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Updated: Apr 16, 2026
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Expression and characterization of recombinant humanized anti-HER2 single-chain antibody in Pichia pastoris for
Xiaodan Cao1, Haijun Yu, Chao Chen
1Biomedical Nanotechnology Center, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200237, People's Republic of China, xdcao@ecust.edu.cn.
Objectives:
The availability of self-targeting and low immunogenic therapeutic agents is critical to efficient cancer therapy. Therefore, the development of humanized therapeutic antibodies is particularly appealing.
Results:
A humanized single-chain variable fragment (scFv) antibody that can target human epidermal growth factor receptor-2 (HER2)-overexpressing cancer cells was designed and produced via expression in Pichia pastoris. The expression gave a high yield of 8 mg protein/l (with a purity of 92 %) using shake-flask cultures. Functional studies also revealed that the purified recombinant anti-HER2 scFv exhibited anti-proliferative activity and could bind efficiently to HER2-overexpressing human breast cancer cell line SKBR3.
Conclusion:
The recombinant scFv offers promising therapeutic and binding efficiencies that are desirable for targeted cancer therapies.
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