ArticleScientific reports2018
Structure and Function Studies of Asian Corn Borer Ostrinia furnacalis Pheromone Binding Protein2.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Heterologous expression, structural analysis, and functional characterization of Ostrinia nubilalis pheromone-binding protein 2 (OnubPBP2).Scientific reports · 2026Article
- Pheromone-Binding Proteins in Pest Control: From Molecular Insights to Real-World Applications.Journal of agricultural and food chemistry · 2025Review
- The functional of cathepsin L in the ontogenesis and reproductive regulation of the Asian corn borer, Ostrinia furnacalis.Scientific reports · 2025Article
- In Vitro and In Silico Studies for the Identification of Potent Metabolites of Some High-Altitude Medicinal Plants from Nepal Inhibiting SARS-CoV-2 Spike Protein.Molecules (Basel, Switzerland) · 2022Article
- Ostrinia furnacalis PBP2 solution NMR structure: Insight into ligand binding and release mechanisms.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Lepidopteran male moths have an extraordinarily sensitive olfactory system that is capable of detecting and responding to minute amounts of female-secreted pheromones over great distances. Pheromone-binding proteins (PBPs) in male antennae ferry the hydrophobic ligand across the aqueous lymph to the olfactory receptor neuron triggering the response. PBPs bind ligands at physiological pH of the lymph and release them at acidic pH near the receptor while undergoing a conformational change. In Anthereae polyphemus PBP1, ligand binding to the hydrophobic pocket and its release is regulated by two biological gates: His70 and His95 at one end of the pocket and C-terminus tail at the other end. Interestingly, in Asian corn borer Ostrinia furnacalis PBP2 (OfurPBP2), critical residues for ligand binding and release are substituted in both biological gates. The impact of these substitutions on the ligand binding and release mechanism in OfurPBP2 is not known. We report here overexpression of soluble OfurPBP2 and structural characterization at high and low pH by circular dichroism (CD) and NMR. Ligand binding and ab initio model development were carried out with fluorescence and small-angle X-ray scattering (SAXS) respectively. OfurPBP2 in solution at pH 6.5 is homogeneous, well-folded and has a compact globular shape.
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Registered trials
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