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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.
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Updated: Mar 20, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Sialoglycan engineering empowered by recombinant sialyltransferases.

Sascha N Woolcott¹, Isabelle Da Barp¹, Chantelle J Capicciotti²

¹Department of Chemistry, The University of Toronto, Canada.

Biochimica Et Biophysica Acta. General Subjects

|March 18, 2026

Summary

Sialic acid sugars regulate biological processes and are key targets in immunity. Sialyltransferases enable glycoengineering for detecting and modifying these sugars, advancing our understanding of health and disease.

Keywords:

Chemical biology Chemoenzymatic synthesis Glycobiology Glycoengineering Sialic acid Sialyltransferases

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Area of Science:

Glycoscience
Biochemistry
Immunology

Background:

Sialic acids are crucial monosaccharides regulating biological processes and immune responses.
Sialoglycans are synthesized by sialyltransferases, which transfer CMP-sialic acid to acceptor glycans.
Sialyltransferases exhibit substrate tolerance, allowing incorporation of modified sialic acids.

Purpose of the Study:

To review chemical modifications of sialic acids compatible with sialyltransferases.
To highlight applications in chemoenzymatic synthesis and selective exo-enzymatic labeling (SEEL).
To underscore the role of these technologies in advancing sialoglycan biology and disease research.

Main Methods:

Utilizing recombinant sialyltransferases for glycoengineering.
Employing chemoenzymatic synthesis with modified sialic acids.
Applying selective exo-enzymatic labeling (SEEL) for cell surface sialoglycan assembly.

Main Results:

Demonstrated compatibility of various chemical sialic acid modifications with diverse sialyltransferases.
Enabled efficient chemoenzymatic synthesis of complex glycan structures.
Facilitated sialoglycan engineering on living cell surfaces via SEEL.

Conclusions:

Sialyltransferase-mediated glycoengineering offers powerful tools for sialoglycan research.
These technologies enhance the understanding of sialoglycan functions in health and disease.
Future applications hold promise for novel diagnostics and therapeutics.