免疫融合蛋白sFcεRIα/mIg(IgG2)的研制

哮喘、过敏性鼻炎、特应性皮炎及食物过敏等疾病为一类常见疾病,但存在治疗效果不佳,患者病程长等特点。IgE 分子是导致过敏性疾病的关键分子。抑制IgE分子与效应细胞膜表面FcεRI受体的结合可抑制过敏反应的发生。通过克隆FcεRI受体α亚基的cDNA与IgG2的稳定区铰链区、CH2和CH3的cDNA连接,以二聚化融合蛋白sFcεRIα/mIg(IgG2)的形式在CHO细胞中表达,达到提高sFcεRIα生物半衰期的目的。表达载体构建和初步的功能性试验等一系列研究证实,所表达的融合蛋白的分子量为170kDa,并与人IgE和鼠IgE有较好的结合活性。这些研究为该融合蛋白最终实现产业化打下良好基础。

Development of Chimera Protein: sFcεRIα/mIg(IgG2)

IgE plays a key role in type I hypersensitivity reactions. The blocks of IgE binding to its high affinity receptor FcεRI can efficiently eliminate allergic reaction. The sFcεRIα/mIg(IgG2)was constructed by gene fusion of the extracellular portion of α subunit of FcεRI receptor with human IgG2 hing region, CH2 and CH3 region. The chimera could be a markedly longer plasma half-life than the soluble extracellular domain. This chimeric protein was produced by transfecting Chinese Hamster Ovary cells (CHO). Following affinity purification, the apparent molecular weight of sFcεRIα/mIg(IgG2), which showed high affinity with human and mouse IgE, was above 170 kDa. A good foundation for industrialization of this new engineered soluble protein for type I hypersensitivity diseases was provided.