Purification and characterization of two odorant-binding proteins from nasal tissue of rabbit and pig

Monte, Massimo Dal; Andreini, Isabella; Revoltella, Roberto P.; Pelosi, Paolo

doi:10.1016/0305-0491(91)90068-o

Cited by 57 publications

(59 citation statements)

References 12 publications

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“…These above results also indirectly indicate that OBPs can bind to various different odorants and also support the results from previous studies, where OBPs were shown to bind to a variety of volatile compounds [5,26,27]. Therefore, OBP subtypes may be part of a larger ligand spectrum and the discovery and characterization of several OBP subtypes in different vertebrate species may be used to identify and tune the selectivity of this ligand spectrum [6,7,28].…”

Section: Discussionsupporting

confidence: 84%

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Specificity of odorant-binding proteins: a factor influencing the sensitivity of olfactory receptor-based biosensors

Lee

et al. 2009

Bioprocess Biosyst Eng

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Odorant-binding proteins (OBPs) primarily function in the transport of hydrophobic odorants. In this study, OBPs originating from rat and pig were cloned into a mammalian expression vector, pcDNA3, and expressed in HEK-293 cells, and their specificity for odorants and olfactory receptors was examined. Results suggest that OBPs have a high affinity for the olfactory receptors when both the OBP and receptor originate from the same species. The rat OBPs were bound not only to the rat olfactory receptor I7 but also to the odorant specific to I7. The solubility of the odorant was increased by both OBP2 and OBP3, which originate from rat, but with different efficiencies. These results demonstrate that OBPs specifically interact with odorants as well as olfactory receptors, and these interactions can influence the sensitivity of olfactory receptor-based biosensors.

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Section: Discussionsupporting

confidence: 84%

“…Historically, OBPs have been defined as non-specific carriers [5]. However, different OBP sub-types have been discovered in the same species and the discovery of several classes of OBPs suggests a role in odor discrimination [6,7]. Studies using recombinant rat OBPs have demonstrated that OBPs have distinct ligand specificity [8].…”

Section: Introductionmentioning

confidence: 98%

Specificity of odorant-binding proteins: a factor influencing the sensitivity of olfactory receptor-based biosensors

Lee

et al. 2009

Bioprocess Biosyst Eng

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“…Several members of this family were later purified from different species of mammals [16][17][18][19][20][21][22][23]. The frog OBP is the only one isolated in a nonmammalian vertebrate [24].…”

Section: Obps and Pbpsmentioning

confidence: 99%

The role of perireceptor events in vertebrate olfaction

Pelosi¹

2001

CMLS, Cell. Mol. Life Sci.

101

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The perception of odours and pheromones is mediated by small soluble carrier proteins that belong to the family of lipocalins. Those secreted by the nasal mucosa are called odorant-binding proteins (OBPs) for their binding activity towards volatile compounds. Proteins of similar structure, which we call pheromone-binding proteins (PBPs), help to deliver volatile pheromones in the environment. They are present in high concentration in biological fluids, such as urine, saliva and vaginal discharge, involved in chemical communication between conspecifics. Several subclasses of OBPs have been identified in the same animal species, each best related to a particular group of PBPs. Such similarities, together with anatomical and behavioural evidence, suggest that OBPs may be involved in the perception of pheromones.

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“…Porcine olfactory binding proteins have been studied extensively because one of the first mammalian OBP was identified in this species (Dal Monte et al 1991;Paolini et al 1998). Besides porcine OBP (pOBP), two other proteins [SAL and Von Ebner's Gland protein (VEG)] were identified and characterized from nasal tissue (Scaloni et al 2001) and the vomeronasal organ (VNO) (Guiraudie et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Natural Ligands of Porcine Olfactory Binding Proteins

et al. 2009

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Knowledge of endogenous ligands of olfactory binding proteins is a prerequisite for studying their role in odor and pheromone transduction. Here, we report the extraction, derivatization, and characterization by gas chromatography-mass spectrometry of the natural ligands of pig, Sus scrofa (L.), Von Ebner's Gland protein (VEG) and odorant binding protein (OBP). We identified two isoforms (VEG1 and VEG2), which differed only by the linkage of an O-N-acetylglucosamine (O-GlcNac) group on VEG1. The natural ligands of VEG1 were characterized as two isomers of testosterone, whereas ligands of VEG2 and OBP were fatty acids or their derivatives. Our findings suggest that the binding specificity of VEG1 for steroids is governed by the presence of an O-GlcNac moiety on the protein. This specificity was confirmed by the binding of radiolabeled testosterone only by VEG1 in an in-gel binding assay. This is the first evidence for a post-translational modification in the process of odorant discrimination by olfactory binding proteins.

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Purification and characterization of two odorant-binding proteins from nasal tissue of rabbit and pig

Cited by 57 publications

References 12 publications

Specificity of odorant-binding proteins: a factor influencing the sensitivity of olfactory receptor-based biosensors

Specificity of odorant-binding proteins: a factor influencing the sensitivity of olfactory receptor-based biosensors

The role of perireceptor events in vertebrate olfaction

Natural Ligands of Porcine Olfactory Binding Proteins

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