Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli.
Secretion to the periplasm of Escherichia coli enables production of many eukaryotic extracellular proteins in a soluble form. The complex disulphide bond arrangement of such proteins is probably a major factor in determining the low yield of correctly folded product observed in many cases. Here we show that co-expression of human protein disulphide isomerase increased the yield of a monoclonal antibody Fab' fragment in the periplasm of E. coli.
Humphreys
D P
DP
School of Biological Sciences, University of Birmingham, UK.
Weir
N
N
Lawson
A
A
Mountain
A
A
Lund
P A
PA
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000096:biosynthesis*; D004926:Escherichia coli / Q000378:metabolism*; D015870:Gene Expression; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000096:biosynthesis*; D007535:Isomerases / Q000096:biosynthesis* / Q000737:chemistry; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry
D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D011993:Recombinant Fusion Proteins; D007535:Isomerases; D019704:Protein Disulfide-Isomerases