Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems
Issued Date
2022-12-01
Resource Type
eISSN
20452322
Scopus ID
2-s2.0-85141164276
Pubmed ID
36323753
Journal Title
Scientific Reports
Volume
12
Issue
1
Rights Holder(s)
SCOPUS
Bibliographic Citation
Scientific Reports Vol.12 No.1 (2022)
Suggested Citation
Kajiura H., Tatematsu K.i., Nomura T., Miyazawa M., Usami A., Tamura T., Sezutsu H., Fujiyama K. Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems. Scientific Reports Vol.12 No.1 (2022). doi:10.1038/s41598-022-22565-7 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/86387
Title
Insights into the quality of recombinant proteins produced by two different Bombyx mori expression systems
Other Contributor(s)
Abstract
The silkworm, Bombyx mori, is an attractive host for recombinant protein production due to its high expression efficiency, quality, and quantity. Two expression systems have been widely used for recombinant protein production in B. mori: baculovirus/silkworm expression system and transgenic silkworm expression system. Both expression systems enable high protein production, but the qualities of the resulting recombinant proteins have not been well evaluated. In this study, we expressed bovine interferon γ (IFN-γ) using the two systems and examined the quality of the resulting proteins in terms of N-glycosylation and protein cleavage. Both expression systems successfully produced IFN-γ as an N-glycoprotein. Although the production in the baculovirus/silkworm expression system was much more efficient than that in the transgenic silkworm expression system, unexpected variants of IFN-γ were also produced in the former system due to the different N-glycosylation and C-terminal truncations. These results indicate that while high protein production could be achieved in the baculovirus/silkworm expression system, unintentional protein modification might occur, and therefore protein expression in the transgenic silkworm expression system is preferable from the point-of-view of N-glycosylation of the recombinant protein and evasion of unexpected attack by a protease in B. mori.