| Title: | "Binding affinity characterization of an antennae-enriched chemosensory protein from the white-backed planthopper, Sogatella furcifera (Horvath), with host plant volatiles" |
| Author(s): | Chen GL; Pan YF; Ma YF; Wang J; He M; He P; |
| Address: | "State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, People's Republic of China. State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, People's Republic of China. Electronic address: hmher@126.com. State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, People's Republic of China. Electronic address: phe1@gzu.edu.cn" |
| DOI: | 10.1016/j.pestbp.2018.09.006 |
| ISSN/ISBN: | 1095-9939 (Electronic) 0048-3575 (Linking) |
| Abstract: | "The white-backed planthopper (WBPH) Sogatella furcifera is a notorious rice pest in Asia. Olfaction is crucial for the WBPH to seek and locate rice plants. However, its mechanism is still not fully understood. Chemosensory proteins (CSPs) are some of the important olfactory-related proteins. In this study, we first used a bacterial system to successfully express the recombinant, antennae-enriched protein SfurCSP5. Further, competitive fluorescence binding assays with 86 candidate ligands, including some known rice plant volatiles, showed that SfurCSP5 has high affinities for 2-tridecanone, 2-pentadecanone, and beta-ionone, which are known to be present in volatile mixtures that can attract rice planthoppers, and produced Ki values of 4.89, 4.09, and 1.39?ª+mumol/L, respectively. Additionally, homology modeling of the protein structure of SfurCSP5 showed that it possesses five alpha-helixes (alpha-1, alpha-2, alpha-3, alpha-4, and alpha-5), which is a non-typical feature of the insect CSPs. Finally, ligand docking results revealed that Leu-44, Ile-64, Phe-90, Trp-98, and Phe-101 are five hydrophobic residues that interact with all of the ligands, indicating their key involvement in the binding of SfurCSP5. Our study lays the foundation for an understanding of the olfaction mechanism of rice planthoppers" |
| Keywords: | "Animals Arthropod Antennae/physiology Hemiptera/*physiology Insect Proteins/chemistry/*physiology Ligands Models, Molecular Olfactory Perception Oryza/metabolism Phytochemicals/*metabolism Protein Binding Protein Conformation Volatile Organic Compounds/*m;" |
| Notes: | "MedlineChen, Guang-Lei Pan, Yu-Feng Ma, Yun-Feng Wang, Jun He, Ming He, Peng eng 2018/12/01 Pestic Biochem Physiol. 2018 Nov; 152:1-7. doi: 10.1016/j.pestbp.2018.09.006. Epub 2018 Sep 28" |
