New Sights in Odorant-Binding Proteins

A special issue of Biology (ISSN 2079-7737). This special issue belongs to the section "Biochemistry and Molecular Biology".

Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 8994

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Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
Interests: molecular and cellular biology; biochemistry; hair follicle and skin biology; topical delivery; hair follicle targeting; hair and skin disorders and aging; chemicals bioactivity; cosmeceuticals; nanotechnology

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Guest Editor
Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
Interests: proteins for surfaces’ functionalization; enzymatic polymerization; enzymatic reactions; deep eutectic solvents for extraction, cosmetics and textile applications
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Dear Colleagues,

Olfaction functions as a chemosensing system, providing important invisible information about the surroundings and allowing chemical communication between individuals. Odorant-binding proteins (OBPs) are players in this chemical sensing and communication process, acting as carriers of volatile molecules in hydrophilic biofluids. OBPs solubilize odorants from external air and deliver them to the olfactory receptors. OBPs have also been detected in other tissues and in urine, saliva, and sexual secretions. Ergo, these reversible binding and transport of odorants occur in both directions: from and to the environment. Despite the available information, OBPs are still very intriguing proteins with biological functions that go beyond the passive transport of volatile organic compounds. Both vertebrate and invertebrate OBPs are small, extracellular soluble proteins with a hydrophobic binding pocket in their compact structure, highly stable, and easily produced by recombinant expression. OBPs have been incorporated into capture and release systems and biosensors intended for the control of pollution, wine and food quality, security, and clinical diagnosis. OBPs constitute tools in insect population management, particularly for the screening of novel semiochemicals. These properties and the broad ligand specificity that can be further tuned by mutagenesis and post-translation modifications confer on OBPs a great biotechnological value.

Dr. Teresa Matamá
Dr. Carla Silva
Guest Editors

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Keywords

  • odorant-binding protein
  • olfaction
  • chemical sensing
  • chemical communication
  • lipocalin
  • volatile organic compound
  • pheromone
  • fragrance
  • odorant molecules
  • biosensor
  • in silico screening

Published Papers (4 papers)

