Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractInvestigating Chemical Composition and Indications of Hydrosol Soft Drinks (Aromatic Waters) Used in Persian Folk Medicine for Women's Hormonal and Reproductive Health Conditions    Next AbstractEffect of microwave hydrolysis on transformation of steroidal hormones during anaerobic digestion of municipal sludge cake »

Sci Rep


Title:Crystal structure of Epiphyas postvittana pheromone binding protein 3
Author(s):Hamiaux C; Carraher C; Lofstedt C; Corcoran JA;
Address:"The New Zealand Institute for Plant and Food Research Limited, Auckland, New Zealand. Department of Biology, Lund University, Lund, Sweden. Biological Control of Insects Research Laboratory, USDA - Agricultural Research Service, Columbia, MO, USA. jacob.corcoran@usda.gov"
Journal Title:Sci Rep
Year:2020
Volume:20201001
Issue:1
Page Number:16366 -
DOI: 10.1038/s41598-020-73294-8
ISSN/ISBN:2045-2322 (Electronic) 2045-2322 (Linking)
Abstract:"The insect olfactory system operates as a well-choreographed ensemble of molecules which functions to selectively translate volatile chemical messages present in the environment into neuronal impulses that guide insect behaviour. Of these molecules, binding proteins are believed to transport hydrophobic odorant molecules across the aqueous lymph present in antennal sensilla to receptors present in olfactory sensory neurons. Though the exact mechanism through which these proteins operate is still under investigation, these carriers clearly play a critical role in determining what an insect can smell. Binding proteins that transport important sex pheromones are colloquially named pheromone binding proteins (PBPs). Here, we have produced a functional recombinant PBP from the horticultural pest, Epiphyas postvittana (EposPBP3), and experimentally solved its apo-structure through X-ray crystallography to a resolution of 2.60 A. Structural comparisons with related lepidopteran PBPs further allowed us to propose models for the binding of pheromone components to EposPBP3. The data presented here represent the first structure of an olfactory-related protein from the tortricid family of moths, whose members cause billions of dollars in losses to agricultural producers each year. Knowledge of the structure of these important proteins will allow for subsequent studies in which novel, olfactory molecule-specific insecticides can be developed"
Keywords:"Animals Carrier Proteins/*metabolism Insect Proteins/*metabolism Molecular Structure Moths/*metabolism Olfactory Receptor Neurons/*metabolism Receptors, Odorant/metabolism Sensilla/*metabolism Sex Attractants/metabolism;"
Notes:"MedlineHamiaux, Cyril Carraher, Colm Lofstedt, Christer Corcoran, Jacob A eng Research Support, Non-U.S. Gov't England 2020/10/03 Sci Rep. 2020 Oct 1; 10(1):16366. doi: 10.1038/s41598-020-73294-8"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 23-11-2024