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二氫葉酸還原脢之微型核糖核酸30干擾對CHO細胞表現嵌合型抗體之研究
Thesis

二氫葉酸還原脢之微型核糖核酸30干擾對CHO細胞表現嵌合型抗體之研究

Zheng, Hong Yu
Masters, 國立清華大學, 生物科技研究所
2008

Abstract

中國倉鼠卵巢細胞 二氫葉酸還原脢 嵌合型抗體 Chinese hamster ovary CHO dihydrofolate reductase dhfr chimeric antibody
Chinese hamster ovary cells (CHO) and dihydrofolate reductase (dhfr)/methotrexate (MTX) gene amplification system are commonly used to generate stable high-producer CHO cell clones in biopharmaceutical industries, such as antibodies, at the present time. Most biopharmaceutical antibody-based products display favorable safety profiles such as chimeric or humanized antibodies. Simulation of bio-pharmaceutical industrial process for antibody production, the expression system using CHO/dhfr- cell as a host cell to express anti-Japanese encephalitis virus (JEV) neutralizing chimeric antibody IgG1-2H2 and IgG1-E3.3. The silencing shRNA vector psd2, which was previously demonstrated the most effective in silencing dhfr RNA transcripts, improved antibody production in dhfr-deficient CHO (CHO/dhfr-¬) cells through dhfr/MTX gene amplification. Initially, a chimeric mouse-human antibody expression vector was used to express JEV neutralizing chimeric antibodies, IgG1-2H2 and IgG1-E3.3. Then, in addition to psd2, other silencing vectors that were mir-30 based sd2 silencing vector (pmir-30 sd2) and nonspecific of dhfr gene silencing vector (pscramble) were adopted to improve IgG1-2H2 expression in CHO/dhfr- cells. Compare to the average expression level of IgG1-2H2 of CHO/dhfr stable clones, the clones with the silencing vectors pMir-30 sd2 and psd2 were about 100% higher than that with pscramble silencing vector and without silencing vector. Higher level of IgG expression and more stable productivity in MTX-free medium was achieved in amplified stable clones containing psd2 or pMir30-sd2. The method proposed here can be applied to screen high producer cell clones for recombinant antibody or other biologics expression in CHO/dhfr- cells with efficient stable transfection. It can be beneficial for the production of recombinant protein therapeutics in bio-industry.

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