Journal of Integrative Agriculture ›› 2023, Vol. 22 ›› Issue (2): 514-525.DOI: 10.1016/j.jia.2022.08.015

• • 上一篇    下一篇

JIA-2022-0023丽蚜小蜂化学感受蛋白EforCSP3的特性及其在寄主定位中的潜在作用

  

  • 收稿日期:2022-01-10 接受日期:2022-05-11 出版日期:2023-02-20 发布日期:2022-05-11

Characterization of the chemosensory protein EforCSP3 and its potential involvement in host location by Encarsia formosa

WANG Ke, HE Yan-yan, ZHANG You-jun, GUO Zhao-jiang, XIE Wen, WU Qing-jun, WANG Shao-li   

  1. Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences, Beijing 100081, P.R.China

  • Received:2022-01-10 Accepted:2022-05-11 Online:2023-02-20 Published:2022-05-11
  • About author:WANG Ke, E-mail: Jackwangcaas@outlook.com; Correspondence WANG Shao-li, Tel: +86-10-82109518, E-mail: wangshaoli@caas.cn
  • Supported by:

    This research was supported by the National Natural Science Foundation of China (31772172), the earmarked fund for China Agriculture Research System (CARS-25) and the Beijing Key Laboratory for Pest Control and Sustainable Cultivation of Vegetables.  

摘要:

化学感受蛋白(chemosensory proteins,CSPs)在昆虫体内发挥多种功能。为了明确丽蚜小蜂化学感受蛋白EforCSP3是否在其寄主定位和寄主选择性方面发挥嗅觉识别作用,本研究从丽蚜小蜂中鉴定到化学感受蛋白EforCSP3,并对其进行了基因表达、配体结合和分子对接试验。结果表明,EforCSP3在丽蚜小蜂雌蜂头部高表达,成虫期该基因的相对表达量显著高于其他发育时期;荧光竞争结合试验发现EforCSP3与多种寄主植物挥发物之间具有较高的结合力,其中,除月桂烯和α-律草烯外,还有邻苯二甲酸二丁酯、1-辛烯、β-榄香烯和十三烷,EforCSP3的结合力最强,这些组分具有被开发为丽蚜小蜂引诱剂的潜力;进一步通过蛋白质结构建模和分子对接预测了可能参与挥发物结合的EforCSP3关键氨基酸残基。结合此前的研究,α-葎草烯和β-月桂烯已被证明可以吸引丽蚜小蜂,本研究亦发现二者EforCSP3有强的结合力。总之,EforCSP3可能参与丽蚜小蜂的化学信息识别接收过程。

Abstract:

Chemosensory proteins (CSPs) perform several functions in insects.  This study performed the gene expression, ligand-binding, and molecular docking assays on the EforCSP3 identified in the parasitoid wasp Encarsia formosa, to determine whether EforCSP3 functions in olfaction, especially in host location and host preference.  The results showed that EforCSP3 was highly expressed in the female head, and its relative expression was much higher in adults than in other developmental stages.  The fluorescence binding assays suggested that the EforCSP3 exhibited high binding affinities to a wide range of host-related volatiles, among which dibutyl phthalate, 1-octene, β-elemene, and tridecane had the strongest binding affinity with EforCSP3, besides α-humulene and β-myrcene, and should be assessed as potential attractants.  Protein structure modeling and molecular docking predicted the amino acid residues of EforCSP3 possibly involved in volatile binding.  α-Humulene and β-myrcene attracted Eformosa in a previous study and exhibited strong binding affinities with EforCSP3 in the current study.  In conclusion, EforCSP3 may be involved in semiochemical reception by Eformosa.

Key words: Encarsia formosa ,  chemosensory protein ,  expression profiles ,  fluorescence binding assay ,  molecular docking