2007/12/23 by Katsura Kojima, Yoshihiko Kuwana, Hideki Sezutsu +4 · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Immunology and Microbiology · Materials Science · #Biochemistry #Biology #Bombyx mori #Cell biology #Chemistry #Fibroin #Gene #Green fluorescent protein #Invertebrate Immune Response Mechanisms #Materials science #Molecular biology #Plasmid #SILK #Silk-based biomaterials and applications #Transgene #Viral Infectious Diseases and Gene Expression in Insects
paper · doi:10.1271/bbb.70353
openalex publication_date 2007/12/23 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/26
We constructed a new plasmid vector for the production of a modified silk fibroin heavy chain protein (H-chain) in the transgenic silkworm. The plasmid (pHC-null) contained the promoter and the 3' region of a gene encoding the H-chain and the coding regions for the N-terminal domain and the C-terminal domain of the H-chain. For the model protein, we cloned a foreign gene that encoded EGFP between the N-terminal domain and the C-terminal domain in pHC-null and generated transgenic silkworms that produced a modified H-chain, HC-EGFP. Transgenic silkworms produced HC-EGFP in the posterior part of silk gland cells, secreted it into the lumen of the gland, and produced a cocoon with HC-EGFP as part of the fibroin proteins. N-terminal sequencing of HC-EGFP localized the signal sequence cleavage site to between positions A((21)) and N((22)). These results indicate that our new plasmid successfully produced the modified H-chain in a transgenic silkworm.