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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。
The Z domain, also called the immunoglobulin binding domain, is a modification of the B domain of Staphylococal Protein A (SPA). SPA is a natural protein that binds to various mammalian antibodies found in the cell wall of Staphylococcus aureus. Of the five domains that make up the SPA, the binding and stability of the antibody to the B domain is dominant. Targeted mutagenesis of Asn-Gly, the 28- to 29-position sensitive residues in the B domain, to Asn-Ala resulted in a more stable Z-domain that was tolerated by hydroxylammonium and hydrogen bromide Processing. The two Z domains, end-to-end connected, are named ZZ domains and have similar antibody binding capacity and stability to SPA, allowing them to withstand harsh environments in industrial purification. ZZ domain with its unique anti-3alpha helical structure, and unique antibody binding ability has been widely used in foreign expression of soluble protein and immune detection, antibody purification and other fields. This article reviews the mechanism of ZZ binding to antibodies and its application in various fields.