| Title: | A Highly Expressed Antennae Odorant-Binding Protein Involved in Recognition of Herbivore-Induced Plant Volatiles in Dastarcus helophoroides |
| Author(s): | Yi SC; Wu YH; Yang RN; Li DZ; Abdelnabby H; Wang MQ; |
| Address: | "Hubei Insect Resources Utilization and Sustainable Pest Management Key Laboratory, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, China. Key Laboratory of Forest Protection of National Forestry and Grassland Administration, Ecology and Nature Conservation Institute, Chinese Academy of Forestry, Beijing 100091, China. Department of Plant Protection, Faculty of Agriculture, Benha University, Banha 13736, Qalyubia, Egypt" |
| ISSN/ISBN: | 1422-0067 (Electronic) 1422-0067 (Linking) |
| Abstract: | "Natural enemies such as parasitoids and parasites depend on sensitive olfactory to search for their specific hosts. Herbivore-induced plant volatiles (HIPVs) are vital components in providing host information for many natural enemies of herbivores. However, the olfactory-related proteins involved in the recognition of HIPVs are rarely reported. In this study, we established an exhaustive tissue and developmental expression profile of odorant-binding proteins (OBPs) from Dastarcus helophoroides, an essential natural enemy in the forestry ecosystem. Twenty DhelOBPs displayed various expression patterns in different organs and adult physiological states, suggesting a potential involvement in olfactory perception. In silico AlphaFold2-based modeling and molecular docking showed similar binding energies between six DhelOBPs (DhelOBP4, 5, 6, 14, 18, and 20) and HIPVs from Pinus massoniana. While in vitro fluorescence competitive binding assays showed only recombinant DhelOBP4, the most highly expressed in the antennae of emerging adults could bind to HIPVs with high binding affinities. RNAi-mediated behavioral assays indicated that DhelOBP4 was an essential functional protein for D. helophoroides adults recognizing two behaviorally attractive substances: p-cymene and gamma-terpinene. Further binding conformation analyses revealed that Phe 54, Val 56, and Phe 71 might be the key binding sites for DhelOBP4 interacting with HIPVs. In conclusion, our results provide an essential molecular basis for the olfactory perception of D. helophoroides and reliable evidence for recognizing the HIPVs of natural enemies from insect OBPs' perspective" |
| Keywords: | "Animals Herbivory Ecosystem Molecular Docking Simulation *Coleoptera/metabolism *Receptors, Odorant/metabolism Insect Proteins/metabolism Arthropod Antennae/metabolism Dastarcus helophoroides behaviorally attractive substances binding affinities herbivore;" |
| Notes: | "MedlineYi, Shan-Cheng Wu, Yu-Hang Yang, Rui-Nan Li, Dong-Zhen Abdelnabby, Hazem Wang, Man-Qun eng 2019YFD1002105/the National Key Research and Development Program of China/ Switzerland 2023/02/26 Int J Mol Sci. 2023 Feb 9; 24(4):3464. doi: 10.3390/ijms24043464" |
