Select what you need: A comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes

Yin, Jun; Li, Guangxing; Ren, Xiaofeng; Herrler, Georg

doi:10.1016/j.jbiotec.2006.07.012

Cited by 305 publications

(204 citation statements)

References 115 publications

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“…To release recombinant proteins into the periplasm and the growth medium, many systems have been studied. As such a approach is complicated, the systems have not been commercialized [1,2,5] .…”

Section: Codon Usage/biasmentioning

confidence: 99%

Strategies for production of active eukaryotic proteins in bacterial expression system

Khow

Suntrarachun

2012

Asian Pacific Journal of Tropical Biomedicine

113

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Section: Codon Usage/biasmentioning

confidence: 99%

Strategies for production of active eukaryotic proteins in bacterial expression system

Khow

Suntrarachun

2012

Asian Pacific Journal of Tropical Biomedicine

113

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“…For this reason, a number of eukaryotic protein production systems have been developed (Aricescu et al, 2006;Yin et al, 2007). Plants and plant cells possess many advantages over other eukaryotic expression hosts, such as high biomass, ease of scaleup, cost effectiveness, and low risk of contamination (Ma et al, 2003;Twyman et al, 2003).…”

mentioning

confidence: 99%

Extremely High-Level and Rapid Transient Protein Production in Plants without the Use of Viral Replication

2008

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Plant-based overexpression of heterologous proteins has attracted much interest and development in recent years. To date, the most efficient vectors have been based on RNA virus-derived replicons. A system based on a disabled version of cowpea mosaic virus RNA-2 has been developed, which overcomes limitations on insert size and introduces biocontainment. This system involves positioning a gene of interest between the 5# leader sequence and 3# untranslated region (UTR) of RNA-2, thereby emulating a presumably stable mRNA for efficient translation. Thus far, the sequence of the 5# UTR has been preserved to maintain the ability of the modified RNA-2 to be replicated by RNA-1. However, high-level expression may be achieved in the absence of RNA-1-derived replication functions using Agrobacterium-mediated transient transformation. To investigate those features of the 5# UTR necessary for efficient expression, we have addressed the role of two AUG codons found within the 5# leader sequence upstream of the main initiation start site. Deletion of an in-frame start codon upstream of the main translation initiation site led to a massive increase in foreign protein accumulation. By 6 d postinfiltration, a number of unrelated proteins, including a full-size IgG and a self-assembling virus-like particle, were expressed to .10% and 20% of total extractable protein, respectively. Thus, this system provides an ideal vehicle for high-level expression that does not rely on viral replication of transcripts.

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“…at a density of 1×10 5 . The next day, the cells were fixed with 4% Paraformaldehyde in 0.1M Phosphate buffer for 10 minutes at room temperature.…”

Section: Confocal Microscopy On Fluorescent Cellsmentioning

confidence: 99%

“…Bacteria, given their cost-effectiveness and robustness, have been by far the most successful hosts for protein production to support biophysical studies, and strategies for the co-expression of genes in Escherichia coli are available [2,3]. Bacteria, and yeast or insect cells for that matter, might be poorly suited for the production of mammalian proteins [4,5]. These proteins may be toxic to the host, may require a better matched folding machinery, and may need post-translational modifications unavailable in the heterologous host.…”

Section: Introductionmentioning

confidence: 99%

Two-color selection for amplified co-production of proteins in mammalian cells

Assur

Schieren

Hendrickson

et al. 2007

Protein Expression and Purification

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Structural and functional analyses for many mammalian systems depend on having abundant supplies of recombinant multi-protein complexes that can be produced best, or only, in mammalian cells. We present an efficient fluorescence marking procedure for establishing stable cell lines that overexpress two proteins in co-ordination, and we validate the method in the production of monoclonal antibody Fab fragments. The procedure has worked without fail on all seven of seven trials on Fabs, which are being used in the crystallization of G-protein coupled receptors. This manner of efficient selection may readily be adapted for the co-production of other complexes of two or more proteins.

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Select what you need: A comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes

Cited by 305 publications

References 115 publications

Strategies for production of active eukaryotic proteins in bacterial expression system

Strategies for production of active eukaryotic proteins in bacterial expression system

Extremely High-Level and Rapid Transient Protein Production in Plants without the Use of Viral Replication

Two-color selection for amplified co-production of proteins in mammalian cells

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