AtaGenix Laboratories
AtaGenix Laboratories
Release time: 2026-03-31 View volume: 29
Glycosylation is the most common and functionally significant post-translational modification in recombinant proteins. It affects protein folding, stability, half-life, and biological activity. This guide explains the types of glycosylation, why they matter, and how expression system choice determines glycan structure.
Glycosylation is the enzymatic attachment of sugar chains (glycans) to specific amino acid residues on a protein. It occurs in the endoplasmic reticulum and Golgi apparatus of eukaryotic cells. Glycans can comprise 10–50% of a glycoprotein’s molecular weight and profoundly influence its biophysical and biological properties.
N-linked glycosylation: Glycan attached to the asparagine (Asn) side chain in an Asn-X-Ser/Thr sequon. The most common type, critical for antibody Fc function (Asn297 in IgG). Subtypes include high-mannose, hybrid, and complex glycans.
O-linked glycosylation: Glycan attached to serine or threonine hydroxyl groups. No consensus sequence; less predictable than N-linked. Important for mucins, cytokines, and some cell-surface receptors.
Protein folding & stability: Glycans assist co-translational folding in the ER, shield hydrophobic patches, and increase thermal and proteolytic stability.
Serum half-life: Sialylated glycans prevent clearance by asialoglycoprotein receptors in the liver. Desialylated proteins are rapidly cleared from circulation.
Antibody effector functions: The Fc N-glycan at Asn297 directly modulates Fcγ receptor binding. Afucosylated antibodies show 50–100× enhanced ADCC — the basis of glycoengineered therapeutic antibodies.
Immunogenicity: Non-human glycan structures (e.g., α-Gal, NGNA) can trigger immune responses in patients, making glycan profile a critical quality attribute for biologics.
| Expression System | Glycosylation Type | Key Characteristics |
|---|---|---|
| E. coli | None | No glycosylation machinery. Use only for proteins where glycans are not required for function. |
| Yeast | High-mannose | Hyper-mannosylation (Man8–Man14+). Can cause rapid clearance and immunogenicity in vivo. |
| Insect (BEVS) | Paucimannose | Simple, truncated glycans (Man3GlcNAc2 ± fucose). Adequate for structural studies, not for therapeutic glycoproteins. |
| CHO / HEK293 | Complex (human-like) | Full processing: sialylation, fucosylation, branching. Required for therapeutic antibodies and in vivo glycoproteins. |
Need properly glycosylated recombinant proteins? AtaGenix offers HEK293 and CHO expression for native human-type glycosylation, with glycan profiling available upon request.
Talk to Technical SupportResponse within 24 hours
Contact Us
+86-27-6552-3339
info@atagenix.com
Building C, R & D Building, No. 666, Shendun 4th Road, Donghu New Technology Development Zone, Wuhan
