Therapeutic proteins expressed using transgenic animals have been of great interest for several years. Especially, transgenic silkworm has been studied intensively because of its ease in handling, low cost, high-yield, and unique glycosylation patterns. However, the physicochemical property of the therapeutic protein expressed in transgenic silkworm remains elusive. Here we constructed an expression system for the TNFR-Fc fusion protein (Etanercept) using transgenic silkworm. The TNFR-Fc fusion protein was employed to N-glycan analysis, which revealed an increased amount of afucosylated protein. Evidence from SPR analysis showed that the TNFR-Fc fusion protein exhibit increased binding affinity for Fcγ Receptor IIIa, and FcRn, compared to the commercial Etanercept, emphasizing the profit of expression system using transgenic silkworm. We have further discussed the comparison of higher order structure, thermal stability, and aggregation of the TNFR-Fc fusion protein.

中文翻译：

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使用转基因蚕产生的TNFR-Fc融合蛋白（Etanercept）的结构见解和稳定性。

使用转基因动物表达的治疗性蛋白质已引起人们极大的兴趣。尤其是，转基因蚕由于易于处理，成本低，产量高以及独特的糖基化模式而受到了广泛的研究。然而，在转基因家蚕中表达的治疗性蛋白质的物理化学性质仍然难以捉摸。在这里我们使用转基因蚕构建了TNFR-Fc融合蛋白（Etanercept）的表达系统。TNFR-Fc融合蛋白用于N-聚糖分析，结果表明岩藻糖基化蛋白的含量增加。SPR分析的证据表明，与市售Etanercept相比，TNFR-Fc融合蛋白对Fcγ受体IIIa和FcRn的结合亲和力增强，强调了使用转基因蚕的表达系统的收益。