Functional characterization of a new class of odorant-binding proteins in the moth Mamestra brassicae

Jonathan Bohbot, Franck Sobrio, Philippe Lucas, Patricia Nagnan-Le Meillour*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

62 Scopus citations

Abstract

A new protocol of binding assay allowed us to functionally characterize two additional odorant-binding proteins in antennae of the moth Mamestra brassicae. These proteins have no N-terminal sequence homology with the moth pheromone-binding proteins and general odorant-binding proteins previously described. One of the proteins designated two MbraAOBP2 is between 60 and 73% similar in N-terminal to several proteins characterized in chemosensory organs of Diptera, Hymenoptera, Lepidoptera, and Phasmids, indicating that these proteins constitute a new group of odorant-binding proteins. A particularly high similarity between MbraAOBP2 and ejaculatory bulb specific protein III of Drosophila suggested that vaccenyl acetate could be a specific ligand for these proteins. As a matter of fact, MbraAOBP2 bound vaccenyl acetate in vitro, but we failed to detect any receptor cell in long and short sensilla trichodea of males. This protocol could be used as a rapid method to identify new odorant-binding proteins in chemosensory organs or tissues.

Original languageAmerican English
Pages (from-to)489-494
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume253
Issue number2
DOIs
StatePublished - 18 Dec 1998
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by INRA (Institut National de la Recherche Agronomique). The authors are grateful to Gunde Ziegelberger for the gift of antibodies, to Jean-Marc Jallon for the gift of tritiated vaccenyl acetate, and to David Tepfer for critical reading of the manuscript.

Keywords

  • Binding assay
  • Mamestra brassicae
  • Odorant-binding proteins
  • Olfaction

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