No abstract

BACKGROUND: The bacterium Escherichia coli is a commonly used host for the production of recombinant protein biopharmaceutical products. One class of such molecules is antibody fragments, typified by the Crohn's disease and rheumatoid arthritis therapy Certolizumab pegol (Cimzia ® ). Antibody fragments generated in E. coli are often directed to the periplasm, so that disulphide bonding can occur and release can be simplified. However, many recombinant protein products are prone to misfolding and mislocalization. Here, we optimized the production of a Fab fragment, D1.3, and its release from the periplasm of E. coli using osmotic shock.