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免疫球蛋白结合蛋白[Immunoglobulin(Ig)-binding protein,IBP]是多种病原体产生的以非抗原形式与免疫球蛋白结合的蛋白,在病原体致病中发挥重要作用。这些蛋白各自具有独特的结构特征及结合特性,赋予其抗体纯化、抗体检测和抗体吸附的应用潜能,已广泛应用于科研、病原体感染抗体特异诊断、抗体药物纯化及临床免疫吸附治疗。应用重组技术所构建的融合IBP较好地保留了母体分子的结合特性,并很好地弥补了各自对不同IgG结合的不足,显著提升了在抗体纯化和免疫沉淀方面的应用优势。应用分子进化技术所获得的由不同IBP单结合结构域组合而成的新型进化免疫球蛋白结合分子(novel evolved immunoglobulin-binding molecule,NEIBM),具有母体IBP所没有的新的Ig结合模式,其中对Ig Fabκ轻链和VH3重链的双位点协同结合大大提高了与IgM的结合能力,并显示出在病原体特异性抗体检测中的应用优势。本文对主要的天然IBP、重组IBP和NEIBM的结构特征、结合特性及其应用作一综述。
Immunoglobulin (Ig) -binding protein (IBP) is a non-antigen-binding immunoglobulin protein produced by a variety of pathogens and plays an important role in pathogenic pathogenesis. Each of these proteins has unique structural features and binding properties, which have given them potential applications in antibody purification, antibody detection and antibody adsorption. They have been widely used in scientific research, antibody specific diagnosis of pathogen infection, antibody drug purification and clinical immunosorbent therapy. The fusion IBP constructed by recombinant technology retains the binding characteristics of the parental molecules well, and it makes up for the deficiencies of their binding to different IgGs, which greatly improves the application advantages in antibody purification and immunoprecipitation. The novel evolved immunoglobulin-binding molecule (NEIBM), which is a combination of different IBP single-binding domains obtained by molecular evolution technique, possesses a novel Ig binding mode that is not found in maternal IBP, Two-site co-binding of the Ig Fabκ light chain and the VH3 heavy chain synergistically increases the binding capacity to IgM and shows an advantage in pathogen-specific antibody detection. This review summarizes the structural features, binding characteristics and their applications of major natural IBP, recombinant IBP and NEIBM.