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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...

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Related Experiment Video

Updated: Jun 19, 2026

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Published on: February 7, 2025

Metabolomics in glycomics.

Evelyn C Soo¹, Joseph P M Hui

¹Institute for Marine Biosciences, National Research Council Canada, Halifax, Nova Scotia, Canada.

Methods in Molecular Biology (Clifton, N.J.)

|November 3, 2009

Summary

This summary is machine-generated.

This study used hydrophilic interaction liquid chromatography-mass spectrometry (HILIC-MS) to analyze sugar-nucleotides involved in novel carbohydrate modifications in Campylobacter sp. The method identified key biosynthetic intermediates and genes, advancing our understanding of bacterial glycosylation.

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Last Updated: Jun 19, 2026

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A Strategy for Sensitive, Large Scale Quantitative Metabolomics

A Strategy for Sensitive, Large Scale Quantitative Metabolomics

Published on: May 27, 2014

Area of Science:

Microbiology
Biochemistry
Metabolomics

Background:

Glycomics offers insights into novel glycoconjugate biosynthesis by analyzing metabolomes for pathway substrates.
Campylobacter sp. flagellins possess highly novel carbohydrate modifications, necessitating detailed biosynthetic pathway investigation.

Purpose of the Study:

To investigate the biosynthesis of novel carbohydrate modifications on Campylobacter sp. flagellins.
To identify sugar-nucleotide intermediates and their corresponding genes involved in this glycosylation process.

Main Methods:

Focused metabolomic study using hydrophilic interaction liquid chromatography-mass spectrometry (HILIC-MS) to analyze sugar-nucleotides.
Utilized high-resolution mass spectrometry and nuclear magnetic resonance (NMR) spectroscopy for structural identification.
Screened isogenic mutants to determine gene functions in the flagellin glycosylation locus.

Main Results:

HILIC-MS effectively discriminated between closely related sugar-nucleotide intermediates.
Identified specific sugar-nucleotides crucial for novel carbohydrate modification biosynthesis.
Determined the roles of specific genes in the flagellin glycosylation locus via mutant screening.

Conclusions:

HILIC-MS is a powerful tool for targeted metabolomic analysis in glycomics.
Elucidated key aspects of the biosynthetic pathway for novel flagellar carbohydrate modifications in Campylobacter sp.
Provided a foundation for further research into bacterial glycosylation mechanisms.