State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, 100101 Beijing, People's Republic of China.
Biotechnol Lett. 2010 Sep;32(9):1271-7. doi: 10.1007/s10529-010-0285-x. Epub 2010 Apr 30.
To improve the secretion and expression of human interferon alpha 2b (IFN) in Lactococcus lactis, a synthetic pro-peptide, LEISSTCDA (LEISS), was fused to the N-terminus of IFN. This gave a higher secretion efficiency (12% vs. 5%) and yield (approximately 2.8-fold) of IFN. The signal peptide, SP(SlpA) (SlpA, an S-layer protein of Lactobacillus brevis), was also tested to secrete IFN instead of SP(Usp45) (Usp45, the main secreted protein in L. lactis). This gave increased IFN secretion (approximately 3-fold) but lower total production. All the recombinant IFN had appropriate bioactivities in an antiviral assay.
为提高人干扰素α2b(IFN)在乳酸乳球菌中的分泌和表达,将一个合成前肽 LEISSTCDA(LEISS)融合到 IFN 的 N 端。这使得 IFN 的分泌效率(12%对 5%)和产量(约 2.8 倍)提高。还测试了信号肽 SP(SlpA)(SlpA,短乳杆菌的 S 层蛋白)代替 SP(Usp45)(Usp45,乳酸乳球菌的主要分泌蛋白)来分泌 IFN。这使得 IFN 的分泌增加(约 3 倍),但总产量降低。所有重组 IFN 在抗病毒测定中均具有适当的生物活性。