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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

6.8K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Related Experiment Video

Updated: Jun 13, 2025

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells
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Modulating antibody N-glycosylation through feed additives using a multi-tiered approach.

Jaka Kranjc1, Lovro Kramer2, Miha Mikelj3

  • 1Institute of Pharmacy, Faculty of Pharmacy, University of Ljubljana, Ljubljana, Slovenia.

Frontiers in Bioengineering and Biotechnology
|September 10, 2024
PubMed
Summary

This study identifies compounds that modulate N-glycosylation in recombinant protein production. These findings enable precise control over glycoform profiles for critical quality attributes in the pharmaceutical industry.

Keywords:
Chinese hamster ovaryantibody productionbioprocessglycosylationmodellingmodulators

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Area of Science:

  • Biotechnology
  • Biopharmaceutical Manufacturing
  • Protein Engineering

Background:

  • Glycosylation is a critical post-translational modification impacting protein function and stability.
  • Controlling glycosylation is essential for producing high-quality biopharmaceuticals.
  • Production media and feeds significantly influence protein glycosylation patterns.

Purpose of the Study:

  • To evaluate the N-glycosylation-modulating effects of various compounds.
  • To identify optimal modulator combinations for desired glycoforms.
  • To develop a predictive model for glycosylation control.

Main Methods:

  • Cultivation of Chinese hamster ovary cells producing IgG antibodies in fed-batch mode.
  • One-factor-at-a-time screening to identify potent modulators.
  • Response surface methodology in an Ambr® 15 bioreactor system to assess compound interactions.

Main Results:

  • Significant modulation of N-glycosylation profiles was achieved.
  • An up to eight-fold increase in specific glycoforms was observed.
  • A predictive model for glycoform control was successfully developed.

Conclusions:

  • Specific compounds effectively modulate N-glycosylation in recombinant antibody production.
  • The developed model facilitates targeted glycoform engineering.
  • This approach enhances control over critical quality attributes in biopharmaceutical manufacturing.