Identification of the chitin-binding proteins from the larval proteins of silkworm, Bombyx mori.

The silkworm is a model organism for Lepidoptera. Its cuticle is composed mainly of chitin and proteins, which plays essential roles in multiple physiological functions. The binding of proteins to chitin plays an important role for cuticle formation. In this research, a chitin-binding assay followed by a proteomics analysis was carried out using the proteins extracted from the 5th instar larval cuticles. As results, twenty-two proteins were identified including nine cuticular proteins, two lysozyme precursors, two proteins with chitin-binding-type 2 domains, and other proteins. A cuticular protein with the RR-1 consensus, BmorCPR56, and a silkworm Tweedle protein, BmorCPT1, were detected in the chitin-binding fraction for the first time and their chitin-binding activities were further confirmed in vitro. The results of this research increase our understanding of the structure of the silkworm larval cuticle.