Albumin fusion of interleukin-28B: production and characterization of its biological activities and protein stability.

TitleAlbumin fusion of interleukin-28B: production and characterization of its biological activities and protein stability.
Publication TypeJournal Article
Year of Publication2013
AuthorsZhao J, Si Y, Cheng M, Yang Y, Niu Y, Li X, Liu X, Yang W
JournalPloS one
Volume8
Issue5
Paginatione64301
Date Published2013
Abstract

The cytokine interleukin-28B (IL-28B) has potential antiviral properties and regulatory roles in adaptive cellular immunity. A genome-wide association study identified a single nucleotide polymorphism near the IL-28B gene that strongly predicts response to hepatitis C treatment with interferon and ribavirin. In this study, we produced human serum albumin (HSA) fused to interleukin-28B (HSA-IL28B) in an attempt to determine the effects of albumin fusion on anti-Hepatitis C virus (HCV) activity and protein stability. HSA-IL28B was expressed at high levels in the yeast expression system we used and was easily purified. The biological activities of IL-28B were only retained when HSA was fused at the N-terminus. Compared with the native IL-28B, HSA-IL28B showed improved protein stability. HSA-IL28B inhibited HCV infection through the membrane receptors IL28R1 and IL10R2. Additionally, we demonstrated that HSA-IL28B was able to induce interferon-stimulated genes, phosphorylate intracellular STAT1, and act in restricted cell types. Our findings highlight the potential clinical applications of the fusion protein during virus infection and for immune regulation.

DOI10.1371/journal.pone.0075620
Alternate JournalPLoS ONE