Cloning,expression and binding specificity analysis of odorant binding protein 3 of the lucerne plant bug, <Emphasis Type="Italic">Adelphocoris lineolatus</Emphasis> (Goeze) |
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Authors: | ShaoHua Gu Yang Sun LiYan Ren XueYing Zhang YongJun Zhang KongMing Wu YuYuan Guo |
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Institution: | (1) USDA Beneficial Insects Research Laboratory, 501 S. Chapel St., Newark, DE 19713, USA |
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Abstract: | Credible evidence shows that odorant binding proteins (OBPs) are required for insect olfaction perception and play a key role
in transporting hydrophobic odorants across the sensillum lymph to the olfactory receptors (ORs). In the present study, a
novel OBP (AlinOBP3) gene from the lucerne plant bug, Adelphocoris lineolatus, was cloned and expressed. The expression pattern of AlinOBP3 was evaluated by qPCR, which indicated that AlinOBP3 was dominantly expressed in antennae. The binding properties of AlinOBP3 with 9 cotton volatiles and 5 sex pheromone analogs
were measured by fluorescence competitive binding assays with the fluorescence probe 1-NPN. The results revealed that of 9
cotton volatiles, Myrcene, β-Ocimene and α-Phellandrene can bind with AlinOBP3. α-Phellandrene especially bound to AlinOBP3
with a high binding affinity, with a dissociation constant of 56.68 μmol/L. Of the 5 sex pheromone analogs, Hexyl butyrate
had the strongest binding affinity with AlinOBP3, with a dissociation constant as 59.53 μmol/L. Butyl butyrate, trans-2-Hexenyl
butyrate and Ethyl butyrate had medium binding affinities with AlinOBP3, with dissociation constants of 227.39, 108.77 and
143.47 μmol/L, respectively. The results suggest that AlinOBP3 might be a pheromone binding protein (PBP) with a dual-function
for the perception of sex pheromones and plant volatiles. |
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