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Gene Review:

OBP - odorant binding protein

Sus scrofa

Burova, T.V. et al., Guiraudie, G. et al., Paolini, S. et al., Johansson, J.S. et al., Burova, T.V. et al., et al.

Johansson, Manderson, Ramoni, Grolli, Eckenhoff,

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High impact information on OBP

Apparently homogeneous odorant binding protein purified from pig nasal mucosa (pOBP) exhibited subunit molecular masses of 17 223, 17 447, and 17 689 (major component) Da as estimated by ESI/MS [1].
A single Gly (121) insertion was found in OBPp when it was compared to OBPb, which may prevent domain swapping from taking place [2].
The proteins belong to the lipocalin superfamily: Alpha-1-acid glycoprotein (AGP), odorant-binding protein (OBP), salivary lipocalin (SAL) and Von Ebner's gland protein (VEG), and displayed different binding capacities for the appeasing compounds [3].
Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein [4].
Large amounts of an odorant-binding protein have been isolated from submaxillary glands of mature male pig [5].

Biological context of OBP

Halothane bound to the cavity in the beta-barrel of porcine odorant binding protein with dissociation constants of 0.46 +/- 0.10 mM and 0.43 +/- 0.12 mM determined using fluorescence quenching and competitive binding with 1-aminoanthracene, respectively [6].

Anatomical context of OBP

Von Ebner gland protein (VEGP) and odorant-binding protein (OBP) were purified from porcine lingual epithelium and nasal mucosa, respectively [7].
An odorant-binding protein, migrating in SDS-PAGE with an apparent molecular weight of 22 kDa and an isoelectric point of 4.2, has been purified from pig nasal mucosa [4].

Associations of OBP with chemical compounds

Isothermal titration calorimetry (ITC) did not detect the binding of either aspartame or denatonium saccharide to VEGP nor did it detect binding of 2-isobutyl-3-methoxypyrazine (IBMP) to OBP [7].
Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: equilibrium studies at neutral pH [8].

Other interactions of OBP

The unfolding transition of VEGP is observed at extremely high temperatures (about 110 degrees C), which is unexpected for a protein with significant structural homology to OBP and other lipocalins [7].

Analytical, diagnostic and therapeutic context of OBP

RT-PCR experiments showed that OBP and VEG are expressed not only in the NM, but also in the VNO and that SAL is only expressed in the VNO [3].
Both VEGP and OBP preparations were homogeneous as indicated by SDS-PAGE, isoelectric focusing, gel-filtration and electrospray mass spectrometry [7].

References

Conformational stability and binding properties of porcine odorant binding protein. Burova, T.V., Choiset, Y., Jankowski, C.K., Haertlé, T. Biochemistry (1999) [Pubmed]
The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Spinelli, S., Ramoni, R., Grolli, S., Bonicel, J., Cambillau, C., Tegoni, M. Biochemistry (1998) [Pubmed]
Functional characterization of olfactory binding proteins for appeasing compounds and molecular cloning in the vomeronasal organ of pre-pubertal pigs. Guiraudie, G., Pageat, P., Cain, A.H., Madec, I., Nagnan-Le Meillour, P. Chem. Senses (2003) [Pubmed]
Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein. Paolini, S., Scaloni, A., Amoresano, A., Marchese, S., Napolitano, E., Pelosi, P. Chem. Senses (1998) [Pubmed]
Lipocalins of boar salivary glands binding odours and pheromones. Marchese, S., Pes, D., Scaloni, A., Carbone, V., Pelosi, P. Eur. J. Biochem. (1998) [Pubmed]
Binding of the volatile general anesthetics halothane and isoflurane to a mammalian beta-barrel protein. Johansson, J.S., Manderson, G.A., Ramoni, R., Grolli, S., Eckenhoff, R.G. FEBS J. (2005) [Pubmed]
Why has porcine VEG protein unusually high stability and suppressed binding ability? Burova, T.V., Rabesona, H., Choiset, Y., Jankowski, C.K., Sawyer, L., Haertlé, T. Biochim. Biophys. Acta (2000) [Pubmed]
Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: equilibrium studies at neutral pH. Parisi, M., Mazzini, A., Sorbi, R.T., Ramoni, R., Grolli, S., Favilla, R. Biochim. Biophys. Acta (2003) [Pubmed]

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