基于大豆种子油体系统表达重组白介素il-21的研究-study on expression of recombinant interleukin il - 21 in soybean seed oil system.docxVIP
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基于大豆种子油体系统表达重组白介素il-21的研究-study on expression of recombinant interleukin il - 21 in soybean seed oil system
Seed oil-body as the carrier for recombinant interleukin IL21 in transgenic SoybeanAbstractAs an important storage compartment of plants, seeds are promising a desirable platform for production of large quantity of recombinant pharmaceutical proteins. Among different plant-based system, plant seeds hold several advantages such as high protein yields, long-term stability of target proteins, easiness of storage and transplantation, suitability of later extraction and recovery. In the past two decades, significant advances in using seeds as bioreactors have occurred for production of many recombinant proteins with some of them moving down the commercialization pipeline. Generally, the newly synthesized proteins in cells are targeted to various cellular compartments for storage such as cytosol, plastids, endoplasmic reticulum (ER), protein storage vacuoles (PSVs), oil bodies (OB) and apoplasts along the secretory pathway. The subcellar localization not only has a significant impact on yield and stability of the recombinant proteins, but also affects post-translational modifications and normal functioning of the proteins. OB is a lipid-containing structure surrounded by a layer consisting of /wiki/Phospholipidphospholipids and the protein /wiki/Oleosinoleosin. By fused with the /wiki/Oleosinoleosin protein, the recombinant proteins can be effectively targeted to the oil-bodies of seeds, thus facilitating the recovery and purification of the plant-derived proteins. Production of the recombinant protein based oil bodies has become an interesting alternative in plant bioreactor research field. Based on the characteristics of soybean seeds which contain approximately 40% protein, 20% oil by weight, we made use of a soybean 24kD oleosin to target fused interleukin IL-21 to the surface of the soybean OB for high and stable expression of the recombinant protein in soybean seeds. Our results might provide an effective production platform with scalability and low-cost for the rec
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