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Updated: Feb 23, 2026
09:53
Real-time In Vitro Monitoring of Odorant Receptor Activation by an Odorant in the Vapor Phase
Published on: April 23, 2019
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Binding specificity of recombinant odorant-binding protein isoforms is driven by phosphorylation
Fanny Brimau1, Jean-Paul Cornard, Chrystelle Le Danvic
1INRA, UMR8576 CNRS/USTL, UGSF, 59655, Villeneuve d'Ascq, France.
Journal of Chemical Ecology
|July 1, 2010
Summary
Porcine odorant-binding protein (OBP) phosphorylation creates different isoforms with distinct ligand-binding properties. This suggests that phosphorylation patterns regulate OBP function and specificity in pigs.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Native porcine odorant-binding protein (OBP) has multiple phosphorylation sites, indicating potential co-existing isoforms.
- Phosphorylation is a dynamic post-translational modification influencing protein conformation and function.
Purpose of the Study:
- To investigate if OBP isoforms, differing in phosphorylation, exhibit varied binding affinities to biologically relevant ligands.
- To explore the role of phosphorylation in OBP binding capacities using recombinant proteins.
Main Methods:
- Produced recombinant porcine OBP in eukaryotic systems (Pichia pastoris, CHO cells).
- Separated OBP isoforms using anion exchange HPLC.
- Mapped phosphorylation sites via MALDI-TOF mass spectrometry.
- Assessed ligand-binding properties using fluorescence spectroscopy.
Main Results:
- Two recombinant OBP isoforms from yeast, differing in phosphorylation patterns, showed distinct binding affinities.
- Phosphorylation significantly impacts OBP binding properties.
Conclusions:
- Phosphorylation patterns play a crucial role in determining the binding specificity of porcine OBP isoforms.
- This finding has implications for understanding olfactory signaling and protein function regulation.
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