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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。
Asthma, allergic rhinitis, atopic dermatitis and food allergies and other diseases as a common disease, but there are poor treatment, patients with longer duration and so on. IgE molecules are the key molecules that cause allergic diseases. Inhibition of IgE molecules and effector cell membrane surface FcεRI receptor binding can inhibit the occurrence of allergic reactions. By cloning the cDNA of the FcεRI receptor α subunit and the hinge region of the IgG2 stable region, the cDNAs of CH2 and CH3 are expressed in CHO cells as dimerized fusion protein sFcεRIα / mlg (IgG2) to increase the biological half-life of sFcεRIα the goal of. A series of studies, including expression vector construction and preliminary functional test, confirmed that the expressed fusion protein has a molecular weight of 170 kDa and good binding activity with human IgE and mouse IgE. These studies lay a solid foundation for the final industrialization of the fusion protein.