湖北农业科学 ›› 2022, Vol. 61 ›› Issue (24): 153-159.doi: 10.14088/j.cnki.issn0439-8114.2022.24.033

• 生物工程 • 上一篇    下一篇

草地贪夜蛾热休克蛋白Hsp70的生物信息学分析

刘芳1, 张志刚1, 方伟1, 王开梅1,2, 王月莹1   

  1. 1.湖北省农业科学院/湖北省生物农药工程研究中心/国家生物农药工程技术研究中心/农业农村部微生物农药创制重点实验室/湖北省农业科技创新中心生物农药分中心,武汉 430064;
    2.洪山实验室,武汉 430070
  • 收稿日期:2022-08-19 出版日期:2022-12-25 发布日期:2023-01-18
  • 通讯作者: 王月莹(1984-),女,湖北襄阳人,助理研究员,博士,主要从事微生物农药资源与新药创制研究,(电话)13517286850(电子信箱)yueying.wang@nberc.com。
  • 作者简介:刘芳(1978-),女,湖北天门人,助理研究员,主要从事微生物农药资源的保藏与挖掘、微生物农药发酵条件及工艺的优化研究,(电话)18086025680(电子信箱)liufang@nberc.com。
  • 基金资助:
    湖北省重点研发计划项目(2021BBA081); 湖北省农业科学院青年科学基金项目(2020NKYJJ18)

Bioinformatics analysis of heat-shock protein Hsp70 from Spodoptera frugiperda

LIU Fang1, ZHANG Zhi-gang1, FANG Wei1, WANG Kai-mei1,2, WANG Yue-ying1   

  1. 1. Hubei Biopesticide Engineering Research Center/National Biopesticide Engineering Technology Research Center/Key Laboratory of Microbial Pesticides, Ministry of Agriculture and Rural Affairs/Biopesticide Branch, Hubei Innovation Centre of Agricultural Science and Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China;
    2. Hubei Hongshan Laboratory, Wuhan 430070, China
  • Received:2022-08-19 Online:2022-12-25 Published:2023-01-18

摘要: 为研究草地贪夜蛾(Spodoptera frugiperda)热休克蛋白Hsp70的功能,对Hsp70的理化性质、亲水/疏水性、二级结构、三级结构、跨膜结构及同源性等进行了分析和预测。结果表明,Hsp70基因共编码 651个氨基酸,是稳定亲水蛋白,蛋白质二级结构主要为α-螺旋,其次为延伸链和无规则卷曲。Hsp70蛋白不具有信号肽及跨膜结构,与其他16种昆虫Hsp70蛋白的氨基酸序列进行对比,发现草地贪夜蛾的Hsp70蛋白与鳞翅目昆虫甜菜夜蛾(Spodoptera exigua)和斜纹夜蛾(Spodoptera litura)的亲缘关系较近。

关键词: 草地贪夜蛾(Spodoptera frugiperda), 热休克蛋白, 环境胁迫, 生物信息学

Abstract: To investigate the function of Hsp70, the physical and chemical properties, hydrophilicity/hydrophobicity, secondary structure, tertiary structure, transmembrane structure, and homology alignment of Hsp70 were predicted and analyzed. The results showed that Hsp70 gene encoded 651 amino acids which was a stable hydrophilic protein. The secondary structure of the protein mainly consisted of α-Helix, followed by extended chains and random coils. The Hsp70 protein had no signal peptide and transmembrane structure. Compared with the Hsp70 proteins of 16 other insects, it was found that the Hsp70 protein of Spodoptera frugiperda was closely related to the Lepidoptera Spodoptera exigua and Spodoptera litura.

Key words: Spodoptera frugiperda, heat-shock proteins, environmental stresses, bioinformatics

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