异源的
抗体
大肠杆菌
翻译(生物学)
生物
贪婪
拉伤
效应器
免疫原性
分子生物学
化学
生物化学
遗传学
信使核糖核酸
基因
解剖
作者
Conrad En Zuo Chan,Angeline Lim,Annie Hoi Yi Chan,Paul A. MacAry,Brendon J. Hanson
出处
期刊:PLOS ONE
[Public Library of Science]
日期:2010-04-20
卷期号:5 (4): e10261-e10261
被引量:24
标识
DOI:10.1371/journal.pone.0010261
摘要
Multi-polypeptide proteins such as antibodies are difficult to express in prokaryotic systems such as E. coli due to the complexity of protein folding plus secretion. Thus far, proprietary strains or fermenter cultures have been required for appreciable yields. Previous studies have shown that expression of heterologous proteins in E. coli can be enhanced by the reduction of protein translation rates. In this paper, we demonstrate that useful quantities of full-length IgG can be expressed and purified from the common E. coli laboratory strain HB2151 in standard shaking culture using a simple strategy of reduced inducer concentration combined with delayed induction times to modulate translation rates. Purified IgG had only marginally reduced avidity compared to mammalian derived IgG. This indicates that this technique can be used to derive antibodies of potentially equal utility as those expressed in mammalian cell culture, particularly for applications where effector functions mediated by the glycosylated residues in the Fragment Crystallizable (Fc) portion of the immunoglobulin are not required.
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