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Stability is essential for insecticidal activity of Vip3Aa toxin against Spodoptera exigua

文献类型： 外文期刊

作者： Fu, Bai-Wen 2 ; Xu, Lian 1 ; Zheng, Mei-Xia 1 ; Chen, Qing-Xi 2 ; Shi, Yan 2 ; Zhu, Yu-Jing 1 ;

作者机构： 1.Fujian Acad Agr Sci, Agr Bioresources Res Inst, Fuzhou 350003, Peoples R China

2.Xiamen Univ, Sch Life Sci, Xiamen 361005, Peoples R China

关键词： Vip3A; Proteolysis; Molecular dynamics simulation; Insecticidal activity

期刊名称：AMB EXPRESS （ 影响因子：4.126； 五年影响因子：4.245 ）

ISSN： 2191-0855

年卷期： 2022 年 12 卷 1 期

页码：

收录情况： SCI

摘要： Vegetative insecticidal proteins 3A (Vip3A) were important insecticidal proteins for control of lepidopteran pests. Previous study demonstrated that Vip3Aa and Vip3Ad showed significant difference in insecticidal activities against Spodoptera exigua, while the molecular mechanism remained ambiguous. Here we demonstrated that the difference in insecticidal activities between Vip3Aa and Vip3Ad might be caused by the difference in stability of Vip3Aa and Vip3Ad in S. exigua midgut protease. Vip3Aa was quite stable while Vip3Ad could be further degraded. Molecular dynamics simulation revealed that Vip3Aa was more stable than Vip3Ad, with smaller RMSD and RMSF value. Amino acid sequence alignment indicated that three were three extra prolines (P591, P605 and P779) located on Vip3Aa. We further identified that residue P591 played a crucial role on stability and insecticidal activity of Vip3Aa. Taken together, our study demonstrated that the stability was essential for the insecticidal activity of Vip3A toxins, which might provide new insight into the action mode of Vip3A toxins and contribute to the design Vip3A variants with improved stability and insecticidal activity.

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