ArticleApplied and environmental microbiology2001
Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins.
Article in Applied and environmental microbiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 59 citations in OpenAlex.
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- Reducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli.Microbial cell factories · 2011Article
- Expression of active recombinant human tissue-type plasminogen activator by using in vivo polyhydroxybutyrate granule display.Applied and environmental microbiology · 2010Article
- Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Microbial cell factories · 2009Article
- Use of folding modulators to improve heterologous protein production in Escherichia coli.Microbial cell factories · 2009Article
- Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli.Applied and environmental microbiology · 2005Article
- Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins.Microbial cell factories · 2004Article
- Studies of single-chain antibody expression in quiescent Escherichia coli.Applied and environmental microbiology · 2004Article
- Ability of Lactococcus lactis to export viral capsid antigens: a crucial step for development of live vaccines.Applied and environmental microbiology · 2003Article
- Structural and Functional Characterization of Recombinant Interleukin-10 from Indian Major CarpJournal of immunology researchArticle
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Attempts were made to engineer the periplasm of Escherichia coli to an expression compartment of heterologous proteins in their native conformation. As a first approach the low-molecular-size additive L-arginine and the redox compound glutathione (GSH) were added to the culture medium. Addition of 0.4 M L-arginine and 5 mM reduced GSH increased the yield of a native tissue-type plasminogen activator variant (rPA), consisting of the kringle-2 and the protease domain, and a single-chain antibody fragment (scFv) up to 10- and 37-fold, respectively. A variety of other medium additives also had positive effects on the yield of rPA. In a second set of experiments, the effects of cosecreted ATP-independent molecular chaperones on the yields of native therapeutic proteins were investigated. At optimized conditions, cosecretion of E. coli DnaJ or murine Hsp25 increased the yield of native rPA by a factor of 170 and 125, respectively. Cosecretion of DnaJ also dramatically increased the amount of a second model protein, native proinsulin, in the periplasm. The results of this study are anticipated to initiate a series of new approaches to increase the yields of native, disulfide-bridged, recombinant proteins in the periplasm of E. coli.
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