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"Alcohol, volatile fatty acid, phenol, and methane emissions from dairy cows and fresh manure"    Next AbstractIdentification of floral scent in chrysanthemum cultivars and wild relatives by gas chromatography-mass spectrometry »

PLoS One


Title:"Functional characterization of chemosensory proteins in the scarab beetle, Holotrichia oblita Faldermann (Coleoptera: Scarabaeida)"
Author(s):Sun H; Guan L; Feng H; Yin J; Cao Y; Xi J; Li K;
Address:"State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, P.R. China; College of Plant Science, Jilin University, Changchun, Jilin Province, P.R. China. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, P.R. China. College of Plant Science, Jilin University, Changchun, Jilin Province, P.R. China"
Journal Title:PLoS One
Year:2014
Volume:20140904
Issue:9
Page Number:e107059 -
DOI: 10.1371/journal.pone.0107059
ISSN/ISBN:1932-6203 (Electronic) 1932-6203 (Linking)
Abstract:"Chemosensory proteins (CSPs) play important roles in chemical communication by insects, as they recognize and transport environmental chemical signals to receptors within sensilla. In this study, we identified HoblCSP1 and HoblCSP2 from a cDNA library of Holotrichia oblita antennae, successfully expressed them in E. coli and purified them by Ni ion affinity chromatography. We then measured the ligand-binding specificities of HoblCSP1 and HoblCSP2 to 50 selected ligands in a competitive binding assay. These results demonstrated that HoblCSP1 and HoblCSP2 have similar ligand-binding spectra. Both proteins displayed the highest affinity for beta-ionone, alpha-ionone and cinnamaldehyde, indicating that they prefer binding to odorants other than sex pheromones. Additionally, immuno-localization revealed that HoblCSP1 is highly concentrated in sensilla basiconica, while HoblCSP2 is specifically localized to sensilla placodea. In conclusion, HoblCSP1 and HoblCSP2 are responsible for binding to general odorants with slightly different specificities due to their different in vivo environments"
Keywords:"Acrolein/analogs & derivatives/chemistry/metabolism Amino Acid Sequence Animals Arthropod Antennae/*metabolism/ultrastructure Binding, Competitive Coleoptera/classification/genetics/*metabolism Escherichia coli/genetics/metabolism Female Gene Expression I;"
Notes:"MedlineSun, Hongyan Guan, Li Feng, Honglin Yin, Jiao Cao, Yazhong Xi, Jinghui Li, Kebin eng Research Support, Non-U.S. Gov't 2014/09/05 PLoS One. 2014 Sep 4; 9(9):e107059. doi: 10.1371/journal.pone.0107059. eCollection 2014"

 
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 22-11-2024