Three amino acid residues of an odorant-binding protein are involved in binding odours in Loxostege sticticalis L.

doi:10.1111/imb.12179

CORC > 中国农业科学院 > 植物保护研究所

	Three amino acid residues of an odorant-binding protein are involved in binding odours in Loxostege sticticalis L.
	Yin, J.1; Zhuang, X.1; Wang, Q.1; Cao, Y.1; Zhang, S.1; Xiao, C.2; Li, K.1
刊名	INSECT MOLECULAR BIOLOGY
	2015
卷号	24 期号:5 页码:528-538
关键词	Loxostege sticticalis odorant binding protein bioinformatics mutants fluorescence assays
ISSN号	0962-1075
DOI	10.1111/imb.12179
通讯作者	Yin, J.
英文摘要	Odorant-binding proteins (OBPs) play an important role in insect olfactory processes and are thought to be responsible for the transport of pheromones and other semiochemicals across the sensillum lymph to the olfactory receptors within the antennal sensilla. As an important general odorant binding protein in the process of olfactory recognition, LstiGOBP1 of Loxostege sticticalis L. has been shown to have good affinity to various plant volatiles. However, the binding specificity of LstiGOBP1 should be further explored in order to better understand the olfactory recognition mechanism of L. sticticalis. In this study, real-time PCR experiments indicated that LstiGOBP1 was expressed primarily in adult antennae. Homology modelling and molecular docking were then conducted on the interactions between LstiGOBP1 and 1-heptanol to understand the interactions between LstiGOBP1 and their ligands. Hydrogen bonds formed by amino acid residues might be crucial for the ligand-binding specificity on molecular docking, a hypothesis that was tested by site-directed mutagenesis. As predicted binding sites for LstiGOBP1, Thr15, Trp43 and Val14 were replaced by alanine to determine the changes in binding affinity. Finally, fluorescence assays revealed that the mutants Thr15 and Trp43 had significantly decreased binding affinity to most odours; in mutants that had two-site mutations, the binding to the six odours that were tested was completely abolished. This result indicates that Thr15 and Trp43 were involved in binding these compounds, possibly by forming multiple hydrogen bonds with the functional groups of the ligands. These results provide new insights into the detailed chemistry of odours' interactions with proteins.
学科主题	Biochemistry & Molecular Biology ; Entomology
语种	英语
出版者	WILEY-BLACKWELL
WOS记录号	WOS:000360761100003
内容类型	期刊论文
源URL	[http://111.203.20.206/handle/2HMLN22E/11629]
专题	植物保护研究所
作者单位	1.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China 2.Yunnan Agr Univ, Coll Plant Protect, Kunming, Peoples R China
推荐引用方式 GB/T 7714	Yin, J.,Zhuang, X.,Wang, Q.,et al. Three amino acid residues of an odorant-binding protein are involved in binding odours in Loxostege sticticalis L.[J]. INSECT MOLECULAR BIOLOGY,2015,24(5):528-538.
APA	Yin, J..,Zhuang, X..,Wang, Q..,Cao, Y..,Zhang, S..,...&Li, K..(2015).Three amino acid residues of an odorant-binding protein are involved in binding odours in Loxostege sticticalis L..INSECT MOLECULAR BIOLOGY,24(5),528-538.
MLA	Yin, J.,et al."Three amino acid residues of an odorant-binding protein are involved in binding odours in Loxostege sticticalis L.".INSECT MOLECULAR BIOLOGY 24.5(2015):528-538.