
咖啡豹蠹蛾普通气味结合蛋白ZcofGOBP1和ZcofGOBP2同源建模及其与杜仲挥发物分子对接
Homology modelling of general odorant binding proteins (ZcofGOBP1 and ZcofGOBP 2) in Zeuzera coffeae and their molecular docking with volatiles of Eucommia ulmoides
黄星瑞1, 2** 邹 洁1, 2 杨 洁1 文 玺1 黄兴龙1, 2***
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DOI:10.7679/j.issn.2095-1353.2024.118
作者单位:1. 吉首大学生物资源与环境科学学院, 吉首 416000; 2. 吉首大学, 杜仲综合利用技术国家地方联合工程实验室,吉首 416000
中文关键词:咖啡豹蠹蛾;分子对接;普通气味结合蛋白;杜仲;挥发物
英文关键词:Zeuzera coffeae; molecular docking; general odorant binding protein; Eucommia ulmoides; volatile
中文摘要:
【目的】 为揭示钻蛀性害虫咖啡豹蠹蛾Zeuzera coffeae选择杜仲作为寄主的嗅觉识别机制。【方法】 借助咖啡豹蠹蛾转录组数据开展普通气味结合蛋白(General odorant
binding proteins, GOBPs)基因鉴定,然后通过同源建模和分子对接预测了这些蛋白与杜仲挥发物的结合特性。【结果】 鉴定得到2个普通气味结合蛋白基因(ZcofGOBP1和ZcofGOBP2),这2个基因编码的蛋白为水溶性蛋白,包含6个α螺旋和6个保守的半胱氨酸残基。同源建模发现ZcofGOBP1和ZcofGOBP2的保守半胱氨酸残基参与了3个二硫键的形成,这些二硫键将α-螺旋约束呈特定的立体结构,α-螺旋围绕的空间形成了一个开口位于蛋白表面的配体结合空腔。分子对接发现,ZcofGOBP1与植醇、11,14,17-三烯酸甲酯等5种杜仲挥发物结合能小于﹣7 kJ/mol,ZcofGOBP2与软脂酸乙酯和大马烯酮等5种杜仲挥发物结合能小于﹣7 kJ/mol;氢键、共价键、范德华力在这两个蛋白与配体的相互作用中发挥了重要作用。【结论】 咖啡豹蠹蛾ZcofGOBP1和ZcofGOBP2是具有配体结合空腔的可溶性蛋白,可能通过结合和转运寄主挥发物分子参与该虫对杜仲的嗅觉识别。
英文摘要:
[Aim] To elucidate the olfactory mechanisms of the wood-boring
pest Zeuzera coffeae selecting Eucommia ulmoides as host plant. [Methods] General odorant binding
proteins (GOBPs) in Z. coffeae were identified by transcriptome data
analysis. Homology modelling and molecular docking were performed to predict
the binding properties of these proteins with volatile compounds from E. ulmoides. [Results] Two GOBP genes (ZcofGOBP1 and ZcofGOBP2) were identified in Z. coffeae. The proteins
encoded by these genes were soluble proteins with six α-helixes and six
conserved cysteine residues. Homology modelling indicated that the conserved
cysteine residues form three disulfide bonds and the α-helixes were fixed by
disulfide bonds to form a ligand-binding pocket with a mouth on the protein
surface. Molecular docking revealed prominent binding abilities (Free energy
lower than -7 kJ/mol) of ZcofGOBPs with several E. ulmoides volatile
compounds. For example, ZcofGOBP1 with phytol and methyl
cis-11,14,17-eicosatrienoate, and ZcofGOBP2 with ethyl palmitate and
damascenone. The interaction of ZcofGOBPs with ligands was strongly influenced
by hydrogen bonds, covalent bonds, and van der Waals forces. [Conclusion] ZcofGOBP1 and ZcofGOBP2
are soluble proteins with ligand binding pockets and may be involved in the
perception of E. ulmoides by binding and transporting the host
volatiles.