While olfactory neurons of silk moths are well known for their exquisite sensitivity to sex pheromone odorants, molecular mechanisms underlying this sensitivity are poorly understood. In searching for proteins that might support olfactory mechanisms, we characterized the protein profile of olfactory neuron receptor membranes of the wild silk moth Antheraea polyphemus. We have purified and cloned a prominent 67-kDa protein which we have named Snmp-1 (sensory neuron membrane protein-1). Northern blot analysis suggests that Snmp-1 is uniquely expressed in antennal tissue; in situ hybridization and immunocytochemical analyses show that Snmp-1 is expressed in olfactory neurons and that the protein is localized to the cilia, dendrites, and somata but not the axons. Snmp-1 mRNA expression increases significantly 1-2 days before the end of adult development, coincident with the functional maturation of the olfactory system. Sequence analysis suggests Snmp-1 is homologous with the CD36 protein family, a phylogenetically diverse family of receptor-like membrane proteins. CD36 family proteins are characterized as having two transmembrane domains and interacting with proteinaceous ligands; Snmp-1 is the first member of this family identified in nervous tissue. These findings argue that Snmp-1 has an important role in olfaction; possible roles of Snmp-1 in odorant detection are discussed.The antennae of silk moths are well known for their exquisite sensitivity to pheremonal odorants (1-3). Early reports demonstrated that the males of the wild silk moth Samia cynthia could locate a sex pheromone source over 2 miles away within several hours of their release (4). Studies of the silk moth Bombyx mori suggested that a single pheromone molecule was sufficient to activate olfactory neurons in the antenna (5). In insects, odors are detected by sensilla, small hair-like structures arrayed along the antennae. The sensilla are hollow, fluid-filled cuticular structures that contain the receptor cilia of olfactory neurons. Small holes penetrate through the wall of a sensillum, permitting entry of odor molecules; odorant-binding proteins are then thought to transport the odor molecules through the fluid-filled lumen to receptor proteins in the receptor membranes of the olfactory neurons (3, 6 -9).In searching for proteins that might support olfactory mechanisms, we characterized the protein profile of olfactory neuron receptor membranes of the wild silk moth Antheraea polyphemus. The morphology of the A. polyphemus antenna permits the relatively easy isolation of olfactory sensilla in a manner yielding olfactory receptor cilia as the only cellular component (10). This preparation is free of other parts of the olfactory neurons as well as of nonneuronal cells of the antenna, and it was previously used to identify a pheromonebinding membrane protein using a radiolabeled photoaffinity analog of the A. polyphemus sex pheromone (10). This protein co-migrated with bovine serum albumin on SDS gels (around 67 kDa) and appeared to be uniquely exp...