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 AbstractEffect of aging on volatile compounds in cooked beef    Next AbstractIdentification of a new pheromone-binding protein in the antennae of a geometrid species and preparation of its antibody to analyze the antennal proteins of moths secreting type II sex pheromone components »

Invert Neurosci


Title:"Analysis of odorant-binding proteins in antennae of a geometrid species, Ascotis selenaria cretacea, which produces lepidopteran Type II sex pheromone components"
Author(s):Watanabe H; Tabunoki H; Miura N; Sato R; Ando T;
Address:"Graduate School of Bio-Applications and Systems Engineering (BASE), Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan"
Journal Title:Invert Neurosci
Year:2007
Volume:20070522
Issue:2
Page Number:109 - 118
DOI: 10.1007/s10158-007-0046-2
ISSN/ISBN:1354-2516 (Print) 1354-2516 (Linking)
Abstract:"Information on the olfactory system in antennae of Geometridae moths is very limited, and odorant-binding proteins (OBPs) working as transporters of lipophilic odors have not been identified. In the first investigation on this family of insects, we examined antennal OBPs of the Japanese giant looper, Ascotis selenaria cretacea. RT-PCR experiments using several pairs of degenerate primers designed from known cDNA sequences encoding lepidopteran OBPs successfully amplified partial sequences of two pheromone-binding proteins (PBPs), named AscrPBP1 and AscrPBP2 in reference to their corresponding nucleotide sequence homologies with other PBPs. Using 5'- and 3'-rapid amplification of cDNA end strategies, a cDNA clone for AscrPBP1 encoding a protein of 141 amino acids was isolated. Western blotting with the antiserum against recombinant AscrPBP1 overexpressed in Escherichia coli showed that the AscrPBP1 gene was more strongly expressed in male antennae than in female antennae. Furthermore, natural AscrPBP1was isolated by immunoprecipitation with the antiserum, and its binding ability was evaluated by using synthetic sex pheromonal compounds with a C(19) chain. The result indicated that AscrPBP1 bound not only the pheromone components, 3,6,9-nonadecatriene and its 3,4-epoxy derivative, but also unnatural 6,7- and 9,10-epoxy derivatives. While no general odorant-binding proteins (GOBPs) were amplified in the RT-PCR experiments, two antisera prepared from GOBP1 and GOBP2 of Bombyx mori suggested the occurrence of at least two GOBPs in the A. s. cretacea antennae"
Keywords:"Amino Acid Sequence Animals Base Sequence Blotting, Western Female Immunoprecipitation Insect Proteins/*genetics/metabolism Male Mechanoreceptors/*physiology Molecular Sequence Data Moths/*physiology Phylogeny Receptors, Odorant/*genetics/metabolism Rever;"
Notes:"MedlineWatanabe, Hayaki Tabunoki, Hiroko Miura, Nami Sato, Ryoichi Ando, Tetsu eng Germany 2007/05/23 Invert Neurosci. 2007 Jun; 7(2):109-18. doi: 10.1007/s10158-007-0046-2. Epub 2007 May 22"

 
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 15-11-2024