Effect of aberrant disulfide bond formation on protein conformation and molecular property of recombinant therapeutics

Abstract

As a comparative study, the extracytoplasmic domain of human CD83 (hCD83ext) was expressed as a glutathione-S-transferase (GST) fusion in two Escherichia coli B strains, i.e., BL21 and Origami B, respectively, with a reductive and oxidative cytoplasm. The final therapeutic products of hCD83ext produced by the two expression hosts exhibited significant differences in protein conformation and molecular property, which presumably resulted from different disulfide patterns. The study highlights the importance of developing proper host/vector systems and biomanufacturing conditions for the production of recombinant therapeutic proteins with a consistent product quality. © 2010 IUPAC.