EspA is a novel fusion partner for expression of foreign proteins in Escherichia coli

Cheng, Yan; Gu, Jiang; Wang, Hai guang; Yu, Seung Do; Liu, Yan qing; Ning, Ya; Zou, Q.; Yu, Xue Jie; Mao, Xuefeng

doi:10.1016/j.jbiotec.2010.09.940

Cited by 10 publications

(2 citation statements)

References 41 publications

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“…Despite the fact that, many fusion proteins were evaluated, it remains difficult to define a “universal fusion protein.” Different options are commercially available (MBP, GST, Trx, DsbC, NusA, etc), and several groups have found new proteins that can be promising alternatives to obtain a soluble and homogeneous recombinant protein (Chatterjee and Esposito, 2006; DelProposto et al, 2009; Cheng et al, 2010; Song et al, 2011) by fusing the target gene. In this work, we evaluated the use of a novel fusion protein, CelDnc that is thermostable (Tm: 71.4°C) and is expressed in massive amounts in E coli system.…”

Section: Discussionmentioning

confidence: 99%

Generation of a vector suite for protein solubility screening

et al. 2014

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Recombinant protein expression has become an invaluable tool for academic and biotechnological projects. With the use of high-throughput screening technologies for soluble protein production, uncountable target proteins have been produced in a soluble and homogeneous state enabling the realization of further studies. Evaluation of hundreds conditions requires the use of high-throughput cloning and screening methods. Here we describe a new versatile vector suite dedicated to the expression improvement of recombinant proteins (RP) with solubility problems. This vector suite allows the parallel cloning of the same PCR product into the 12 different expression vectors evaluating protein expression under different promoter strength, different fusion tags as well as different solubility enhancer proteins. Additionally, we propose the use of a new fusion protein which appears to be a useful solubility enhancer. Above all we propose in this work an economic and useful vector suite to fast track the solubility of different RP. We also propose a new solubility enhancer protein that can be included in the evaluation of the expression of RP that are insoluble in classical expression conditions.

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Section: Discussionmentioning

confidence: 99%

Generation of a vector suite for protein solubility screening

et al. 2014

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“…Linear B-cell and discontinuous B-cell epitopes of chimeric construct were predicted using Bcepred server (http://www.imtech.res.in/raghava/bcepred/) and Ellipro server (http://tools.immuneepitope.org/tools/ElliPro). The different segments were fused together using the appropriate ɑ-helix producing linkers [4,26]; the 6 histidine tag and ochre stop codon (TAA) sequences were added to the C-terminal of the chimeric gene (Fig. 1A).…”

Section: Genetic Engineering and Generating Expression Constructmentioning

confidence: 99%

Immunogenic properties of trivalent recombinant protein composed of B-subunits of LT, STX-2, and CT toxins

Kazemi

Akhavian

Amani

et al. 2016

Microbes and Infection

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Infectious diarrhoea remains an emerging problem in the world health program. Among diarrheagenic agents, Vibrio cholerae and enterotoxigenic and enterohemorrhagic Escherichia coli are critical enteropathogens. AB5 toxin produced by these bacteria, heat-labile enterotoxin (LT), cholera enterotoxin (CT), and shiga-like cytotoxin (STX) can target the immune system and are subunit vaccine candidates. A chemically-synthesized chimeric construct composed of the binding subunits of these toxins (LTB, STXB, and CTXB) was developed based on bioinformatics studies. The whole chimeric protein (rLSC) and each of the segments (rLTB, rSTXB, and rCTXB) were expressed in a prokaryotic expression system (E. coli), purified, and analysed for their immunogenic properties. The results indicate that these recombinant proteins were effectively able to present appropriate epitopes to an animal model of the immune system which could result in and increase IgG in serum and immune responses that protect against the binding activity of these toxins. The immunological assays revealed that the sera of immunized mice prevented toxins from binding to their specific receptors and neutralized their toxic effects. The proposed construct should be considered as a potent immunogen to prevent toxicity and diarrhoea.

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The NT11, a novel fusion tag for enhancing protein expression in Escherichia coli

Nguyen

Son

et al. 2019

Appl Microbiol Biotechnol

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EspA is a novel fusion partner for expression of foreign proteins in Escherichia coli

Cited by 10 publications

References 41 publications

Generation of a vector suite for protein solubility screening

Generation of a vector suite for protein solubility screening

Immunogenic properties of trivalent recombinant protein composed of B-subunits of LT, STX-2, and CT toxins

The NT11, a novel fusion tag for enhancing protein expression in Escherichia coli

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