| Literature DB >> 28801873 |
Zhengying You1, Qiujie Qian1,2, Yiran Wang3, Jiaqian Che1, Lupeng Ye1, Lirong Shen4, Boxiong Zhong5.
Abstract
Major royal jelly protein-1 (MRJP1) is the most abundant glycoprotein of royal jelly (RJ) and is considered a potential component of functional foods. In this study, we used silkworm transgenic technology to obtain five transgenic silkworm lineages expressing the exogenous recombinant Chinese honeybee, Apis cerana cerana, protein-1 (rAccMRJP1) under the control of a fibroin light chain (Fib-L) promoter in the posterior silk glands. The protein was successfully secreted into cocoons; specifically, the highest rAccMRJP1 protein content was 0.78% of the dried cocoons. Our results confirmed that the protein band of the exogenous rAccMRJP1 protein expressed in the transgenic silkworm lineages was a glycosylated protein. Therefore, this rAccMRJP1 protein could be used as an alternative standard protein sample to measure the freshness of RJ. Moreover, we also found that the overall trend between the expression of the endogenous and exogenous genes was that the expression level of the endogenous Fib-L gene declined as the expression of the exogenous rAccMRJP1 gene increased in the transgenic silkworm lineages. Thus, by employing genome editing technology to reduce silk protein expression levels, a silkworm bioreactor expression system could be developed as a highly successful system for producing various valuable heterologous proteins, potentially broadening the applications of the silkworm.Entities:
Keywords: AccMRJP1; Bombyx mori; Glycosylation; Posterior silk gland (PSG); Royal jelly (RJ)
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Year: 2017 PMID: 28801873 DOI: 10.1007/s11248-017-0034-1
Source DB: PubMed Journal: Transgenic Res ISSN: 0962-8819 Impact factor: 2.788