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 Abstract"Characterization of the bacterial community composition in a hypoxic zone induced by Microcystis blooms in Lake Taihu, China"    Next AbstractConstruction and analysis of cDNA libraries from the antennae of Batocera horsfieldi and expression pattern of putative odorant binding proteins »

Int J Biol Macromol


Title:Molecular recognition of floral volatile with two olfactory related proteins in the Eastern honeybee (Apis cerana)
Author(s):Li H; Zhang L; Ni C; Shang H; Zhuang S; Li J;
Address:"Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, China"
Journal Title:Int J Biol Macromol
Year:2013
Volume:20130208
Issue:
Page Number:114 - 121
DOI: 10.1016/j.ijbiomac.2013.01.032
ISSN/ISBN:1879-0003 (Electronic) 0141-8130 (Linking)
Abstract:"The honeybee relies on its sensitive olfaction to perform the foraging activities in the field. In the antennal chemoreception system of honeybee, odorant-binding proteins (OBPs) and chemosensory protein (CSPs) are major two protein families capable of binding with some plant volatiles and chemical ligands. However, the chemical binding interaction of plant odors with OBPs and CSPs in the honeybee olfactory system is still not clear yet. Hence, complex fluorescent spectra, ultraviolet absorption spectra, circular dichroism spectra and molecular docking were used to investigate the binding property of AcerASP2 (an OBP of Apis cerana) and AcerASP3 (a CSP of Apis cerana) with beta-ionone, one of ordinary floral volatiles in botanical flower. As a result, beta-ionone had a strong capability to quench the fluorescence that the two proteins produced, and their interaction was a dynamic process that was mainly driven by a hydrophobic force. AcerASP2 had a larger hydrophobic cavity than that of AcerASP3 and the conformation of AcerASP2 was changed less than AcerASP3 when binding with beta-ionone. Our data suggests that OBPs like AcerASP2 might make a large contribution toward assisting the honeybee in sensing and foraging flowers, and A. cerana has evolved a good circadian rhythm to perceive a flower's odor following the fluctuation of temperature in the olfactory system. This significantly extends our knowledge on how to strengthen the honeybees' pollination service via manipulation of target proteins in the olfactory system"
Keywords:Amino Acid Sequence Animals Bees Circular Dichroism Flowers/*chemistry Insect Proteins/chemistry/isolation & purification/*metabolism Kinetics Molecular Docking Simulation Molecular Sequence Data Norisoprenoids/chemistry/*metabolism Olfactory Pathways/*me;
Notes:"MedlineLi, Hongliang Zhang, Linya Ni, Cuixia Shang, Hanwu Zhuang, Shulin Li, Jianke eng Research Support, Non-U.S. Gov't Netherlands 2013/02/14 Int J Biol Macromol. 2013 May; 56:114-21. doi: 10.1016/j.ijbiomac.2013.01.032. Epub 2013 Feb 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 27-12-2024