Skerra A
Max-Planck-Institut für Biophysik, Frankfurt am Main, Germany.
Curr Opin Immunol. 1993 Apr;5(2):256-62. doi: 10.1016/0952-7915(93)90014-j.
The expression of Ig fragments in Escherichia coli permits rapid access to engineered molecules with antigen-binding properties. While the expression in a functional state by secretion to the periplasm is the standard method for the production of Fv and Fab fragments, single chain Fv fragments are mainly produced by refolding from insoluble aggregates. Although all of these Ig fragments serve as valuable aids in the study of antigen binding, their different biochemical properties must be considered when using them as research tools or for medical applications. In addition to these simple univalent antibody fragments, the bacterial expression of bivalent and bispecific versions and of hybrid proteins with novel effector functions is gaining increasing importance.
免疫球蛋白片段在大肠杆菌中的表达使得能够快速获得具有抗原结合特性的工程分子。虽然通过分泌到周质以功能状态表达是生产Fv和Fab片段的标准方法,但单链Fv片段主要通过从不溶性聚集体中重折叠产生。尽管所有这些免疫球蛋白片段在抗原结合研究中都是有价值的辅助工具,但在将它们用作研究工具或用于医学应用时,必须考虑它们不同的生化特性。除了这些简单的单价抗体片段外,二价和双特异性版本以及具有新型效应功能的杂合蛋白的细菌表达正变得越来越重要。