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 AbstractExpression of pheromone binding proteins during antennal development in the gypsy moth Lymantria dispar    Next AbstractOdorant-binding-protein subfamilies associate with distinct classes of olfactory receptor neurons in insects »

J Neurosci


Title:Molecular cloning and sequencing of general odorant-binding proteins GOBP1 and GOBP2 from the tobacco hawk moth Manduca sexta: comparisons with other insect OBPs and their signal peptides
Author(s):Vogt RG; Rybczynski R; Lerner MR;
Address:"Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510"
Journal Title:J Neurosci
Year:1991
Volume:11
Issue:10
Page Number:2972 - 2984
DOI: 10.1523/JNEUROSCI.11-10-02972.1991
ISSN/ISBN:0270-6474 (Print) 1529-2401 (Electronic) 0270-6474 (Linking)
Abstract:"Odorant-binding proteins (OBPs) are small, water-soluble proteins uniquely expressed in olfactory tissue of insects and vertebrates. OBPs are present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid. OBPs may represent the initial biochemical recognition step in olfaction, because they transport odorants to the receptor neurons. Insect OBPs are represented by multiple classes: pheromone-binding proteins (PBPs) and general odorant-binding proteins (GOBP1 and GOBP2). PBPs associate with pheromone-sensitive neurons, while GOBPs associate with general odorant-sensitive neurons. Analysis of N-terminal amino acid sequences of 14 insect OBPs isolated from six species indicated that the PBPs were variable and the GOBPs were highly conserved. However, inferred properties of these proteins were based only on partial sequence data. We now report the full-length sequences of a GOBP1 and GOBP2 from the moth Manduca sexta and compare these sequences with those of PBPs from three species, including M. sexta, Antheraea polyphemus, and A. pernyi. We also compare these with a GOBP2 of A. pernyi, previously identified only as a novel OBP. These comparisons fully support our N-terminal analysis. The signal peptide sequences of seven insect OBPs reveal conserved sequences within OBP classes, but not between OBP classes even within the same animal species. This suggests that multiple OBPs may be coexpressed in the same cell type, but differentially processed in a class-specific manner. Properties of the GOBPs suggest that general olfaction is broadly receptive at the periphery. Properties of the PBPs suggest that pheromone olfaction is discriminatory at the periphery, and that the initial biochemical steps in pheromone detection may play an active role in odor perception"
Keywords:"Amino Acid Sequence Animals Blotting, Northern Carrier Proteins/*genetics *Cloning, Molecular DNA/genetics Gene Library Insecta/*metabolism Molecular Sequence Data Moths/*metabolism Polymerase Chain Reaction Protein Biosynthesis Protein Sorting Signals/*m;"
Notes:"MedlineVogt, R G Rybczynski, R Lerner, M R eng R01-NS27086/NS/NINDS NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1991/10/01 J Neurosci. 1991 Oct; 11(10):2972-84. doi: 10.1523/JNEUROSCI.11-10-02972.1991"

 
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 16-11-2024