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Free keywords:
odorant-binding-protein
pheromone-binding
molecular-cloning
immunocytochemical localization
olfactory sensilla
ligand-binding
moth antennae
lepidoptera
morphology
insecta
Behavioral Sciences
Food Science & Technology
Neurosciences &
Neurology
Physiology
Abstract:
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 com pounds 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-MbraA1-CSP-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.
