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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...

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...

Glycocalyx and its Functions

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Glycosaminoglycans

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...

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Related Experiment Video

Updated: May 8, 2025

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

MicroGlycoDB: A database of microbial glycans using Semantic Web technologies.

Sunmyoung Lee¹, Louis-David Leclercq², Yann Guerardel²

¹Glycan and Life Systems Integration Center (GaLSIC), Soka University, Hachioji, Tokyo, Japan.

|December 25, 2024

Summary

This summary is machine-generated.

Microbial glycans are crucial for host interactions. A new database, MicroGlycoDB, integrates microbial glycosylation data using Semantic Web Technologies for easier access and analysis.

Keywords:

Data integration Database Glycosylation Microbes Semantic data

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Published on: November 2, 2021

Area of Science:

Microbiology
Glycoscience
Bioinformatics

Background:

Microbial surface glycoconjugates are vital for host-microbe interactions.
Understanding microbial glycosylation is key for therapeutic and probiotic applications.
Current glycan information is fragmented across databases and literature.

Purpose of the Study:

To develop a centralized database for microbial glycosylation information.
To integrate and structure data on microbial glycans from model organisms.
To facilitate research on microbial glycosylation processes and applications.

Main Methods:

Development of the MicroGlycoDB database.
Utilization of Semantic Web Technologies for data representation.
Ontology-based data structuring for machine accessibility.

Main Results:

Integrated glycan information for key model microorganisms is now available.
MicroGlycoDB provides structured, machine-readable microbial glycan data.
The database facilitates data sharing and integration with other biological resources.

Conclusions:

MicroGlycoDB addresses the challenge of dispersed microbial glycan information.
Semantic data representation enhances knowledge discovery in microbiology.
The database serves as a foundation for expanding glycosylation information across more microorganisms.