Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Oligosaccharide Assembly

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...

Protein Glycosylation

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

miR-132 overexpression is associated with modulation in miR-21 expression and glioblastoma cell behavior.

PloS one·2026

Same author

Optimization of keratinase production by <i>Bacillus cereus</i> HD1 using feather waste and its laboratory scale validation in bioreactor with oxygen and carbon supplementation.

Preparative biochemistry & biotechnology·2026

Same author

Overexpression of histidine decarboxylase promotes cancer cell apoptosis and migration in HN5 cells.

Naunyn-Schmiedeberg's archives of pharmacology·2025

Same author

Chitosan nanoparticles loaded with ribavirin, carboplatin, and thyme oil downregulate SNQ2, ERG11, CDR1, and MDR1 in Candida strains.

Scientific reports·2025

Same author

Catalytically active inclusion bodies of cold-adapted lipase: production and its industrial potential.

AMB Express·2025

Same author

Immobilized inclusion bodies of recombinant cold-adaptive lipase from Antarctic Pseudomonas sp. as catalysts.

Applied microbiology and biotechnology·2025

Search research articles

Related Experiment Video

Updated: Mar 12, 2026

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells

Published on: June 2, 2022

Humanizing glycosylation pathways in eukaryotic expression systems.

Amjad Hayat Khan¹, Hadi Bayat^2,3, Masoumeh Rajabibazl^4,5

¹Department of Medical Biotechnology, School of Advanced Technologies in Medicine, International Campus, Tehran University of Medical Sciences, Tehran, Iran.

World Journal of Microbiology & Biotechnology

|November 13, 2016

Summary

Glycosylation, a key protein modification, impacts therapeutic glycoprotein function. This review explores strategies for humanizing glycosylation in expression hosts and highlights Leishmania as a promising system.

Keywords:

Eukaryotic expression systems Glycoengineering Glycosylation pattern LEXSY

More Related Videos

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

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

Published on: December 28, 2015

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Related Experiment Videos

Last Updated: Mar 12, 2026

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells

Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells

Published on: June 2, 2022

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

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

Published on: December 28, 2015

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Area of Science:

Biochemistry
Molecular Biology
Biotechnology

Background:

Glycosylation is a prevalent posttranslational modification impacting protein properties.
Therapeutic glycoproteins require specific glycosylation for efficacy.
Existing expression systems have limitations in achieving human-like glycosylation.

Purpose of the Study:

To review strategies for humanizing glycosylation pathways in expression hosts.
To highlight the potential of protozoan parasites, specifically Leishmania tarentolae, as a mammalian-like glycosylation expression system.

Main Methods:

Literature review of glycosylation strategies in various expression systems.
Analysis of glycosylation pathways in eukaryotic hosts.
Evaluation of Leishmania tarentolae's glycosylation capabilities.

Main Results:

Eukaryotic expression systems often produce non-human glycosylation patterns.
Various strategies exist to engineer glycosylation pathways for humanization.
Leishmania tarentolae exhibits mammalian-like glycosylation, offering a novel expression system.

Conclusions:

Engineering glycosylation pathways is crucial for producing effective therapeutic glycoproteins.
Leishmania expression systems present a viable alternative for achieving human-like glycosylation.