Due to the biological significance and therapeutic potential of Interleukin-3 (IL-3) secreted mainly by activated T cells, various protein expression systems have been challenged to produce recombinant IL3 to meet the increasing demands worldwide. Recently, we established an updated silkworm-based baculovirus expression vector system (silkworm-BEVS), which in most cases, produces eukaryotic proteins in biological or enzymatical active forms with considerable amounts. We attempted to reconstruct and express a recombinant mouse IL-3 (rMmIL-3) with C-terminal His8-Strep tags in silkworm-BEVS in the current study. From our results, we gained an active glycosylated rMmIL-3 protein in a substantial amount and quality. As compared with the E. coli expression system, silkworm-BEVS is a better choice regarding the glycosylations attached in rMmIL-3 and up-scalable system in case that a commercial amount is required in the future. Collectively, our method shares an excellent model to produce interleukin molecular for approaching pharmaceutical applications.

由于主要由活化 T 细胞分泌的白细胞介素 3 (IL-3) 的生物学意义和治疗潜力，各种蛋白质表达系统都面临着生产重组 IL3 以满足全球日益增长的需求的挑战。最近，我们建立了一种更新的基于蚕的杆状病毒表达载体系统 (silkworm-BEVS)，在大多数情况下，该系统以生物或酶活性形式生产大量真核蛋白质。在当前的研究中，我们试图在蚕-BEVS 中重建和表达具有 C 端 His8-Strep 标签的重组小鼠 IL-3 (rMmIL-3)。根据我们的结果，我们获得了数量和质量都很高的活性糖基化 rMmIL-3 蛋白。与大肠杆菌相比在表达系统中，蚕-BEVS 是 rMmIL-3 中附加的糖基化和可升级系统的更好选择，以防将来需要商业量。总的来说，我们的方法共享一个很好的模型来生产用于接近药物应用的白细胞介素分子。