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机构地区:[1]中国人民解放军第二军医大学基础部病原生物学教研室,上海200433
出 处:《中国生物制品学杂志》2014年第1期135-140,共6页Chinese Journal of Biologicals
基 金:国家自然科学基金(30872405;30972632);国家科技重大专项课题传染病专项(2009ZX10004-105);国家科技重大专项课题重大新药专项(2011ZX09506-001)
摘 要: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 proteins are derived from various pathogens, which binding to Ig in form of non- antigen and play an important role in pathogenesis. The proteins have unique structures and antibody-binding characteris- tics, conferring their potential applications in purification, detection and adsorption of antibody, which have been widely applied in detection of pathogen-specific antibody, purification of antibody drugs, immunoadsorption therapy, and antibody- associated scientific researches. The fusion IBP proteins constructed through recombinant technology maintain the binding properties of their parent proteins and, based on complementation each other, acquire the application advantages in antibody purification and immunoprecipitation. Novel evolved Ig binding molecules (NEIBMs) yielded by in vitro molecular evolution consist of specific combination of the binding domains from different IBPs, and produce the new Ig binding modes. The novel Ig binding properties of some NEIBMs with the double-site binding to VH3 and VK regions of human Ig Fab create the high affinity for human IgM, and present application advantage in detection of pathogen-specific antibodies. This paper reviews the structural and binding characteristics as well as application of natural IBP, recombinant IPB and MEIBM.
关 键 词:细菌 免疫球蛋白结合蛋白 新型进化免疫球蛋白结合分子
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