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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Expression, purification and characterization of human IFN-lambda1 in Pichia pastoris
Yun Fei Xie1, Hong Chen, Bing Ren Huang
1National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College, 5 Dong Dan San Tiao Street, Beijing, 100005, China.
Journal of Biotechnology
|March 14, 2007
Summary
Recombinant human interferon-lambda 1 (rhIFN-lambda1) was successfully produced in Pichia pastoris. This novel expression system yielded glycosylated rhIFN-lambda1 with antiviral activity comparable to commercial interferon alpha2a.
Area of Science:
- Biotechnology
- Immunology
- Molecular Biology
Background:
- Interferon-lambda (IFN-lambda) is a class II cytokine with antiviral properties.
- Understanding its production is crucial for therapeutic applications.
Purpose of the Study:
- To produce recombinant human IFN-lambda1 (rhIFN-lambda1) using the Pichia pastoris expression system.
- To characterize the secreted rhIFN-lambda1 and assess its biological activity.
Main Methods:
- Cloning and expression of human IFN-lambda1 cDNA in Pichia pastoris.
- Utilizing the yeast integrative vector pAO815 for constructing expression plasmids.
- Purification of rhIFN-lambda1 using cation exchange chromatography and gel filtration.
Main Results:
- Two forms of mature, glycosylated rhIFN-lambda1 were secreted by the GS115/IFNlambda1G strain.
- A yield of approximately 65 mg/L of low-glycosylated rhIFN-lambda1 was achieved.
- Purified rhIFN-lambda1 demonstrated STAT1 and STAT2 activation comparable to IFNalpha2a.
Conclusions:
- Pichia pastoris is an effective system for producing biologically active rhIFN-lambda1.
- The produced rhIFN-lambda1 exhibits potent antiviral signaling capabilities.
- This study provides a foundation for the large-scale production of IFN-lambda for therapeutic use.
