Related Experiment Video

Updated: May 9, 2026

High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension
11:42

High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension

Published on: December 28, 2015

Glycosylation control strategies for recombinant therapeutic proteins in CHO cells

Weifeng Wang1, Weidong Li2, Qianwen Wang3

  • 1Institutes of Health Central Plains, Xinxiang Key Laboratory for Tumor Drug Screening and Targeted Therapy, Xinxiang Medical University, Xinxiang, 453003, China; International Joint Research Laboratory for Recombinant Pharmaceutical Protein Expression System of Henan, Xinxiang, 453003, China; Henan Key Laboratory of Neurorestoratology and Protein Modification, the First Affiliated Hospital of Xinxiang Medical University, Xinxiang, 453003, China.

Biochimie
|March 3, 2026
PubMed

Insights

Chinese hamster ovary (CHO) cells are key for producing therapeutic proteins. Glycosylation impacts protein function, and this review explores controlling it for better protein quality and stability.

Area of Science:

  • Biotechnology
  • Biochemistry
  • Cell Biology

Background:

  • Chinese hamster ovary (CHO) cells are the primary hosts for recombinant therapeutic protein (RTP) production.
  • Glycosylation is a critical post-translational modification affecting RTP function, stability, and immunogenicity.
  • Understanding glycosylation is vital for optimizing RTP quality and efficacy.

Purpose of the Study:

  • To review the biological role of glycosylation in CHO cells.
  • To analyze factors influencing recombinant protein glycosylation.
  • To explore strategies for controlling glycosylation in RTP production.

Main Methods:

  • Literature review of glycosylation in CHO cells.
  • Analysis of intrinsic and extrinsic factors affecting glycosylation.
  • Exploration of gene editing and cell culture optimization techniques.

Main Results:

  • Glycosylation significantly impacts protein folding, stability, immunogenicity, biological activity, and half-life.
  • Intrinsic and extrinsic factors can be modulated to control glycosylation patterns.
  • Gene editing and cell culture optimization show promise for enhancing RTP glycosylation.

Conclusions:

  • Controlling glycosylation in CHO cells is crucial for improving RTP quality and therapeutic potential.
  • Current strategies offer effective modulation of glycosylation patterns.
  • Further research is needed to address challenges and advance glycosylation control.
Keywords:
BiopharmaceuticalChinese hamster ovary cellsGenetic engineeringGlycosylationRecombinant protein

More Related Videos

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells06:53

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells

Published on: June 2, 2022

Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Bioreactor Controls-III01:22

Bioreactor Controls-III

Strain improvement is a foundational strategy in industrial microbiology aimed at maximizing microbial productivity, particularly because natural isolates typically yield commercially valuable products in very low concentrations. Although optimizing the culture medium and environmental conditions can improve yields, these adjustments are inherently limited by the organism’s genetic potential. As a result, the focus shifts toward genetic modifications to enhance biosynthetic capacity. The...
Upstream Processing01:27

Upstream Processing

Upstream processing represents a critical phase in biomanufacturing, wherein biological systems such as microorganisms, mammalian cells, or insect cells are cultivated to produce therapeutic proteins, vaccines, enzymes, or other biologically derived products. This phase encompasses all steps from the selection and genetic manipulation of the production organism to the cultivation of cells in bioreactors under tightly controlled environmental conditions.Host Selection and Genetic OptimizationThe...
Production of Pharmaceuticals01:30

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...