Expression of correctly folded proteins in Escherichia coli

The kinetics and protection of the antiviral state induced by recombinant iIFN1a in rainbow trout against infectious hematopoietic necrosis virus

“…In this study, the recombinant iIFN1a was mostly expressed in the inclusion bodies even after several attempts for soluble expression. This type of expression may be associated with the high level of expression observed and the lack of glycosylation (Georgiou and Valax, 1996). Additionally, the unglycosylated iIFN1a also possessed significant antiviral properties both in vitro and in vivo.…”

Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli

“…Goloubinoff et al, 1989;Blum et al, 1992;Georgiou and Valax, 1996;Nishihara et al, 1998;Baneyx and Palumbo, 2002). Although the substrate specificity of these chaperone systems 10 has been characterized and an enormous progress in understanding chaperone mediated protein folding processes has been achieved, the success of chaperone coproduction on increasing soluble protein accumulation is still a trial-and-error process and cannot be predicted from properties of the recombinant protein (Hoffmann and Rinas, 2004;Baneyx and Mujacic, 2004;Ventura and Villaverde, 2006).…”

Overproduction of Bacterial Protein Disulfide Isomerase (DsbC) and Its Modulator (DsbD) Markedly Enhances Periplasmic Production of Human Nerve Growth Factor in Escherichia coli

“…The periplasm of Escherichia coli contains enzymes that can assist protein folding such as Dsb (disulfide bond formation) proteins (1)(2)(3)(4)(5)(6), like endoplasmic reticulum of eukaryotes, and can provide an oxidative environment potentially useful for production of heterologous secretory proteins (e.g. eukaryotic cytokines and peptide hormones) that have a number of disulfide bonds (1,7).…”