Recombinant Protein Expression in Escherichia coli (E.coli): What We Need to Know

被引:86
作者
Hayat, Seyed Mohammad Gheibi [1 ]
Farahani, Najmeh [2 ]
Golichenari, Behrouz [3 ]
Sahebkar, Amirhossein [4 ,5 ,6 ]
机构
[1] Shahid Sadoughi Univ Med Sci, Sch Med, Dept Genet, Yazd, Iran
[2] Isfahan Univ Med Sci, Dept Genet & Mol Biol, Esfahan, Iran
[3] Mashhad Univ Med Sci, Sch Pharm, Dept Pharmaceut Biotechnol, Mashhad, Iran
[4] Mashhad Univ Med Sci, Neurogen Inflammat Res Ctr, Mashhad, Iran
[5] Mashhad Univ Med Sci, Pharmaceut Technol Inst, Biotechnol Res Ctr, Mashhad, Iran
[6] Mashhad Univ Med Sci, Sch Pharm, Mashhad, Iran
关键词
Escherichia coli; cloning; recombinant protein; vector; host; genome; TERMINAL HALF; RNASE E; FUSION; VECTORS; PURIFICATION; OVEREXPRESSION; STRATEGIES; STABILITY; BL21;
D O I
10.2174/1381612824666180131121940
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Background: Host, vector, and culture conditions (including cultivation media) are considered among the three main elements contributing to a successful production of recombinant proteins. Accordingly, one of the most common hosts to produce recombinant therapeutic proteins is Escherichia coli. Methodology: A comprehensive literature review was performed to identify important factors affecting production of recombinant proteins in Escherichia coli. Results: Escherichia coli is taken into account as the easiest, quickest, and cheapest host with a fully known genome. Thus, numerous modifications have been carried out on Escherichia coli to optimize it as a good candidate for protein expression and; as a result, several engineered strains of Escherichia coli have been designed. In general; host strain, vector, and cultivation parameters are recognized as crucial ones determining success of recombinant protein expression in Escherichia coli. In this review, the role of host, vector, and culture conditions along with current pros and cons of different types of these factors leading to success of recombinant protein expression in Escherichia coli were discussed. Conclusion: Successful protein expression in Escherichia coli necessitates a broad knowledge about physicochemical properties of recombinant proteins, selection among common strains of Escherichia coli and vectors, as well as factors related to media including time, temperature, and inducer.
引用
收藏
页码:718 / 725
页数:8
相关论文
共 52 条
[1]   Recombinant protein expression in Escherichia coli [J].
Baneyx, F .
CURRENT OPINION IN BIOTECHNOLOGY, 1999, 10 (05) :411-421
[2]   The complete genome sequence of Escherichia coli K-12 [J].
Blattner, FR ;
Plunkett, G ;
Bloch, CA ;
Perna, NT ;
Burland, V ;
Riley, M ;
ColladoVides, J ;
Glasner, JD ;
Rode, CK ;
Mayhew, GF ;
Gregor, J ;
Davis, NW ;
Kirkpatrick, HA ;
Goeden, MA ;
Rose, DJ ;
Mau, B ;
Shao, Y .
SCIENCE, 1997, 277 (5331) :1453-+
[3]  
Cantrell Sally A, 2003, Methods Mol Biol, V235, P257
[4]  
Casali Nicola, 2003, Methods Mol Biol, V235, P27
[5]   An investigation into the pathogenic properties of Escherichia coli strains BLR, BL21, DH5α and EQ1 [J].
Chart, H ;
Smith, HR ;
La Ragione, RM ;
Woodward, MJ .
JOURNAL OF APPLIED MICROBIOLOGY, 2000, 89 (06) :1048-1058
[6]  
Constans A, 2002, SCIENTIST, V16, P37
[7]   VECTORS THAT FACILITATE THE EXPRESSION AND PURIFICATION OF FOREIGN PEPTIDES IN ESCHERICHIA-COLI BY FUSION TO MALTOSE-BINDING PROTEIN [J].
DIGUAN, C ;
LI, P ;
RIGGS, PD ;
INOUYE, H .
GENE, 1988, 67 (01) :21-30
[8]   The toxicity of recombinant proteins in Escherichia coli:: A comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3) [J].
Dumon-Seignovert, L ;
Cariot, G ;
Vuillard, L .
PROTEIN EXPRESSION AND PURIFICATION, 2004, 37 (01) :203-206
[9]  
Francis DM, 2010, CURR PROTOC PROTEIN, DOI DOI 10.1002/0471140864.PS0524S61
[10]   SOLUBILIZATION AND PURIFICATION OF ENZYMATICALLY ACTIVE GLUTATHIONE-S-TRANSFERASE (PGEX) FUSION PROTEINS [J].
FRANGIONI, JV ;
NEEL, BG .
ANALYTICAL BIOCHEMISTRY, 1993, 210 (01) :179-187