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The Insect Attractant 1-Octen-3-ol Is the Natural Ligand of Bovine Odorant-binding Protein

Authors :
Christian Cambillau
Florence Vincent
François-Didier Boyer
Roberto Ramoni
Mariella Tegoni
Silvia Spinelli
Christian Malosse
Patricia Nagnan-Le Meillour
Stefano Grolli
Virna Conti
University of Parma = Università degli studi di Parma [Parme, Italie]
Architecture et fonction des macromolécules biologiques (AFMB)
Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)
Unité de recherche Phytopharmacie et Médiateurs Chimiques (UPMC)
Institut National de la Recherche Agronomique (INRA)
Unité de phytopharmacie et médiateurs chimiques
Centre National de la Recherche Scientifique (CNRS)
Source :
Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2001, 276 (10), pp.7150-7155. ⟨10.1074/jbc.M010368200⟩
Publication Year :
2001
Publisher :
HAL CCSD, 2001.

Abstract

Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-A resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet et al. (1996) Nat. Struct. Biol. 3, 934-939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-A resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors like Anopheles (Plasmodium) or Glossina (Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.

Details

Language :
English
ISSN :
00219258 and 1083351X
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2001, 276 (10), pp.7150-7155. ⟨10.1074/jbc.M010368200⟩
Accession number :
edsair.doi.dedup.....bf115051c0e8cbd9704df0201ee79818
Full Text :
https://doi.org/10.1074/jbc.M010368200⟩