Escherichia coli as a glycoprotein production host: recent developments and challenges.
Escherichia coli as a glycoprotein production host: recent developments and challenges.
复制标题
DOI：
10.1016/j.copbio.2014.07.006
复制
发表时间：
2014-12
影响因子：
7.7
通讯作者：
Stephen R P Jaffé;Benjamin Strutton;Zdenko Levarski;J. Pandhal;P. Wright
中科院分区：
文献类型：
--
作者：
Stephen R P Jaffé;Benjamin Strutton;Zdenko Levarski;J. Pandhal;P. Wright
重点介绍了E.大肠杆菌中的糖基化酶，提高糖基化效率。中国人卵巢细胞是大规模生产人类治疗性糖蛋白的最受欢迎的宿主表达系统，但是，工程大肠杆菌进行糖基化的竞赛正在加快步伐。2002年，空肠弯曲菌的N-糖基化途径成功地转移到大肠杆菌中，可以被认为是关键的第一个工程步骤。本文就重组治疗蛋白在大肠杆菌中N-糖基化的研究进展作一综述。大肠杆菌细胞，从聚糖组成的操纵，以提高糖基化效率，沿着的挑战，仍然存在之前的E.大肠杆菌可用作经济上可行的糖蛋白生产的工业宿主细胞。
HighlightsGlycosylation of therapeutic proteins in E. coli.Increasing the efficiency of glycosylation.Producing the eukaryotic glycan within E. coli.Targeting glycans towards a eukaryotic consensus sequence.Quantifying glycoproteins.Chinese Hamster Ovary cells are the most popular host expression system for the large-scale production of human therapeutic glycoproteins, but, the race to engineer Escherichia coli to perform glycosylation is gathering pace. The successful functional transfer of an N-glycosylation pathway from Campylobacter jejuni to Escherichia coli in 2002 can be considered as the crucial first engineering step. Here, we discuss the recent advancements in the field of N-glycosylation of recombinant therapeutic proteins in E. coli cells, from the manipulation of glycan composition, to the improvement in glycosylation efficiency, along with the challenges that remain before E. coli can be available as an industry host cell for economically viable glycoprotein production.