Expression and characterization of recombinant humanized anti-HER2 single-chain antibody in Pichia pastoris for targeted cancer therapy

Xiaodan Cao; Haijun Yu; Chao Chen; Jia Wei; Ping Wang

doi:10.1007/s10529-015-1804-6

Expression and characterization of recombinant humanized anti-HER2 single-chain antibody in Pichia pastoris for targeted cancer therapy

Xiaodan Cao, Haijun Yu, Chao Chen, Jia Wei, Ping Wang

Bioproducts and Biosystems Engineering

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1347-1354
Number of pages	8
Journal	Biotechnology Letters
Volume	37
Issue number	7
DOIs	https://doi.org/10.1007/s10529-015-1804-6
State	Published - Jul 5 2015

Keywords

Anti-HER2
Breast cancer cell line SKBR3
Cancer therapy
Heterogeneous expression
Humanized single-chain variable fragment
Pichia pastoris

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title = "Expression and characterization of recombinant humanized anti-HER2 single-chain antibody in Pichia pastoris for targeted cancer therapy",

abstract = "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.",

keywords = "Anti-HER2, Breast cancer cell line SKBR3, Cancer therapy, Heterogeneous expression, Humanized single-chain variable fragment, Pichia pastoris",

author = "Xiaodan Cao and Haijun Yu and Chao Chen and Jia Wei and Ping Wang",

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T1 - Expression and characterization of recombinant humanized anti-HER2 single-chain antibody in Pichia pastoris for targeted cancer therapy

AU - Cao, Xiaodan

AU - Yu, Haijun

AU - Chen, Chao

AU - Wei, Jia

AU - Wang, Ping

PY - 2015/7/5

Y1 - 2015/7/5

N2 - 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.

AB - 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.

KW - Anti-HER2

KW - Breast cancer cell line SKBR3

KW - Cancer therapy

KW - Heterogeneous expression

KW - Humanized single-chain variable fragment

KW - Pichia pastoris

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