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Use of High-Throughput Automated Microbioreactor System for Production of Model IgG1 in CHO Cells
Published on: September 28, 2018
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Glycoengineering design options for IgG1 in CHO cells using precise gene editing.
Morten A Schulz1, Weihua Tian1, Yang Mao1
1Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, Copenhagen N, Denmark.
Glycobiology
|March 30, 2018
Summary
Precise gene editing enables stable engineering of host cells for therapeutic glycoprotein production. This study demonstrates novel glycoform designs for human IgG1 antibodies, optimizing glycosylation for therapeutic applications.
Area of Science:
- Biotechnology and genetic engineering
- Glycobiology and therapeutic protein development
- Mammalian cell line engineering
Background:
- Glycosylation of therapeutic glycoproteins significantly impacts product quality, pharmacokinetics, and bioactivity.
- Specific glycan structures, such as core fucosylation on IgG1 antibodies, modulate effector functions.
- Controlling N-glycan structures is crucial for consistent and effective biologic drug development.
Purpose of the Study:
- To explore precise gene engineering strategies for controlling N-glycan structures on human IgG1 antibodies.
- To develop stable cell lines producing recombinant antibodies with defined and homogenous glycoforms.
- To assess the feasibility of engineering specific glycoforms, including sialylation and fucosylation patterns.
Main Methods:
- Utilized precise gene editing techniques to engineer Chinese hamster ovary (CHO) cells for recombinant protein production.
- Focused on modifying N-glycosylation pathways to achieve specific glycan structures on human IgG1.
- Developed and validated methods for producing homogenous biantennary and monoantennary N-glycans with controlled sialylation and fucosylation.
Main Results:
- Successfully engineered stable cell lines producing homogenous biantennary N-glycans with and without galactose (G0F, G2F).
- Achieved stable production of α2,6-linked monosialylated glycoforms (G2FS1) and a novel monoantennary glycoform with complete sialic acid capping.
- Demonstrated the ability to engineer glycoforms both with and without core α1,6-fucose.
- Observed limitations in generating substantial disialylated glycoforms.
Conclusions:
- Precise gene engineering offers robust options for creating diverse and defined N-glycoforms on human IgG1 antibodies.
- Engineered glycoforms, including specific sialylation and fucosylation patterns, can be stably produced for therapeutic applications.
- These advancements enable the selection of optimal glycoforms to enhance antibody efficacy and therapeutic profiles.
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