Recombinant protein expression in Escherichia coli: advances and challenges

被引：1659
作者：
Rosano, German L. [1 ,2 ]
Ceccarelli, Eduardo A. [1 ,2 ]
机构：
[1] Inst Biol Mol b& Celularde Rosario, Consejo Nacl Invest Cient & Tecn Esmeralda & Ocam, RA-2000 Rosario, Santa Fe, Argentina
[2] Univ Nacl Rosario, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Santa Fe, Argentina
来源：
FRONTIERS IN MICROBIOLOGY | 2014年 / 5卷
关键词：
recombinant protein expression; Escherichia coli; expression plasmid; inclusion bodies; affinity tags; E. coli expression strains; HIGH-LEVEL EXPRESSION; HIGH CELL-DENSITY; DISULFIDE BOND FORMATION; SYNONYMOUS CODON USAGE; PLASMID COPY NUMBER; L-ARABINOSE OPERON; FUSION PROTEINS; HETEROLOGOUS PROTEINS; INCLUSION-BODIES; GENE-EXPRESSION;
D O I：
10.3389/fmicb.2014.00172
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Escherichia coli is one of the organisms of choice for the production of recombinant proteins. Its use as a cell factory is well-established and it has become the most popular expression platform. For this reason, there are many molecular tools and protocols at hand for the high-level production of heterologous proteins, such as a vast catalog of expression plasmids, a great number of engineered strains and many cultivation strategies. We review the different approaches for the synthesis of recombinant proteins in E. coli and discuss recent progress in this ever-growing field.
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页数：17
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