抗菌肽CM4与人可溶性B淋巴细胞因子hsBAFF在大肠杆菌中的融合表达

为进一步探讨抗菌肽CM4的原核表达及其生物学功能，本实验研究了抗菌肽CM4与人可溶性B淋巴细胞刺激因子hsBAFF的融合表达及抗菌肽CM4的生物学活性。运用PCR把B淋巴细胞因子hsBAFF和家蚕抗菌肽CM4进行基因融合，构建了融合表达载体pET28a (+)/CM4-hsBAFF，并在大肠杆菌中获得高可溶性表达的融合靶蛋白，且存在于超声破碎后的上清，经分子筛Sephadex G-75纯化后的重组融合蛋白用SDS-PAGE和Western blot分析鉴定.SDS-PAGE分析表明：可以通过分子筛一步纯化得到融合蛋白，该重组融合蛋白的分子量约22.0 KDa。Western blot结果显示该重组蛋白能与鼠抗人hsBAFF的抗体发生特异性反应.运用基因工程的方法获得CM4-hsBAFF重组融合蛋白，并具有很好的抑菌生物学活性。

The expression of antibacterial peptide CM4 in Escherichia coli fused with human soluble B lymphocyte stimulator activing factor

To explore the expression and function of antibacterial peptide CM4, the expression and biological activity of recombinant fusion protein CM4-hsBAFF were studied. The human soluble B lymphocyte stimulator activing factor (hsBAFF) gene was fused to the sequence encoding CM4 to construct an expression vector pET28a (+)/CM4-hsBAFF. The recombinant protein was high expression of soluble recombinant protein in Escherichia coli cells, and existed in the supernatant after sonication. Recombinant fusion protein which was purified through size-exclusion chromatography was identified by SDS-PAGE and Western blot analysis. SDS-PAGE and Western blot indicated that recombinant protein was secreted as a protein of around 22.0 KDa and can be specially recognized anti-hsBAFF antibody. The recombinant protein can be expressed and displays antimicrobial activity.