Strategies for the production of soluble human alphainterferons in Escherichia coli: expression, purification, and characterization

Abstract

Escherichia coli has been the favorite expression host for the last decades when it comes to simple recombinant proteins used as biopharmaceuticals. This organism is well-characterized and able to deliver enormous amounts of heterologous polypeptides, especially when no complex post-translational modifications are needed, such as the case of alphainterferons, which are small cytokines used against viral infections and tumors. One major disadvantage of bacterial systems is that target molecules are commonly synthesized as insoluble and inactive inclusion bodies in the cytoplasm, bringing up the need for laborious and expensive steps of solubilization and renaturation before the product may be purified. Here we review past experiences, advances, and gaps that may represent future opportunities to deliver interferon-α in its soluble and functional form, including optimization of culture conditions, use of engineered strains, and solubility fusion partners, among others.