Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli

FEBS Lett. 1996 Feb 12;380(1-2):194-7. doi: 10.1016/0014-5793(96)00028-2.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal / biosynthesis*
  • Escherichia coli / metabolism*
  • Gene Expression
  • Humans
  • Immunoglobulin Fab Fragments / biosynthesis*
  • Isomerases / biosynthesis*
  • Isomerases / chemistry
  • Molecular Sequence Data
  • Protein Disulfide-Isomerases
  • Protein Folding
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / chemistry

Substances

  • Antibodies, Monoclonal
  • Immunoglobulin Fab Fragments
  • Recombinant Fusion Proteins
  • Isomerases
  • Protein Disulfide-Isomerases