Bioinformatic analysis of gene encoding odorant binding protein (OBP) 1, OBP2, and chemosensory proteins in Grapholita molesta
文献类型: 外文期刊
作者: Zhao, Zhiguo 1 ; Liu, Baoling 1 ; Rong, Erhua 1 ; Zhang, Lijun 1 ; Guo, Yanqiong 1 ; Li, Jie 2 ; Kong, Weina 3 ; Ma, Ruiy 1 ;
作者机构: 1.Shanxi Agr Univ, Coll Agr, Jinzhong 030801, Shanxi, Peoples R China
2.Shanxi Acad Agr Sci, Pomol Inst, Jinzhong 030815, Shanxi, Peoples R China
3.Shanxi Acad Agr Sci, Inst Plant Protect, Taiyuan 030801, Shanxi, Peoples R China
关键词: Grapholita molesta;Odorant binding protein;Chemosensory protein;Bioinformatics analysis;Pest
期刊名称:BIOCHEMICAL SYSTEMATICS AND ECOLOGY ( 影响因子:1.381; 五年影响因子:1.351 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: In this study, odorant binding proteins (OBPs) and chemosensory protein (CSP), which are associated with the sensitivity of Grapholita molesta, were comprehensively analysed using bioinformatics. The full-length cDNAs of GmolOBP1, GmolOBP2, and Gmo1CSP were downloaded and their open reading frames (ORFs) were analysed. Their physicochemical properties were determined and their structures and functions were predicted. Additionally, a phylogenetic tree was constructed to investigate the evolutionary relationships among GmolOBP1, GmolOBP2, Gmo1CSP, and 14 other insect proteins. GmolOBP1, Gmo1OBP2 and GmoICSP were composed of 164, 161, and 127 amino acids. GmolOBP1 and GmolOBP2 contained 7 and 6 cysteine residues forming 3 disulphide bonds. The trans membrane, hydrophobic, and signal peptide regions overlapped in GmoIOBP1 and Gmo1CSP and were located in the extracellular environment. Gmo1CSP showed more coiled coils and a smaller cavity in the three-dimensional structure than GmolOBP1 and GmolOBP2. In the phylogenetic tree, GmolOBP1, GmolOBP2, and GmoICSP were in different clusters or sub-clusters. In conclusion, GmolOBP1 and GmolOBP2 shared some common properties with other OBPs. Additionally, GmolOBP1, GmolOBP2, and GmoICSP may have evolved independently. (C) 2016 Elsevier Ltd. All rights reserved.
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