Related Experiment Video
Updated: Jul 18, 2026
09:54
Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Lectin-resistant CHO glycosylation mutants
Santosh Kumar Patnaik1, Pamela Stanley
1Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY, USA.
Methods in Enzymology
|November 23, 2006
Summary
Chinese hamster ovary (CHO) cells resistant to plant lectins reveal diverse protein and lipid glycosylation defects. These mutants are crucial for understanding glycosylation pathways and engineering cellular glycan structures.
Area of Science:
- Biochemistry
- Cell Biology
- Genetics
Background:
- Plant lectins are proteins that bind to specific carbohydrate structures.
- Lectins can be cytotoxic to cells, particularly those with altered glycosylation.
- Chinese hamster ovary (CHO) cells are widely used in biological research and biopharmaceutical production.
Purpose of the Study:
- To describe a panel of lectin-resistant CHO cell mutants.
- To summarize the glycan alterations in these mutants.
- To elucidate the biochemical and genetic basis of these mutations.
Main Methods:
- Isolation of CHO mutant cells resistant to plant lectin cytotoxicity.
- Characterization of glycan alterations in the mutant cells.
- Biochemical and genetic analysis to determine the basis of mutations.
Main Results:
- A diverse panel of lectin-resistant CHO mutants with various glycosylation defects was generated.
- These mutants exhibit specific alterations in protein and lipid glycosylation.
- The biochemical and genetic underpinnings of these glycosylation mutations were identified.
Conclusions:
- Lectin-resistant CHO mutants are valuable tools for studying glycosylation.
- These mutants facilitate the characterization of glycosylation pathways and gene functions.
- The mutants enable glycosylation engineering for biological and biotechnological applications.
Related Concept Videos
01:24Oligosaccharide 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...
Multiple sugar molecules that may or may...
01:25Protein 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...
Glycosylation occurs in...
01:05Proteoglycans
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,...
01:27Glucose Transporters
Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes: