摘要
Z结构域,又叫免疫球蛋白结合结构域,是由金黄色葡萄球菌蛋白A(Staphylococal Protein A,SPA)中B结构域改构而成。SPA是从金黄色葡萄球菌的细胞壁中发现的能与多种哺乳动物的抗体相结合的天然蛋白,组成SPA的5个结构域中,以B结构域的抗体结合力及稳定性占绝对优势。将B结构域28～29位敏感性残基Asn-Gly定向诱变成为Asn-Ala后,得到的结构域被称为Z结构域,其稳定性更高,可耐受羟铵和溴化氢的处理。首尾相连的两个Z结构域,被命名为ZZ结构域,具有与SPA相类似的抗体结合容量以及更高的稳定性,可以耐受工业纯化中苛刻的环境。ZZ结构域以其独特的反3α螺旋结构、以及特有的抗体结合能力已广泛应用于外源蛋白的可溶表达及免疫检测、抗体纯化等领域。该文将对ZZ与抗体结合的机制研究以及它在各领域的应用研究进行综述。
Z domain, also called IgG binding domain, is derived from the B domain of Staphylococcal Protein A （SPA）. SPA is a cell wall associated protein exposed on the surface of the bacterium Staphylococcus aureus. SPA has a high affinity to IgG from most mammalian species. It consists of five homologous domains which are individually IgG-binding and the B domain holds the best bind- ing ability. In order to increase domain B＇s stability, the sensitive Asn-Gly dipeptide at residues 28-29 is changed by site directed mutagenesis to Asn-Ala, resulting in an engineered domain denoted Z. Two Z domains joined end to end （designated the ZZ domain） have similar molar binding capacity for IgG as the native SPA, but better stability, which makes it possible to withstand the hash environment in industry purifications. Due to its unique antiparallel three α-helical structures, and its high affinity to IgG, ZZ domain has found its widespread use as a tool in the detection and purification of antibodies, as well as soluble expression of heterologous proteins. In this review, the studies of binding mechanism and the applications in various fields are focused.
出处
《药物生物技术》
CAS
CSCD
2012年第3期274-277,共4页
Pharmaceutical Biotechnology
基金
先声药业研究生创新基金(No.02704051)
江苏省普通高校研究生科研创新计划资助(No.CXLX11_0799)
