Expression of Recombinant Antibodies

Frenzel, André; Hust, Michael; Schirrmann, Thomas

These new antibody generation technologies have increased the amount of antibodies for different applications and, therefore, also the need of efficient production systems. Immunoglobulin G (IgG) is a heterotetrameric molecule consisting of two heavy and two light chains, respectively, which are connected via disulfide bonds. Heavy and light chains (HC and LC) also contain intramolecular disulfide bonds for stabilization (23). These structural properties require a sophisticated folding apparatus as well as an oxidizing environment for the generation of disulfide bonds. Consequently, many traditionally expression hosts do not provide these mechanisms for efficient production of IgGs. Therefore, smaller antibody fragments have been developed which combine easier production with full antigen binding capacity of an IgG (Figure 1 ). In addition, the development of smaller fragments was the basis for most of the in vitro antibody generation systems (18-22). These antibody fragments can be used for applications, where epitope binding is sufficient for the desired effect including therapeutic applications such as virus neutralization or receptor blocking.