Chem. Senses 25: 541-553,
2000
© Oxford University Press 2000
Chemosensory Proteins from the Proboscis of Mamestra brassicae
INRA, Unité de Phytopharmacie et des Médiateurs Chimiques, Bâtiment A, Route de Saint-Cyr, F-78026 Versailles Cedex, France and 1 Max-Planck-Institut für Verhaltensphysiologie, D-82319 Seewiesen, Germany
Correspondence to be sent to: P. Nagnan-Le Meillour, INRA, UPMC, Bâtiment A, Route de Saint-Cyr, F-78026 Versailles Cedex, France. e-mail: nagnan{at}versailles.inra.fr
Soluble, low molecular weight proteins were immunodetected in proboscis extracts of Mamestra brassicae males by Western blot, using antibodies raised against the general odorant-binding protein of the moth Antheraea polyphemus. The same antibodies weakly labelled the sensillum lymph and subcuticular space of sensilla styloconica on ultrathin sections of the proboscis. The morphology of sensilla styloconica is described. The immunodetected proteins yielded several N-terminal sequences, three of which showed strong affinity for tritiated analogues of pheromonal compounds of M. brassicae in binding assays. The cDNAs coding for these sequences were cloned and it was shown that the new proteins are related to the OS-D protein of Drosophila. They are named chemosensory proteins (CSP-MbraA1CSP-MbraA5 and CSP-MbraB1 and CSP-MbraB2) and may have an odorant-binding protein-like function. A common localization in both olfaction and taste organs suggests a physiological role depending on the cellular environment.
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