文献类型： 外文期刊
作者： Xie, Long 1 ; Huang, Zhenwen 1 ; Lan, Meiyu 1 ; Cao, Yaqi 2 ; Sun, Lingling 1 ; Zhang, Lang 1 ; Zuo, Erwei 2 ; Lu, Yangqing 1 ;
作者机构： 1.Guangxi Univ, State Key Lab Conservat & Utilizat Subtrop Agrobio, Nanning, Peoples R China
2.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Guangdong Lab Lingnan Modern Agr, Shenzhen Branch,Minist Agr & Rural Affairs,Key Lab, Shenzhen, Peoples R China
关键词： Genetically modified chicken; Deposited foreign protein in eggs; Recombinant protein secretion; Nonsecretory protein secretion; Bioreactor
期刊名称：JOURNAL OF BIOLOGICAL ENGINEERING （ 影响因子：5.6； 五年影响因子：5.5 ）
ISSN： 1754-1611
年卷期： 2024 年 18 卷 1 期
页码：
收录情况： SCI
摘要： Maternal secretion of recombinant proteins into chicken eggs may provide a viable approach for pharmaceutical production but remains limited by poor secretion efficiency through the membrane of oviduct cells, despite high expression levels. Here, we used site-specific integration of an EGFP fused to the OVAL gene by a rigid linker, (EAAAK)3, at the endogenous ovalbumin locus in chicken primordial germ cells to generate OVAL-E3-EGFP transgenic chickens, with transgenic chickens expressing CMV immediate enhancer/beta-actin-driven EGFP (CAG-EGFP) as a non-secreted control. In OVAL-E3-EGFP chickens, EGFP protein produced in maternal oviducts accumulates to high levels in eggs, but not in eggs of CAG-EGFP chickens. These results indicated that the secretion of foreign proteins can be substantially increased through fusion to the highly secreted endogenous ovalbumin. This study describes a basis for high yield recombinant protein expression in chicken eggs, enabling rapid and scalable production of numerous pharmaceutical proteins or metabolites.
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