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Title: Structural and Functional Characterization of European Corn Borer, Ostrinia nubilalis, Pheromone Binding Protein 3
Ostrinia nubilalis, a lepidopteran moth, also known as the European corn borer, has a major impact on the production of economically important crops in the United States and Europe. The female moth invites the male moth for mating through the release of pheromones, a volatile chemical signal. Pheromone binding proteins (PBPs) present in the male moth antennae are believed to pick up the pheromones, transport them across the aqueous sensillum lymph, and deliver them to the olfactory receptor neurons. Here we report for the first time the cloning, expression, refolding, purification, and structural characterization of Ostrinia nubilalis PBP3 (OnubPBP3). The recombinant protein showed nanomolar affinity to each isomer of the Ostrinia pheromones, E- and Z-11-tetradecenyl acetate. In a pH titration study by nuclear magnetic resonance, the protein exhibited an acid-induced unfolding at pH below 5.5. The molecular dynamics simulation study demonstrated ligand-induced conformational changes in the protein with both E- and Z-isomers of the Ostrinia pheromone. The simulation studies showed that while protein flexibility decreases upon binding to E-pheromone, it increases when bound to Z-pheromone. This finding suggests that the OnubPBP3 complex with E-pheromone is more stable than with Z-pheromone.  more » « less
Award ID(s):
1726397 1807722
NSF-PAR ID:
10345462
Author(s) / Creator(s):
Date Published:
Journal Name:
Journal of agricultural and food chemistry
Volume:
69
Issue:
46
ISSN:
1520-5118
Page Range / eLocation ID:
14013-14023
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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