Increased antiviral activity of microscale‐purified Hu IFN α8 (human interferon α8) over Hu IFN α2b in Hep‐2 cells challenged with Mengo virus

Human proteins are not routinely expressed at high levels in Escherichia coli for, among other reasons, different codon usage. Several purification procedures have been applied to recover recombinant proteins for further biological characterization. However, the vast majority involve costly chromatography procedures. In the present study, both Hu IFN α2b (human interferon α2b) and Hu IFN α8 were expressed efficiently in E. coli BL21‐codonplus‐RIL. Subsequently, both recombinant proteins were purified to homogeneity by passive elution from reverse‐stained SDS/PAGE gels, a cost‐effective purification procedure. After purification, both recovered proteins were biologically active. The Hu IFN α8 subtype induced 1.46‐fold more antiviral activity than Hu IFN α2b using Hep‐2 human laryngeal carcinoma cell challenged with Mengo virus.