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Conserved odorant-binding proteins from aphids and eavesdropping predators.

Sophie Vandermoten1, Frédéric Francis, Eric Haubruge

  • 1Gembloux Agro-Bio Tech, Functional and Evolutionary Entomology, University of Liege, Gembloux, Belgium.

Plos One
|September 14, 2011
PubMed
Summary
This summary is machine-generated.

Odorant-binding proteins (OBPs) in aphids and their predators show conserved binding to (E)-ß-farnesene, a key aphid alarm pheromone. This suggests conserved olfactory mechanisms across distinct insect orders for processing this semiochemical.

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Area of Science:

  • * Insect chemical ecology and olfactory system research.
  • * Comparative genomics and molecular biology of insect communication.

Background:

  • * (E)-ß-farnesene is a critical alarm pheromone for aphids like Sitobion avenae.
  • * Predators, including Episyrphus balteatus and Harmonia axyridis, use (E)-ß-farnesene as a kairomone to locate prey.
  • * Aphid-predator interactions provide a model for studying conserved olfactory processing of semiochemicals.

Purpose of the Study:

  • * To investigate the conservation of odorant-binding proteins (OBPs) in binding (E)-ß-farnesene across different insect taxa.
  • * To determine if OBPs from aphids and their predators share conserved binding properties for this key semiochemical.

Main Methods:

  • * Cloning and expression of OBP genes from Sitobion avenae and its predators.
  • * Utilizing fluorescence-based assays to test binding affinities of recombinant OBPs.
  • * Testing binding of (E)-ß-farnesene and other relevant volatile compounds.

Main Results:

  • * OBPs from aphids and predators exhibit high conservation, with no apparent orthologues in other insect species.
  • * Recombinant SaveOBP3 (aphid) and EbalOBP3 (hoverfly) specifically bind (E)-ß-farnesene with high affinity.
  • * These conserved OBPs showed no binding affinity for related compounds.

Conclusions:

  • * Insect species from distinct orders possess conserved OBPs that specifically bind common semiochemicals.
  • * This study demonstrates conserved molecular mechanisms for semiochemical detection across diverse insect taxa.
  • * OBPs play a crucial role in the specific recognition of (E)-ß-farnesene in aphid-predator communication systems.