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Successive remodeling of IgG glycans using a solid-phase enzymatic platform
Yen-Pang Hsu1,2, Deeptak Verma3, Shuwen Sun1
1Analytical Research and Development, Merck & Co., Inc, Rahway, NJ, 07065, USA.
Communications Biology
|April 8, 2022
Summary
Glycoengineering controls therapeutic glycoprotein structures for enhanced safety and efficacy. This study harmonizes immunoglobulin G (IgG) glycans using enzymatic remodeling, improving drug quality and biocompatibility.
Area of Science:
- Biochemistry
- Glycobiology
- Pharmaceutical Sciences
Background:
- Therapeutic glycoproteins are widely used but exhibit glycan heterogeneity.
- Controlling glycosylation can improve drug safety, efficacy, and bioavailability.
- Enzymatic glycan remodeling offers a strategy for constructing defined glycan structures.
Purpose of the Study:
- To quantitatively evaluate enzymes for glycoengineering immunoglobulin G (IgG).
- To develop a solid-phase platform for successive glycan remodeling.
- To harmonize IgG glycans into specific N-glycoforms.
Main Methods:
- Screening over 30 glycoengineering enzymes.
- Utilizing a solid-phase platform for sequential enzymatic reactions.
- Characterizing remodeled IgG N-glycans.
Main Results:
- Demonstrated successful successive glycan remodeling on immobilized IgG.
- Achieved harmonization of IgG glycans into defined complex-type N-glycoforms.
- Obtained high yield and efficiency in glycan modification while preserving IgG binding affinity.
Conclusions:
- Enzymatic glycan remodeling is an effective strategy for controlling glycoprotein structures.
- The developed solid-phase platform enables efficient IgG glycan harmonization.
- This approach has potential for improving the quality and therapeutic potential of glycoprotein drugs.