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Research

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13 pages, 1999 KiB  
Article
Ligand Binding Properties of Odorant-Binding Protein OBP5 from Mus musculus
by Lucie Moitrier, Christine Belloir, Maxence Lalis, Yanxia Hou, Jérémie Topin and Loïc Briand
Biology 2023, 12(1), 2; https://doi.org/10.3390/biology12010002 - 20 Dec 2022
Cited by 1 | Viewed by 1951
Abstract
Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species that are believed to be involved in the transport of odorants toward olfactory receptors. In this study, we report the functional characterization of mouse OBP5 (mOBP5). [...] Read more.
Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species that are believed to be involved in the transport of odorants toward olfactory receptors. In this study, we report the functional characterization of mouse OBP5 (mOBP5). mOBP5 was recombinantly expressed as a hexahistidine-tagged protein in bacteria and purified using metal affinity chromatography. The oligomeric state and secondary structure composition of mOBP5 were investigated using gel filtration and circular dichroism spectroscopy. Fluorescent experiments revealed that mOBP5 interacts with the fluorescent probe N-phenyl naphthylamine (NPN) with micromolar affinity. Competitive binding experiments with 40 odorants indicated that mOBP5 binds a restricted number of odorants with good affinity. Isothermal titration calorimetry (ITC) confirmed that mOBP5 binds these compounds with association constants in the low micromolar range. Finally, protein homology modeling and molecular docking analysis indicated the amino acid residues of mOBP5 that determine its binding properties. Full article
(This article belongs to the Special Issue New Sights in Odorant-Binding Proteins)
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13 pages, 3160 KiB  
Article
The Nature of Functional Features of Different Classes of G-Protein-Coupled Receptors
by Ke An, Xiaohong Zhu and Chen Bai
Biology 2022, 11(12), 1839; https://doi.org/10.3390/biology11121839 - 16 Dec 2022
Cited by 5 | Viewed by 2020
Abstract
G-protein-coupled receptors (GPCRs) are a critical family in the human proteome and are involved in various physiological processes. They are also the most important drug target, with approximately 30% of approved drugs acting on such receptors. The members of the family are divided [...] Read more.
G-protein-coupled receptors (GPCRs) are a critical family in the human proteome and are involved in various physiological processes. They are also the most important drug target, with approximately 30% of approved drugs acting on such receptors. The members of the family are divided into six classes based on their structural and functional characteristics. Understanding their structural–functional relationships will benefit us in future drug development. In this article, we investigate the features of protein function, structure, and energy that describe the dynamics of the GPCR activation process between different families. GPCRs straddle the cell membrane and transduce signals from outside the membrane into the cell. During the process, the conformational change in GPCRs that is activated by the binding of signal molecules is essential. During the binding process, different types of signal molecules result in different signal transfer efficiencies. Therefore, the GPCR classes show a variety of structures and activation processes. Based on the experimental crystal structures, we modeled the activation process of the β2 adrenergic receptor (β2AR), glucagon receptor (GCGR), and metabotropic glutamate receptor 2 (mGluR2), which represent class A, B, and C GPCRs, respectively. We calculated their activation free-energy landscapes and analyzed the structure–energy–function relationship. The results show a consistent picture of the activation mechanisms between different types of GPCRs. This could also provide us a way to understand other signal transduction proteins. Full article
(This article belongs to the Special Issue New Sights in Odorant-Binding Proteins)
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12 pages, 1167 KiB  
Article
Proteomic Characterization of Drosophila melanogaster Proboscis
by Enisa Aruçi, Jean-Michel Saliou, Jean-François Ferveur and Loïc Briand
Biology 2022, 11(11), 1687; https://doi.org/10.3390/biology11111687 - 21 Nov 2022
Cited by 3 | Viewed by 1721
Abstract
Drosophila melanogaster flies use their proboscis to taste and distinguish edible compounds from toxic compounds. With their proboscis, flies can detect sex pheromones at a close distance or by contact. Most of the known proteins associated with probosci’s detection belong to gustatory receptor [...] Read more.
Drosophila melanogaster flies use their proboscis to taste and distinguish edible compounds from toxic compounds. With their proboscis, flies can detect sex pheromones at a close distance or by contact. Most of the known proteins associated with probosci’s detection belong to gustatory receptor families. To extend our knowledge of the proboscis-taste proteins involved in chemo-detection, we used a proteomic approach to identify soluble proteins from Drosophila females and males. This investigation, performed with hundreds of dissected proboscises, was initiated by the chromatographic separation of tryptic peptides, followed by tandem mass spectrometry, allowing for femtomole detection sensitivity. We found 586 proteins, including enzymes, that are involved in intermediary metabolism and proteins dedicated to various functions, such as nucleic acid metabolism, ion transport, immunity, digestion, and organ development. Among 60 proteins potentially involved in chemosensory detection, we identified two odorant-binding proteins (OBPs), i.e., OBP56d (which showed much higher expression in females than in males) and OBP19d. Because OBP56d was also reported to be more highly expressed in the antennae of females, this protein can be involved in the detection of both volatile and contact male pheromone(s). Our proteomic study paves the way to better understand the complex role of Drosophila proboscis in the chemical detection of food and pheromonal compounds. Full article
(This article belongs to the Special Issue New Sights in Odorant-Binding Proteins)
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Review

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23 pages, 2416 KiB  
Review
An Overview of D7 Protein Structure and Physiological Roles in Blood-Feeding Nematocera
by Patricia H. Alvarenga and John F. Andersen
Biology 2023, 12(1), 39; https://doi.org/10.3390/biology12010039 - 26 Dec 2022
Cited by 3 | Viewed by 2242
Abstract
Each time an insect bites a vertebrate host, skin and vascular injury caused by piercing triggers a series of responses including hemostasis, inflammation and immunity. In place, this set of redundant and interconnected responses would ultimately cause blood coagulation, itching and pain leading [...] Read more.
Each time an insect bites a vertebrate host, skin and vascular injury caused by piercing triggers a series of responses including hemostasis, inflammation and immunity. In place, this set of redundant and interconnected responses would ultimately cause blood coagulation, itching and pain leading to host awareness, resulting in feeding interruption in the best-case scenario. Nevertheless, hematophagous arthropod saliva contains a complex cocktail of molecules that are crucial to the success of blood-feeding. Among important protein families described so far in the saliva of blood sucking arthropods, is the D7, abundantly expressed in blood feeding Nematocera. D7 proteins are distantly related to insect Odorant-Binding Proteins (OBP), and despite low sequence identity, observation of structural similarity led to the suggestion that like OBPs, they should bind/sequester small hydrophobic compounds. Members belonging to this family are divided in short forms and long forms, containing one or two OBP-like domains, respectively. Here, we provide a review of D7 proteins structure and function, discussing how gene duplication and some modifications in their OBP-like domains during the course of evolution lead to gain and loss of function among different hematophagous Diptera species. Full article
(This article belongs to the Special Issue New Sights in Odorant-Binding Proteins)
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