文献类型: 外文期刊
作者: Long Xie;Zhenwen Huang;Meiyu Lan;Yaqi Cao;Lingling Sun;Lang Zhang;Erwei Zuo;Yangqing Lu
作者机构:
关键词: (1-2-2)Bioreactor;Deposited foreign protein in eggs;Genetically modified chicken;Nonsecretory protein secretion;Recombinant protein secretion
期刊名称: Journal of Biological Engineering
ISSN: 1754-1611
年卷期: 2024 年 18 卷 1 期
页码:
收录情况: SCIE(2024版)
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/β-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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