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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...

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Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

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Approaches toward High-Mannose-Type Glycan Libraries.

Kohki Fujikawa^1,2, Akira Seko¹, Yoichi Takeda^1,3

¹Japan Science and Technology Agency (JST), ERATO Ito Glycotrilogy Project, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.

Chemical Record (New York, N.Y.)

|October 24, 2015

Summary

Researchers developed a chemoenzymatic strategy to synthesize all high-mannose glycans, crucial for glycoprotein quality control in the endoplasmic reticulum (ER). This advancement aids in understanding the molecular basis of glycan recognition and function.

Keywords:

carbohydrates glycoconjugates glycoproteins glycosylation protein folding

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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

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Published on: August 26, 2025

Area of Science:

Glycobiology
Molecular Biology
Endoplasmic Reticulum (ER) Function

Background:

Asparagine-linked (N-linked) glycans in the ER are vital for glycoprotein quality control.
Misfolded glycoproteins are targeted for degradation, while correctly folded ones move to the Golgi.
The molecular mechanisms by which proteins recognize specific high-mannose oligosaccharide structures remain unclear.

Purpose of the Study:

To establish a systematic synthesis strategy for high-mannose-type glycans.
To enable precise structure-function relationship studies of high-mannose glycans.
To elucidate the molecular foundations of glycan recognition in glycoprotein processing.

Main Methods:

Development of a "top-down" chemoenzymatic approach.
Systematic synthesis of a comprehensive library of high-mannose-type glycans.
Generation of 37 distinct high-mannose glycans, including G1M9-M3 structures.

Main Results:

Successful and expeditious synthesis of a wide array of high-mannose glycans.
Comprehensive delivery of 37 unique high-mannose-type glycans.
Creation of a valuable resource for studying glycan structure-function relationships.

Conclusions:

The developed chemoenzymatic strategy provides access to all high-mannose glycans.
This facilitates detailed investigation into the roles of specific glycan structures in ER glycoprotein quality control.
The findings pave the way for understanding the molecular basis of glycan-protein interactions.