文献类型：期刊文献

中文题名：马尾松毛虫两个OBPs的表达分析及与其寄主挥发物的分子对接

英文题名：Expression analysis of two odorant binding proteins from Dendrolimus punctatus and molecular docking with the host volatiles

作者：谢明慧[1,2] 陈静[2] 王正[2] 李承锦[2] 武承旭[1] 张苏芳[2]

第一作者：谢明慧

机构：[1]贵州大学林学院,贵州贵阳550025;[2]中国林业科学研究院森林生态环境与自然保护研究所,国家林业和草原局森林保护学重点实验室,北京100091

年份：2025

卷号：44

期号：5

起止页码：1-10

中文期刊名：中国森林病虫

外文期刊名：Forest Pest and Disease

收录：;北大核心:【北大核心2023】；

基金：国家自然科学基金面上项目“马尾松毛虫适应寄主萜烯类防御物质的分子机制”(32371895);中国林业科学研究院基本科研业务费专项资金“重要林业害虫RNA干扰效率限速机制研究”(CAFYBB2020QC001)。

语种：中文

中文关键词：马尾松毛虫;气味结合蛋白;表达分析;蛋白质建模;分子对接

外文关键词：Dendrolimus punctatus;odorant binding protein;expression analysis;protein modeling;molecular docking

分类号：S763.42

摘要：为明确马尾松毛虫Dendrolimus punctatus气味结合蛋白(odorant binding proteins,OBPs)在寄主挥发物识别中的功能,利用PCR和RT-qPCR技术,克隆在马尾松毛虫体内2个表达量较高的OBPs基因DpunOBP6和DpunOBP27的cDNA,测定其表达特性;利用系统发育分析和序列分析研究DpunOBP6、DpunOBP27的进化关系和序列结构特征;通过蛋白建模和分子对接模拟预测蛋白DpunOBP6和DpunOBP27与其寄主挥发物的结合效果。结果表明:DpunOBP6和DpunOBP27基因在马尾松毛虫卵和蛹中相对表达量均较低,在成虫触角中相对表达量最高;蛋白建模得到DpunOBPs的蛋白质三维结构模型,分子对接技术得到蛋白DpunOBP6和DpunOBP27与马尾松Pinus massoniana主要挥发物结合效果良好。在马尾松毛虫27种寄主挥发物中,DpunOBP6与(+)-苜蓿烯、β-石竹烯、依兰烯、反式石竹烯结合能最小,DpunOBP27与β-金合欢烯结合能最小。2个结合蛋白与α-松油醇作用均产生氢键,DpunOBP27与异松樟酮结合产生氢键。研究结果为探明基因DpunOBP6和DpunOBP27的功能及基于反向化学生态学筛选马尾松毛虫行为调控剂奠定基础。
To elucidate the role of odorant binding proteins(OBPs)of Dendrolimus punctatus in host volatiles recognition,cDNA of two OBPs genes,DpunOBP6 and DpunOBP27,which were highly expressed in D.punctatus,were cloned using PCR,and the expression characteristics were determined by RT-qPCR;the evolutionary relationship and sequence structural characteristics were determined by using phylogenetic and sequence analyses,respectively;binding effects of the two proteins to the host volatiles were predicted by protein modeling and molecular docking simulations.The results demonstrated that relative expression levels of both DpunOBP6 and DpunOBP27 were low in eggs and pupae of D.punctatus,but reaching the highest level in antennae of adults.The three-dimensional structural model of DpunOBPs was obtained through protein modeling,and DpunOBP6 and DpunOBP27 had good binding effects with main volatile compounds of Pinus massoniana by molecular docking technology.Among 27 tested volatile compounds from P.massoniana,DpunOBP6 exhibited the lowest binding energy with four compounds:(+)-sativene,β-caryophyllene,ylangene and trans-caryophyllene.DpunOBP27 showed the lowest binding energy withβ-farnesene.Molecular interaction analysis revealed that both DpunOBP6 and DpunOBP27 protein formed hydrogen bonding interactions withα-terpineol,and DpunOBP27 specifically formed hydrogen bonds with isopino camphone.These findings provided a foundation for elucidating functions of gene DpunOBP6 and DpunOBP27,and for screening behavior-regulating agents of D.punctatus based on reverse chemical ecology.