Abstract
Chemosensory proteins (CSPs) are a class of small, soluble proteins present at high concentrations in chemosensory organs of different insect species. Several pieces of evidence suggest their involvement in carrying chemical messages from the environment to chemosensory receptors. However, a structural description of the mechanism of delivery has not been reported. In order to provide the ®rst detailed
conformational characterization of these molecules, we cloned a speci®c isoform (CSP-sg4) from Schistocerca gregaria and expressed it in Escherichia coli. The product was obtained with yields of more than 20 mg per L of culture, all in its soluble form. The recombinant protein was identical to the native one with respect to pairing of the disul®de bridges, aggregative state and secondary structure elements. Structural investigations revealed a signicantly stable polypeptide with respect to variations in temperature and acidity. CD analysis, preliminary NMR data and
secondary structure prediction pointed to a correctly folded structure where helical regions and loops are alternated in a similar fashion as that observed for other classes of odorantand pheromone-binding proteins presenting no sequence
similarity to CSPs.