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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...
Proteoglycans01:05

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,...
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...
Chemistry of Carbohydrates03:25

Chemistry of Carbohydrates

Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

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Related Experiment Video

Updated: Jun 2, 2026

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry
13:06

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Published on: November 20, 2014

Structural characterization of complex O-linked glycans from insect-derived material.

Estelle Garenaux1, Emmanuel Maes, S Levêque

  • 1Université de Lille1, Unité de Glycobiologie Structurale et Fonctionnelle, UGSF, F-59650 Villeneuve d'Ascq, France.

Carbohydrate Research
|May 4, 2011
PubMed
Summary

Insect glycosylation diversity is explored in Hymenoptera species. Wasp nests revealed complex O-glycans, while hornet nests showed a simpler structure, expanding knowledge of insect glycan profiles.

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Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry
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Published on: June 25, 2018

Area of Science:

  • Biochemistry
  • Glycobiology
  • Entomology

Background:

  • Insects exhibit vast diversity, yet structural data on their glycosylation is limited.
  • Hymenoptera, a major insect order, includes social insects like wasps, bees, and ants.
  • Previous studies identified key O-glycans in wasp mucins.

Purpose of the Study:

  • To investigate the structural diversity of O-glycans in two Hymenoptera species.
  • To analyze and compare O-glycan structures from common wasp and hornet nests.
  • To contribute to understanding insect glycosylation capabilities.

Main Methods:

  • Reductive β-elimination of nest materials.
  • Fractionation of oligosaccharide-alditols using multidimensional HPLC.
  • Structural elucidation via tandem mass spectrometry and NMR spectroscopy.

Main Results:

  • Wasp nests yielded complex O-glycans with core types 1 and 2, Lewis X, and Gal-Gal motifs.
  • Unusual O-glycans with a fucose-substituted reducing GalNAc unit were identified in wasps.
  • Hornet nests contained a homogeneous family of core 1 O-glycans with galactose extensions.

Conclusions:

  • Significant structural diversity exists in Hymenoptera O-glycans.
  • Wasp and hornet glycosylation patterns differ notably.
  • This study enhances the understanding of insect glycan structures and their variations.