Purification and molecular cloning of chemosensory proteins from Bombyx mori

Soluble low molecular weight acidic proteins are suspected to transport sti mulus molecules to the sensory neurons within insect sensilla. From the ant ennae of Bombyx mori, we have purified and sequenced a protein (BmorCSP1) b earing sequence similarity to a class of soluble chemosensory proteins rece ntly discovered in several orders of insects, Based on its N-terminal seque nce, the cDNA encoding this protein has been amplified and cloned. Differen tial screening of a B. mori antennal cDNA library led to the identification of a second gene encoding a related protein (BmorCSP2), sharing 35-40% ide ntity to BmorCSP1 and chemosensory proteins from other species. The predict ed secondary structures of moth's, chemosensory proteins comprise alpha-hel ical foldings at conserved positions and a reduced hydrophobicity with resp ect to this novel family of chemosensory proteins. Arch. insect Biochem. Ph ysiol. 44:120-129, 2000. (C) 2000 Wiley-Liss, Inc.