期刊
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
卷 227, 期 -, 页码 75-82出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpb.2018.10.001
关键词
Odorant-binding protein; Plus-C subfamily; Expression patterns; Ligand binding; Homology modeling, molecular docking
资金
- Key Laboratory of Biology, Genetics and Breeding of Special Economic Animals & Plants, Ministry of Agriculture, P. R. China [Y2018PT14]
- National Natural Science Foundation of China [31501652, 31471778]
- Zhejiang Provincial Natural Science Foundation of China [LQ16C140003]
- Central public interest Scientific Institution Basal Research Fund [1610212018010]
- Research Foundation of State Key Laboratory for Biology of Plant Diseases and Insect Pests [SKLOF201719]
Odorant-binding proteins (OBPs) can bind and transport hydrophobic odorants across the sensillum lymph to the olfactory receptors (ORs) and play crucial roles in insect chemosensory systems. Although the ligand spectra of classical OBPs have been extensively characterized, little is known about OBPs in the Plus-C subgroup. Here, we focus on AlinOBP14, a Plus-C OBP from the hemipteran mirid bug pest Adelphocoris lineolatus (Goeze). Quantitative real-time PCR experiments suggest that AlinOBP14 is ubiquitously expressed at different developmental stages but is highly expressed in the adult head, the non-chemosensory organ. Fluorescence-based competitive binding assays show that beta-ionone, nerolidol, farnesol and insect juvenile hormone III (JHIII) strongly bind to AlinOBP14. No significant internal binding pocket is predicted by homology modeling. Instead, the long N-terminal and C-terminal regions and parts of several alpha-helixes form a cupped cavity to accommodate ligands. Molecular docking reveals that the four potential ligands have distinct binding orientations, implying different roles of the N-terminal extension in ligand recognition. This hypothesis is further confirmed via a ligand binding assay in which the recombinant N-terminal mutant AlinOBP14 displays comparable binding affinities for beta-ionone and trans, trans-farnesol but decreased binding affinities for nerolidol and JHIII. Thus, our current study is the first to characterize the ligand binding spectra of a Plus-C OBP in hemipteran insect species and reveals that N-terminal extensions could be required for its recognition of putative ligands.
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