Functional characteristic analysis of three odorant‐binding proteins from the sweet potato weevil ( Cylas formicarius ) in the perception of sex pheromones and host plant volatiles

2020 ◽  
Vol 77 (1) ◽  
pp. 300-312
Author(s):  
Jinfeng Hua ◽  
Chao Pan ◽  
Yongmei Huang ◽  
Yanqing Li ◽  
Huifeng Li ◽  
...  
Insects ◽  
2019 ◽  
Vol 10 (9) ◽  
pp. 302
Author(s):  
Jing ◽  
Zhang ◽  
Bai ◽  
Prabu ◽  
He ◽  
...  

Insects recognize odorous compounds using sensory neurons organized in olfactory sensilla. The process odor detection in insects requires an ensemble of proteins, including odorant binding proteins, olfactory receptors, and odor degrading enzymes; each of them are encoded by multigene families. Most functional proteins seem to be broadly tuned, responding to multiple chemical compounds with different, but mostly quite similar structures. Based on the hypothesis that insects recognize host volatiles by means of general odorant binding proteins (GOBPs), the current study aimed to characterize GOBPs of the yellow peach moth, Conogethes punctiferalis (Guenée). In oviposition preference tests, it was found that the yellow peach moth preferred volatiles from Prunus persica (peach) in finding their host plant. Exposure of the moth to volatiles from peaches affected the expression level of GOBP genes. Binding affinity of GOBPs from yellow peach moth was assessed for 16 host plant volatiles and 2 sex pheromones. The fluorescence ligand-binding assays revealed highest affinities for hexadecanal, farnesol, and limonene with KD values of 0.55 ± 0.08, 0.35 ± 0.04, and 1.54 ± 0.39, respectively. The binding sites of GOBPs from yellow peach moth were predicted using homology modeling and characterized using molecular docking approaches. The results indicated the best binding affinity of both GOBP1 and GOBP2 for farnesol, with scores of −7.4 and −8.5 kcal/mol. Thus, GOBPs may play an important role in the process of finding host plants.


Sensor Review ◽  
2017 ◽  
Vol 37 (4) ◽  
pp. 396-403 ◽  
Author(s):  
Yanli Lu ◽  
Yao Yao ◽  
Shuang Li ◽  
Qian Zhang ◽  
Qingjun Liu

Purpose Using the remarkable olfaction ability, insects can sense trace amounts of host plant volatiles that are notorious for causing severe damage to fruits and vegetables and in consequence the industry. The purpose of the paper is to investigate the interactions between olfactory proteins, odorant-binding proteins (OBPs) and host plant volatiles through the developed olfactory biosensors. It might be helpful to develop novel pest control strategies. Design/methodology/approach Using the successfully expressed and purified OBPs of the oriental fruit fly Bactrocera dorsalis, a biosensor was developed by immobilizing the proteins on interdigitated electrodes through nitrocellulose membrane. Based on electrochemical impedance sensing, benzaldehyde emitted by the host plants, such as Beta vulgaris, was detected, which could be used to investigate and analyze the mechanisms of pests’ sense of chemical signals. The relative decreases of charge transfer resistances of the sensor were proportional to the odorant concentrations from 10−7 M to 10−3 M. Meanwhile, the interactions between OBPs and benzaldehyde were studied through the process of molecular docking. Findings The paper provides a pest OBPs-based biosensor that could sensitively detect the host odorants benzaldehyde. Meanwhile, the most related amino acids of OBPs that bind to host plant volatiles can be distinguished with molecular docking. Originality/value An olfactory biosensor was developed to explore interactions and mechanism between the pest OBPs and benzaldehyde, which showed promising potentials for small organic molecule sensing. Simultaneously, it might be helpful for novel pest control strategies.


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