THE B-PROTEINS SECRETED BY THE TUBULAR ACCESSORY SEX GLANDS OF THE MALE MEALWORM BEETLE, TENEBRIO-MOLITOR, HAVE SEQUENCE SIMILARITY TO MOTHPHEROMONE-BINDING PROTEINS

B proteins represent one of the four major protein groups secreted by the tubular accessory glands of adult, male mealworm beetles. They are acidic proteins with an apparent molecular mass of 18,8kDa. In this p aper we present the deduced amino-acid sequences of two, almost identi cal B proteins, termed Bf and B2, The mature proteins are Ifs amino ac ids long. They contain 11 (B2) or 12 (B1) possible phosphorylation sit es and are rich in glutamic acid (16%). Lectin binding experiments ind icate the presence of asparagine linked carbohydrate, The secondary st ructure of the B proteins is predicted to be almost completely alpha-h elical. The B proteins show significant sequence resemblance to a grou p of pheromone- and odorant-binding proteins in moths and Drosophila, suggesting a role as carrier proteins for lipids.