| Title: | Characterization of two odorant binding proteins in Spodoptera exigua reveals functional conservation and difference |
| Author(s): | Liu NY; Zhu JY; Zhang T; Dong SL; |
| Address: | "Key Laboratory of Forest Disaster Warning and Control of Yunnan Province, Southwest Forestry University, Kunming 650224, China; Education Ministry Key Laboratory of Integrated Management of Crop Disease and Pests, College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Education Ministry Key Laboratory of Integrated Management of Crop Disease and Pests, College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Education Ministry Key Laboratory of Integrated Management of Crop Disease and Pests, College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: sldong@njau.edu.cn" |
| Journal Title: | Comp Biochem Physiol A Mol Integr Physiol |
| DOI: | 10.1016/j.cbpa.2017.08.002 |
| ISSN/ISBN: | 1531-4332 (Electronic) 1095-6433 (Linking) |
| Abstract: | "As the first biochemical step of olfactory reception and recognition, odorant binding proteins (OBPs) have been demonstrated to be essential. Considering functional diversities of OBPs within a single species, we here extended the characterization of two other OBPs from Spodoptera exigua, belonging to insect Classic OBPs. With a combination of transcriptome and Rapid Amplification of cDNA End (RACE) approaches, two OBP genes in S. exigua were identified, namely SexiOBP1 and OBP7. Expression pattern analysis revealed that both of them exhibited a distinct expression pattern, where OBP1 was broadly and highly expressed in several tissues including antennae of adults whereas OBP7 was abundant only in the antennae of both sexes, strongly indicative of olfactory roles. Further, binding assays showed that the two SexiOBPs shared a common odorant-response spectrum with considerable affinities to host odorants of acetophenone, farnesol and beta-ionone (K(i)<20muM). Specially, OBP1 could strongly bind an insect attractant beta-caryophyllene (K(i)=2.76muM) released by maize. Intriguingly, the major sex pheromone of S. exigua, Z9,E12-14:Ac, was the best ligand for OBP7 with K(i) value of 7.58muM. Ligand structural analysis revealed that the two SexiOBPs were capable of accommodating different types of ligands in shape and size, possibly implying the plasticity of binding pockets. Ultimately, comparison of binding properties among 10 SexiOBPs including the two OBPs in this study implied a cross-talk in functions, i.e. different OBPs are also suitable to accept some common odorants except for unique ligands. Taken together, this study has provided evidence for their involvements in seeking and orientation of host plants, and meanwhile indicates functional conservation and differences between OBP1 and OBP7 from S. xigua" |
| Keywords: | "Animals Cloning, Molecular Electrophoresis, Polyacrylamide Gel Female Gene Expression Regulation Male Real-Time Polymerase Chain Reaction Receptors, Odorant/genetics/*metabolism Spodoptera/*metabolism Antenna-enriched expression Binding property Expressio;" |
| Notes: | "MedlineLiu, Nai-Yong Zhu, Jia-Yao Zhang, Ting Dong, Shuang-Lin eng 2017/08/16 Comp Biochem Physiol A Mol Integr Physiol. 2017 Nov; 213:20-27. doi: 10.1016/j.cbpa.2017.08.002. Epub 2017 Aug 12" |
