| Title: | Identification and functional analysis of odorant-binding proteins of the parasitoid wasp Scleroderma guani reveal a chemosensory synergistic evolution with the host Monochamus alternatus |
| Author(s): | Huang G; Liu Z; Gu S; Zhang B; Sun J; |
| Address: | "State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China. Hebei Basic Science Center for Biotic Interactions/College of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding 071002, China. Department of Entomology, China Agricultural University, Beijing 100193, China. State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China; Hebei Basic Science Center for Biotic Interactions/College of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding 071002, China. Electronic address: sunjh@ioz.ac.cn" |
| DOI: | 10.1016/j.ijbiomac.2023.126088 |
| ISSN/ISBN: | 1879-0003 (Electronic) 0141-8130 (Linking) |
| Abstract: | "Scleroderma guani is a generalist ectoparasitoid of wood-boring insects. The chemosensory genes expressed in its antennae play crucial roles in host-seeking. In the present study, we identified 14 OBP genes for the first time from the antennae transcriptomes and genomic data of S. guani. The expression profiles of 14 OBPs were tested by RT-qPCR, and the RT-qPCR results showed that SguaOBP2/5/6/11/12/13 were specifically highly expressed in the female antennae. Then we performed ligand binding assays to test the interactions between six selected SguaOBPs with host specific chemical compounds from M. alternatus and pines. The binding results indicated that SguaOBP12 had a higher binding affinity with longifolene, beta-caryophyllene, alpha-pinene, beta-pinene, myrcene, butylated hydroxytoluene, and 3-carene. SguaOBP11 had a high or medium binding affinity with them. Furthermore, both SguaOBP11 and SguaOBP12 had a medium binding affinity with the aggregation pheromone of Monochamus species, 2-undecyloxy-1-ethanol. Finally, by using molecular docking and RNAi, we further explored the molecular interactions and behavioral functions of SguaOBP11 and SguaOBP12 with these vital odor molecules. Our study contributes to the further understanding of chemical communications between S. guani and its host, and further exploration for its role as a more effective biological control agent" |
| Keywords: | "Female Animals *Wasps/genetics Odorants Molecular Docking Simulation *Coleoptera/genetics Pheromones Insect Proteins/metabolism *Receptors, Odorant/chemistry Phylogeny Binding assay Odorant binding proteins RNA interference Scleroderma guani;" |
| Notes: | "MedlineHuang, Guangzhen Liu, Zhudong Gu, Shaohua Zhang, Bin Sun, Jianghua eng Netherlands 2023/08/03 Int J Biol Macromol. 2023 Sep 30; 249:126088. doi: 10.1016/j.ijbiomac.2023.126088. Epub 2023 Jul 31" |
