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Molecular Mechanisms Subserving Taste and Olfaction Systems

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".

Deadline for manuscript submissions: 30 May 2024 | Viewed by 1191

Special Issue Editor


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Guest Editor
Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA
Interests: ingestive behavior; taste; chemosensory systems; food learning & memory; gut-brain axis

Special Issue Information

Dear Colleagues,

Olfaction and gustation are the two main sensory systems that subserve nutrition. Our ability to rapidly and accurately sense the odorants and tastants released from foods enables us to locate, select, and ingest the essential compounds required for good health and survival, and avoid those that may be detrimental. Although both chemosensory systems come hardwired to detect these biologically significant substances in the environment, they are also highly plastic, shaped by experience and physiological conditions. Empirical evidence has showcased the sheer complexity of canonical and non-canonical molecular machinery present in chemosensory end organs and pathways, through which their signals are broadcast to higher-order brain areas for integrative processing. However, precise knowledge on how these peripheral and central systems facilitate dynamic sensing and orchestrate adaptive behaviors, as well as how they are in turn regulated by diverse factors (such as genes, diets and disease states across the lifespan), is lacking. For this Special Issue, we invite original research articles and critical reviews that advance our understanding of the molecular mechanisms that subserve chemosensory function.

Dr. Lindsey Schier
Guest Editor

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Keywords

  • taste
  • olfaction
  • gustation
  • odor
  • chemoreception
  • taste bud cells
  • nutrient sensing
  • ingestive behavior
  • olfactory cilia
  • olfactory receptor neurons
  • olfactory bulb
  • gustatory cortex
  • piriform cortex
  • sensory development
  • food learning
  • neural plasticity
  • obesity
  • eating disorders
  • appetite

Published Papers (1 paper)

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Research

17 pages, 7716 KiB  
Article
EsigPBP3 Was the Important Pheromone-Binding Protein to Recognize Male Pheromones and Key Eucalyptus Volatiles
by Hengfei Fu, Guipeng Xiao, Zhende Yang and Ping Hu
Int. J. Mol. Sci. 2024, 25(5), 2940; https://doi.org/10.3390/ijms25052940 - 03 Mar 2024
Viewed by 773
Abstract
Pheromone-binding proteins (PBPs) are specific odorant-binding proteins that can specifically recognize insect pheromones. Through transcriptional analysis of the antennae of adult Endoclita signifer, EsigPBP3 was discovered and identified, and EsigPBP3 was found to be highly expressed in the antennae of male moths. [...] Read more.
Pheromone-binding proteins (PBPs) are specific odorant-binding proteins that can specifically recognize insect pheromones. Through transcriptional analysis of the antennae of adult Endoclita signifer, EsigPBP3 was discovered and identified, and EsigPBP3 was found to be highly expressed in the antennae of male moths. Based on the binding characteristics and ability of EsigPBP3, we can find the key ligands and binding site to consider as a target to control the key wood bore E. signifier. In this study, the fluorescence competitive binding assays (FCBA) showed that EsigPBP3 had a high binding affinity for seven key eucalyptus volatiles. Molecular docking analysis revealed that EsigPBP3 had the strongest binding affinity for the sexual pheromone component, (3E,7E)-4,7,11-trimethyl-1,3,7,10-dodecatetraene. Furthermore, same as the result of FCBA, the EsigPBP3 exhibited high binding affinities to key eucalyptus volatiles, eucalyptol, α-terpinene, (E)-beta-ocimene, (−)-β-pinene, and (−)-α-pinene, and PHE35, MET7, VAL10, PHE38, ILE52, and PHE118 are key sites. In summary, EsigPBP3 exhibits high binding affinity to male pheromones and key volatile compounds and the crucial binding sites PHE35, MET7, VAL10, PHE38, ILE52, and PHE118 can act as targets in the recognition of E. signifier pheromones. Full article
(This article belongs to the Special Issue Molecular Mechanisms Subserving Taste and Olfaction Systems)
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