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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

Conservation, Compensation, and Evolution of N-Linked Glycans in the HIV-1 Group M Subtypes and Circulating

Simon A Travers1

  • 1Medical Research Council Unit for Bioinformatics Capacity Development, South African National Bioinformatics Institute, University of the Western Cape, Private Bag X17, Belville 7535, South Africa.

ISRN AIDS
|September 21, 2013
PubMed

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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.
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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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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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