New insight into the mechanism of in vivo fibroin self-assembly and secretion in the silkworm, Bombyx mori

Fibroin of the silkworm consists of fibroin heavy chain (Fib-H) with hydrophobic intermediate repeats flanked by hydrophilic N and C terminal domains (NTD and CTD, respectively), fibroin light chain (Fib-L), and P25. However, the respective roles of each polypeptide in silk processing remain largely unknown. Here, a series of transgenic silkworms with different fusion gene expression cassettes were created in order to selectively express different fluorescent fusion proteins in silk glands. The roles of different components in silk processing were investigated via observing and analyzing the movement and distribution of these proteins in the silk gland and in cocoon silk. The data showed that hydrophilic NTDs were distributed on the surface of micelles, providing sufficient electrostatic repulsion to prevent premature crystallization of silk proteins. Hydrophilic CTD==Ls (== represents the disulfide bond) were located on the inner layer of micelles to control the solubility of large micelles. The results presented here elucidated the underlying mechanisms of silkworm silk processing in vivo. This is significant for the development of artificial spinning technology, novel silk biomaterials, and silk gland expression systems. (C) 2020 Elsevier B.V. All rights reserved.

Automated summary

Silk fibroin of the silkworm consists of different components, each playing distinct roles in silk processing. The hydrophilic NTDs and CTDs are shown to be located differently in micelles, providing electrostatic repulsion and controlling solubility, respectively. This elucidates the underlying mechanisms of silkworm silk processing.