[Expression, purification and antiviral activities of a new recombinant human interferon-lambda2]

Area of Science:

• Biotechnology
• Molecular Biology
• Immunology

Background:

• Interferons are crucial cytokines in the innate immune response.
• Human interferon lambda2 (IFN-λ2) has shown therapeutic potential but requires efficient expression systems.
• Understanding IFN-λ2's properties, including species specificity, is vital for its clinical application.

Purpose of the Study:

• To develop a method for expressing recombinant human interferon lambda2 (IFN-λ2) in Escherichia coli (E. coli).
• To characterize the antiviral activities and species specificity of the expressed IFN-λ2.
• To compare the anti-hepatitis B virus (anti-HBV) activity of IFN-λ2 with interferon-alpha2b (IFN-α2b).

Main Methods:

• Optimized human IFN-λ2 gene synthesis based on E. coli codon preference.
• Cloning into the pBV220 expression vector and transformation into E. coli DH5α.
• Purification using CM FF and size exclusion chromatography, followed by antiviral assays.

Main Results:

• High-level expression of IFN-λ2, constituting approximately 15% of total E. coli protein.
• Achieved ~90% purity of the recombinant protein with a specific antiviral activity of 1.5 x 10^6 IU/mg.
• Demonstrated stringent species specificity, with higher activity on primate-origin cells, and comparable anti-HBV activity to IFN-α2b.

Conclusions:

• Successful expression of functional recombinant human IFN-λ2 in E. coli.
• The expressed IFN-λ2 exhibits notable species specificity and comparable anti-HBV efficacy to IFN-α2b.
• This study provides a foundation for further investigation and therapeutic development of IFN-λ2.