Many insects have sexually dimorphic antennae with sensilla peculiar to one sex specialized to detect sex pheromones released by the other sex. In the moth Manduca sexta, the axons of receptor cells in the male-specific sensilla as well as those common to both sexes terminate in the antennal lobes of the brain. We have used 2-dimensional electrophoresis (2DE) to study some of the proteins that are produced by sensory receptor cells in developing antennae and transported through their axons to the brain. Extracts of antennal nerves from mature male and female M. sexta yield nearly identical 2DE patterns of proteins after staining or fluorography. Gels prepared from antennal nerves of developing animals, however, exhibit a sexual dimorphism in the quantitative pattern of at least 2 classes of proteins. One class consists of four 49 kDa proteins of similar charge, designated 49a, 49b, 49c, and 49d in order of decreasing mobility on nonequilibrium pH gradient electrophoresis gels. The total amount and apparent rate of synthesis of 49b and 49d are ca. 4- to 7-fold greater in antennal nerves of developing males than in those of females. Protein 49c is comparably enriched in female antennal nerves, while 49a is enriched ca. 1.2-fold in females. The second class consists of a single polypeptide of 24 kDa, which is nearly undetectable in silver-stained gels but was shown to be ca. 9-fold enriched in males by fluorography. At the end of adult development, male and female moths have similar patterns of the 49 kDa polypeptides, and synthesis of the 24 kDa polypeptide is reduced to nearly undetectable levels. The patterns of sexual dimorphism thus appear to be associated with the growth and maturation of antennal sensory axons into the antennal lobes. Biosynthesis of the 24 kDa polypeptide was nearly undetectable in antennal lobes or fragments of antennal nerves incubated in vitro with radiolabeled methionine. The 49 and 24 kDa polypeptides appear to belong to separate classes of rapidly transported proteins. The 24 kDa polypeptide is among the most rapidly transported proteins; it is found exclusively in a particulate fraction and is associated with plasma membrane but apparently not mitochondria. The 49 kDa polypeptides are found in both the particulate and soluble fractions; the more basic 49a and 49b are enriched in the particulate fraction, while the more acidic 49c and 49d are enriched in the soluble fraction.