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Updated: Jul 12, 2026
Laboratory Scale Production and Purification of a Therapeutic Antibody
Published on: January 24, 2017
Antibody therapeutics: isotype and glycoform selection
1University of Birmingham, Division of Immunity & Infection, The School of Medicine, Edgbaston, Birmingham B15 2TT, UK. R.Jefferis@bham.ac.uk
Choosing the right recombinant monoclonal antibody (rMAb) isotype is crucial for therapeutic success. Optimizing antibody structure, like non-fucosylated IgG1 or aglycosylated IgG2, can enhance or minimize effector functions for specific diseases.
Area of Science:
- Immunology
- Biotechnology
- Pharmacology
Background:
- Recombinant monoclonal antibody (rMAb) therapy offers two main strategies: cell killing or molecule neutralization.
- The selection of an appropriate rMAb isotype is critical for determining in vivo biological activities.
- Predicting in vivo antibody activity is complex due to numerous influencing factors like IgG subclass and Fc receptor polymorphisms.
Purpose of the Study:
- To explore the impact of antibody structure on effector functions.
- To guide the selection of optimal antibody formats for specific therapeutic indications.
Main Methods:
- Analysis of molecular interactions between IgG-Fc and effector ligands in vitro.
- Engineering novel antibody structures with modified effector function profiles.
Main Results:
- Non-fucosylated IgG1 formats are optimal for maximal antibody-dependent cell-mediated cytotoxicity (ADCC).
- Aglycosylated IgG2 formats are suitable for applications requiring minimal effector activity.
Conclusions:
- Tailoring antibody structure, specifically Fc-glycoforms, allows for precise control of effector functions.
- Optimized antibody formats can improve therapeutic outcomes in various disease indications.
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