Expression of mammalian proteins for diagnostics and therapeutics: a review

Abstract

Background: Antibodies have proven to be remarkably successful for biomedical applications. They play important roles in epidemiology and medicine from diagnostics of diseases to therapeutics, treating diseases from incessant chronic diseases such as rheumatology to pandemic outbreaks. With no end in sight for the demand for antibody products, optimizations and new techniques must be expanded to accommodate this.

Methods and results: This review discusses optimizations and techniques for antibody production through choice of discovery platforms, expression systems, cell culture mediums, and other strategies to increase expression yield. Each system has its own merits and demerits, and the strategy chosen is critical in addressing various biological aspects.

Conclusions: There is still insufficient evidence to validate the efficacy of some of these techniques, and further research is needed to consolidate these industrial production systems. There is no doubt that more strategies, systems, and pipelines will contribute to enhance biopharmaceutical production.

Keywords: Antibody; Antibody diagnostic; Antibody therapeutic.

Fig. 1

Schematic structure of a human IgG1 antibody. IgG consists of two heavy and two light chains. The variable domains are variable light (VL) and variable heavy (VH), which forms the antigen binding site. The constant domains are CL (constant light) and CH1–3 (constant heavy). IgG can be furthermore divided into Fab (fragment antigen binding) which consists of Fv (fragment variable) and Fc (fragment crystallizable) which induce effector functions

Fig. 2

Crystal structure of human IgG1-Fc. Image from the RCSB PDB (rcsb.org) of PBD ID 5JII [53]