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The silk gland of  Bombyx mori  (BmSG) has gained significant attention by dint of superior synthesis and secretion of proteins. However, the application of BmSG bioreactor is still a controversial issue because of low yields of recombinant proteins. Here, a 3057 bp full-length coding sequence of  Hpl  was designed and transformed into the silkworm genome, and then the mutant ( Hpl / Hpl ) with specific expression of  Hpl  in posterior BmSG (BmPSG) was obtained. In the mutants, the transcription level of  Fib-L  and  P25 , and corresponding encoding proteins, did not decrease. However, the mRNA level of  Fib-H  was reduced by 71.1%, and Fib-H protein in the secreted fibroin was decreased from 91.86% to 71.01%. The mRNA level of  Hpl  was 0.73% and 0.74% of  Fib-H  and  Fib-L , respectively, while HPL protein accounted for 18.85% of fibroin and 15.46% of the total amount of secreted silk protein. The exogenous protein was therefore very efficiently translated and secreted. Further analysis of differentially expressed gene (DEG) was carried out in the BmPSG cells and 891 DEGs were detected, of which 208 genes were related to protein metabolism. Reduced expression of endogenous silk proteins in the BmPSG could effectively improve the production efficiency of recombinant exogenous proteins.

High yield exogenous protein HPL production in the Bombyx mori silk gland provides novel insight into recombinant expression systems