scholarly journals Three odorant binding proteins may regulate the behavioural response of Chrysopa pallens to plant volatiles and the aphid alarm pheromone (E)-β-farnesene

2017 ◽  
Vol 26 (3) ◽  
pp. 255-265 ◽  
Author(s):  
Z.-Q. Li ◽  
S. Zhang ◽  
X.-M. Cai ◽  
J.-Y. Luo ◽  
S.-L. Dong ◽  
...  
Keyword(s):  
Plant Volatiles ◽  
Binding Proteins ◽  
Alarm Pheromone ◽  
Behavioural Response ◽  
Odorant Binding Proteins ◽  
Odorant Binding ◽  
Aphid Alarm Pheromone

scholarly journals Two Odorant-Binding Proteins Mediate the Behavioural Response of Aphids to the Alarm Pheromone (E)-ß-farnesene and Structural Analogues

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e32759 ◽  
Author(s):  
Yu Feng Sun ◽  
Filomena De Biasio ◽  
Hui Li Qiao ◽  
Immacolata Iovinella ◽  
Shao Xiang Yang ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Alarm Pheromone ◽  
Behavioural Response ◽  
Odorant Binding Proteins ◽  
Structural Analogues ◽  
Odorant Binding

Discrimination of alarm pheromone (E)-β-farnesene by aphid odorant-binding proteins

2009 ◽  
Vol 39 (5-6) ◽  
pp. 414-419 ◽  
Author(s):  
Huili Qiao ◽  
Elena Tuccori ◽  
Xiaoli He ◽  
Angelo Gazzano ◽  
Linda Field ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Alarm Pheromone ◽  
Odorant Binding Proteins ◽  
Odorant Binding

scholarly journals Three odorant-binding proteins are involved in the behavioral response of Sogatella furcifera to rice plant volatiles

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e6576 ◽  
Author(s):  
Kui Hu ◽  
Sheng Liu ◽  
Lin Qiu ◽  
Youzhi Li
Keyword(s):  
Rice Plant ◽  
Plant Volatiles ◽  
Binding Proteins ◽  
Signal Transduction Pathway ◽  
Insect Behavior ◽  
Binding Affinities ◽  
Sogatella Furcifera ◽  
Odorant Binding Proteins ◽  
Weak Binding ◽  
Odorant Binding

Plant volatiles play an important role in regulating insect behavior. Odorant binding proteins (OBPs) are involved in the first step of the olfactory signal transduction pathway and plant volatiles recognition. Sogatella furcifera is one of the most destructive pests of rice crops. Understanding the functions of S. furcifera OBPs (SfurOBPs) in the host plant location and the behavioral responses of S. furcifera to rice plant volatiles could lead to improved, more environmentally-friendly, methods for controlling this pest. We found that SfurOBP1 displayed only weak binding with all the tested volatiles. SfurOBP2, SfurOBP3 and SfurOBP11 had different binding affinities to β-ionone. SfurOBP2 and SfurOBP11 had strong binding affinities to β-caryophyllene (Ki = 2.23 µM) and plant alcohol (Ki = 2.98 µM), respectively. The results of Y-olfactometer experiments indicate that S. furcifera was significantly repelled by octanal and n-octane but strongly attracted by (+)-limonene, acetophenone, 2-heptanone, n-hendecane, α-farnesene and β-ionone. Furthermore, the dsRNA-mediated gene silencing of SfurOBP2, SfurOBP3 and SfurOBP11 shifted the olfactory behavior of S. furcifera for β-ionone, α-farnesene and plant alcohol, respectively. These results suggest that the SfurOBPs are involved in the recognition of rice plant volatiles, and several potential repellants and lures for controlling this pest.

scholarly journals GOBP1 Plays a Key Role in Sex Pheromones and Plant Volatiles Recognition in Yellow Peach Moth, Conogethes punctiferalis (Lepidoptera: Crambidae)

Insects ◽  
2019 ◽  
Vol 10 (9) ◽  
pp. 302
Author(s):  
Jing ◽  
Zhang ◽  
Bai ◽  
Prabu ◽  
He ◽  
...  
Keyword(s):  
Host Plant ◽  
Binding Affinity ◽  
Plant Volatiles ◽  
Sex Pheromones ◽  
Binding Proteins ◽  
Prunus Persica ◽  
Olfactory Sensilla ◽  
Odorant Binding Proteins ◽  
Yellow Peach Moth ◽  
Odorant Binding

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.

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