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Commonly used fusion techniques — electroporation,...
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Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells
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Glycan Remodeling Technologies for Enhancing Antibody Function.

Shino Manabe1,2, Methanee Hiranyakorn3

  • 1Hoshi University, Tokyo, Japan. s-manabe@hoshi.ac.jp.

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|March 31, 2026
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Summary
This summary is machine-generated.

Antibody N-linked glycans critically impact drug efficacy and safety. Glycan remodeling technologies offer a path to producing homogeneous glycoforms, enhancing therapeutic antibody functionality and consistency for improved drug development.

Keywords:
Antibody dependent cellular cytotoxicity (ADCC)Antibody-drug conjugate (ADC)Endo-β-N-acetylglucosaminidase (ENGase)N-glycan

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Area of Science:

  • Biopharmaceutical development
  • Glycobiology
  • Protein engineering

Background:

  • Therapeutic antibodies, primarily Immunoglobulin G (IgG), are a major class of medicines.
  • N-linked glycans in the IgG Fc domain significantly influence functions like antibody-dependent cellular cytotoxicity (ADCC) and pharmacokinetics.
  • Glycan heterogeneity leads to batch-to-batch variations, affecting antibody efficacy and safety.

Purpose of the Study:

  • To review advancements in profiling N-linked glycans for antibody drug development.
  • To discuss glycan remodeling technologies for optimizing IgG functionality.
  • To highlight the importance of homogeneous glycoforms in antibody therapeutics.

Main Methods:

  • Review of recent advancements in mass spectrometry and chromatography for glycan analysis.
  • Discussion of various glycan remodeling strategies.
  • Analysis of applications in antibody drug development, quality control, and biosimilar production.

Main Results:

  • Advanced analytical techniques enable more precise structural analysis of N-linked glycans.
  • Glycan profiling is essential for predicting and improving antibody function.
  • Homogeneous glycoforms are key to enhancing IgG functionality.

Conclusions:

  • Glycan remodeling technologies are crucial for producing consistent and effective therapeutic antibodies.
  • Optimizing IgG glycoforms can improve antibody efficacy, safety, and pharmacokinetic properties.
  • Further development in glycan engineering holds significant promise for biopharmaceutical innovation.