Details

Autor(en) / Beteiligte

• Yin, Mao-Zhu
• Li, Jian-Qiao
• Liu, Qiang
• Ma, Sai
• Hu, Zhuang-Zhuang
• Liu, Xing-Zhou
• Wang, Chao-Wei
• Yao, Wei-Chen
• Zhu, Xiu-Yun
• Wang, Yue-Ying
• Li, Jin-Bu
• Zhang, Ya-Nan

Titel

Binding properties of chemosensory protein 12 in Riptortus pedestris to aggregation pheromone (E)-2-hexenyl (Z)-3-hexenoate

Ist Teil von

• Pesticide biochemistry and physiology, 2023-08, Vol.194, p.105513-105513, Article 105513

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2023

Quelle

ScienceDirect

Beschreibungen/Notizen

• Riptortus pedestris (bean bug), a common soybean pest, has a highly developed olfactory system to find hosts for feeding and oviposition. Chemosensory proteins (CSPs) have been identified in many insect species; however, their functions in R. pedestris remain unknown. In this study, quantitative real time-polymerase chain reaction (qRT-PCR) revealed that the expression of RpedCSP12 in the adult antennae of R. pedestris increased with age. Moreover, a significant difference in the expression levels of RpedCSP12 was observed between male and female antennae at one and three days of age. We also investigated the binding ability of RpedCSP12 to different ligands using a prokaryotic expression system and fluorescence competitive binding assays. We found that RpedCSP12 only bound to one aggregation pheromone, (E)-2-hexenyl (Z)-3-hexenoate, and its binding decreased with increasing pH. Furthermore, homology modelling, molecular docking, and site-directed mutagenesis revealed that the Y27A, L74A, and L85A mutants lost their binding ability to (E)-2-hexenyl (Z)-3-hexenoate. Our findings highlight the olfactory roles of RpedCSP12, providing insights into the mechanism by which RpedCSPs bind to aggregation pheromones. Therefore, our study can be used as a theoretical basis for the population control of R. pedestris in the future. [Display omitted] •The expression of RpedCSP12 in the adult antennae increased with age.•The expression levels of RpedCSP12 increased consistently over time.•We acquired a high-quality recombinant RpedCSP12 protein.•RpedCSP12 had binding affinity to (E)-2-hexenyl (Z)-3-hexenoate.•Three residues participate in the interaction between RpedCSP12 and pheromone.