Protein Composition of Silk Filaments Spun under Water by Caddisfly Larvae

Abstract

Silk fiber produced by the larvae of Trichoptera (caddisflies) and Lepidoptera (moths and butterflies) is composed of two filaments embedded in a layer of glue proteins. In an aerial environment Lepidoptera spin silk filaments assembled from heavy chain fibroin (H-fibroin), light chain fibroin (L-fibroin), and the glycoprotein P25. The silk filament of caddisflies, which is produced and persists in water, contained homologues of H-fibroin (>500 kDa) and L-fibroin (25 kDa) but not of P25. The amphiphilic nature of H-fibroin and its high content of charged amino acids probably facilitate the secretion and storage of a covalently linked L-fibroin/H-fibroin dimer in the absence of P25. Several types of short amino acid motifs were arranged in orderly fashion in the regularly reiterated repeats that made up more than 95% of the length of H-fibroin. The H-fibroins of Hydropsyche angustipennis and Limnephilus decipiens from different caddisfly suborders contained GPXGX, SXSXSXSX, and GGX motifs such as the lepidopteran and spider silks but differed from them by a lack of poly(A) and poly(GA) motifs. H-fibroins of both caddisfly species harbored a conserved repeat of 31 residues but were distinguished by a few species-specific motifs and their organization in higher order repeats. Structural differences may be related to the silk function as a catching net in H. angustipennis and a stitching fiber in L. decipiens.