Identification of honeybee antennal proteins/genes expressed in a sex- and/or caste selective manner.
We identified three candidate proteins/genes involved in caste and/or sex-specific olfactory processing in the honeybee Apis mellifera L., that are differentially expressed between the antennae of the worker, queen, and drone honeybees using SDS-polyacrylamide gel electrophoresis or the differential display method. A protein was identified, termed D-AP1, that was expressed preferentially in drone antennae when compared to those of workers. cDNA cloning revealed that D-AP1 is homologous to carboxylesterases. Enzymatic carboxylesterase activity in the drone antennae was higher than in the workers, suggesting its dominant function in the drone antennae. In contrast, two proteins encoded by genes termed W-AP1 and Amwat were expressed preferentially in worker antennae when compared to those of queens. W-AP1 is homologous to insect chemosensory protein, and Amwat encodes a novel secretory protein. W-AP1 is expressed selectively in worker antennae, while Amwat is expressed both in the antennae and legs of the workers. These findings suggest that these proteins are involved in the antennal function characteristic to drone or worker honeybees.
Kamikouchi
Azusa
A
Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Japan.
Morioka
Mizue
M
Kubo
Takeo
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001516:Bees / Q000378:metabolism*; D015152:Blotting, Northern; D002265:Carboxylic Ester Hydrolases / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D015870:Gene Expression; D020869:Gene Expression Profiling; D008969:Molecular Sequence Data; D018035:Receptors, Odorant / Q000235:genetics* / Q000378:metabolism*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D012737:Sex Factors; D012930:Social Dominance
D018076:DNA, Complementary; D018035:Receptors, Odorant; D002265:Carboxylic Ester Hydrolases