Porcine Odorant-binding Protein Selectively Binds to a Human Olfactory Receptor

Matarazzo, Valéry; Zsürger, Nicole; Guillemot, Jean‐Claude; Clot-Faybesse, Olivier; Botto, J.; Farra, Claude Dal; Crowe, Mark L.; Demaille, Jacques; Vincent, Jean‐Pierre; Mazella, Jean; Ronin, Catherine

doi:10.1093/chemse/27.8.691

Cited by 54 publications

(47 citation statements)

References 42 publications

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“…This does not mean that porcine OBPs only bind to olfactory receptors originating from same species. In contrast to our results, an interaction between the human olfactory receptor and the porcine OBP has been reported [25]. 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].…”

Section: Discussionsupporting

confidence: 86%

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: 86%

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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“…Whether or not the ligand-linked alterations of OBP dynamics seen in this study are sufficient to allow recognition of the ligation state of OBPs by the olfactory receptor remains to be seen. In any event, the presence of such conformational modifications provide additional, unforeseen elements which may enrich potential chemoreception mechanisms such as those proposed by Matarazzo et al (19).…”

Section: Discussionmentioning

confidence: 92%

Odorant Binding and Conformational Dynamics in the Odorant-binding Protein

Hajjar

Pérahia

Débat

et al. 2006

Journal of Biological Chemistry

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In mammals, the olfactory epithelium secretes odorantbinding proteins (OBPs), which are lipocalins found freely dissolved in the mucus layer protecting the olfactory neurons. OBPs may act as passive transporters of predominantly hydrophobic odorant molecules across the aqueous mucus layer, or they may play a more active role in which the olfactory neuronal receptor recognizes the OBP-ligand complex. To better understand the molecular events accompanying the initial steps in the olfaction process, we have performed molecular dynamics studies of rat and pig OBPs with the odorant molecule thymol. These calculations provide an atomic level description of conformational changes and pathway intermediates that remain difficult to study directly. A series of eight independent molecular dynamics trajectories of rat OBP permitted the observation of a consensus pathway for ligand unbinding and the calculation of the potential of mean force (PMF) along this path. Titration microcalorimetry confirmed the specific binding of thymol to this protein with a strong hydrophobic component. In both rat and pig OBPs we observed lipocalin strand pair opening in the presence of ligand, consistent with potential roles of these proteins in olfactive receptor recognition.

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“…The primary approach is experimental, where excitatory responses are identified following the exposure of olfactory receptor neurons (one receptor corresponds to one neuron) to a panel of odorants. [9][10][11][12] Excitatory responses that arise from these interactions over a range of concentrations of odorants (typically organic chemical compounds) are then measured. This opinion paper is primarily concerned with the secondarycomputational-approach.…”

Section: Opinionmentioning

confidence: 99%

“…Functional studies have established this odorant as strongly excitatory for the hOR17-209 receptor. 12 The figures represent the simulation box that is used for our molecular dynamics simulations. This box consists of a model of the receptor in yellow.…”

Section: Re-addressing the Or-odorant Interaction Paradigmmentioning

confidence: 99%

Novel Paradigm for Odorant-Olfactory Receptor Interactions

Crasto¹

2016

MOJPB

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Abbreviations: GPCR, g (TP-binding) protein coupledreceptors; HMM, hidden markov models; OR, olfactory receptor(s); NMR, nuclear magnetic resonance; TM, transmembrane; RMSD, root mean square displacement; RMSF, root mean square fluctuations OpinionThe publication of the discovery of olfactory receptors (OR) in 1991 1 sparked burgeoning research efforts in the domain of chemoreception. The need to study the role of olfactory receptors in olfaction became imperative, following the publication of the initial drafts of the human genome. Olfactory or olfactory-like receptors mined from the human genome constituted its largest family, possessing between 350 and 400 functional ORs genes. [2][3][4] Interestingly, the functional genes in the OR super family were a little more than third of the approximately, 1000 olfactory receptor repertoire mined from the genome the remaining are non-functional or pseudogenes. This raises very important questions as to how the sense of smell in human beings has evolved. Rodent 5,6 and canine 7 OR repertoires (consisting of about 1200 OR genes), when mined from their genomes, showed, that approximately, half of these genes were pseudogenic, or otherwise, non-functional. More recently, the OR repertoire from the African elephant genome listed 5000 ORs, of which, 40% are functional. 8One of the primary challenges in the study of ORs is elucidating the mechanism(s) by which a few hundred ORs in mammals discriminate several thousand odorants from the environment, which singly or in combination produce distinct and identifiable odors. OR-odorant interactions are promiscuous: one OR is known to bind multiple odorants; odorants, in turn, are known to interact with more than one OR.Research in deorphanizing ORs-identifying odorants or odors that are likely to bind an OR-has adopted a two-pronged approach. The primary approach is experimental, where excitatory responses are identified following the exposure of olfactory receptor neurons (one receptor corresponds to one neuron) to a panel of odorants. [9][10][11][12] Excitatory responses that arise from these interactions over a range of concentrations of odorants (typically organic chemical compounds) are then measured. This opinion paper is primarily concerned with the secondarycomputational-approach. This approach has often been a companion to the experimental functional analysis approach. 13,14 But it is increasingly coming into its own as an independent sub-domain of study. Computational studies involve studying the interactions between ORs and odorants, in silico. This paper will culminate in the recommendation to revisit the established paradigms related to the computational approaches for deorphanizing ORs. The challenges facing in silico approachesORs are membrane bound proteins. They belong to a class of fairly ubiquitous proteins called G(TP-binding) Protein Coupled Receptors (GPCRs). These receptors, following excitatory responses to stimuli (an interaction with an odorant or odor) bind to a G-protein and initiate a cytoplasmic signal...

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Porcine Odorant-binding Protein Selectively Binds to a Human Olfactory Receptor

Cited by 54 publications

References 42 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

Odorant Binding and Conformational Dynamics in the Odorant-binding Protein

Novel Paradigm for Odorant-Olfactory Receptor Interactions

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