An ovalbumin fusion strategy to increase recombinant protein secretion in chicken eggs

文献类型： 外文期刊

第一作者： Xie, Long

作者： Xie, Long;Huang, Zhenwen;Lan, Meiyu;Sun, Lingling;Zhang, Lang;Lu, Yangqing;Xie, Long;Cao, Yaqi;Zuo, Erwei

作者机构：

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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