Characterization of bovine interferon α1: expression in yeast Pichia pastoris, biological activities, and physicochemical characteristics
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Updated: Apr 21, 2026

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Jianwei Shao1, Chong Cao, Jun Bao
11 College of Veterinary Medicine, Northeast Agricultural University , Harbin, China .
Abstract:
A bovine interferon α (BoIFNα) gene that included signal sequence was amplified from bovine liver genomic DNA. The gene was named BoIFN-α1 according to the position at which the encoded gene of the bovine IFN was located in the bovine genome. The sequence included a 23-amino-acid signal peptide and a 166-amino-acid mature peptide. The structural characteristics and phylogenetic relationships of the BoIFN-α1 gene were analyzed. A recombinant mature BoIFN-α1 (rBoIFN-α1) was expressed in the yeast Pichia pastoris. Physicochemical characteristics and antiviral activity were determined in vitro. Recombinant BoIFN-α1 was found to be highly sensitive to trypsin and stable at pH 2.0 or 65°C. It also exhibited antiviral activity, which was neutralized by a rabbit anti-rBoIFNα polyclonal antibody. This study revealed that rBoIFN-α1 has the typical characteristics of IFNα and can be used for both research and industrial application.
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