

作者机构：

关键词： Bacillus thuringiensis; Sip1Aa; site-directed mutation; structure analysis; Colaphellus bowringiBaly

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：5.64； 五年影响因子：6.32 ）

ISSN： 1664-302X

年卷期： 2020 年 11 卷

页码：

收录情况： SCI

摘要： Colaphellus bowringiBaly mainly damages cruciferous vegetables, leading to huge economic losses. The secretory insecticidal protein (Sip) ofBacillus thuringiensis(Bt) has high insecticidal activity againstC. bowringiBaly. The tertiary structure of Sip1Aa protein was analyzed by homologous modeling and other bioinformatics methods to predict the conserved domain of Sip1Aa protein. Acidic and basic amino acids in the conserved domain were selected, and alanine was used to replace these amino acids by site-directed mutation. The difference between the insecticidal activities of mutant protein and Sip1Aa protein was analyzed. The insecticidal activities of H99A, K109A, K128A, and E130A againstC. bowringiBaly were significantly increased, among which that of K128A was the most obviously changed, and the LC(50)value was decreased by about 10 times compared with that of Sip1Aa protein. The LC(50)value of mutant E130A was 0.286 mu g/mL, which was about six times less than that of Sip1Aa. K128 and E130 were both in the beta 9-beta 10 loop. The toxicity of D290A, H242A, and H303A toC. bowringiBaly was significantly reduced, and their LC(50)value increased by about six, eight, and three times compared with that of Sip1Aa protein, respectively. This study showed that acidic and basic amino acid residues played a certain role in the toxicity of Sip1Aa protein, and the loss of side chains in key residues had a significant impact on the insecticidal activity of the protein. This study provides the theoretical basis for revealing the relationship between the structure and function of Sip1Aa protein and also provides a new method for the subsequent study ofsipgene.

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