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Related Concept Videos

Protein Glycosylation01:25

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...
Oligosaccharide Assembly01:24

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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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Emerging technologies for making glycan-defined glycoproteins.

Lai-Xi Wang1, Joseph V Lomino

  • 1Institute of Human Virology, University of Maryland School of Medicine, Baltimore, 21201, United States. lwang@som.umaryland.edu

ACS Chemical Biology
|December 7, 2011
PubMed
Summary

Emerging technologies enable the production of specific glycoforms of glycoproteins. These advancements are crucial for understanding protein function and developing new therapeutics by overcoming challenges in isolating homogeneous glycoproteins.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Biotechnology

Background:

  • Protein glycosylation is a complex posttranslational modification creating diverse glycoproteins.
  • Glycoproteins are typically produced as heterogeneous mixtures of glycoforms, complicating isolation.
  • There is a significant need for homogeneous glycan-defined glycoproteins for research and therapeutics.

Purpose of the Study:

  • To review emerging technologies for producing glycan-defined glycoproteins.
  • To highlight advancements in manipulating protein glycosylation.
  • To focus on key areas of glycoengineering, chemoenzymatic remodeling, and site-specific glycosylation.

Main Methods:

  • Review of recent literature on protein glycosylation technologies.
  • Emphasis on glycoengineering of host pathways.
  • Discussion of in vitro chemoenzymatic glycosylation remodeling.
  • Exploration of chemoselective and site-specific protein glycosylation.

Main Results:

  • Emerging technologies offer promising solutions for generating glycan-defined glycoproteins.
  • Specific glycoengineering of host pathways allows for targeted glycan synthesis.
  • In vitro chemoenzymatic methods enable precise remodeling of existing glycans.
  • Chemoselective and site-specific approaches facilitate controlled glycosylation.

Conclusions:

  • Advancements in technology are overcoming the challenge of producing homogeneous glycoproteins.
  • These methods are essential for detailed structure-function studies.
  • The development of glycan-defined glycoproteins will accelerate therapeutic applications.