High-mannose Oligosaccharides
High-mannose Oligosaccharides - Related Videos
01:24
Oligosaccharide Assembly
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2023
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...
09:56
Hierarchical and Programmable One-Pot Oligosaccharide Synthesis
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2019
This protocol demonstrates how to use the Auto-CHO software for hierarchical and programmable one-pot synthesis of oligosaccharides. It also describes the general procedure for RRV determination experiments and one-pot glycosylation of SSEA-4.
10:07
Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
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2025
This NMR-based protocol investigates weak protein-glycan interactions using cyanovirin-N and D-mannose. Combining ligand- and protein-detected methods, it maps binding sites, detects allosteric effects, and identifies encounter complexes. The approach outlines sample preparation and data analysis, offering structural and dynamic insights valuable for glycan-specific diagnostics and recognition mechanisms.
11:49
Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques
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Cited by 1 •
2016
This protocol describes the specific techniques used for the structural characterization of reducing end (RE) and internal region glycosyl sequence(s) of heteroxylans by tagging the RE with 2 aminobenzamide prior to enzymatic (endoxylanase) hydrolysis and then analysis of the resultant oligosaccharides using mass spectrometry (MS) and nuclear magnetic resonance (NMR).
03:27
Insoluble Chromogenic Biomass-Based Enzyme Screening: An Assay to Evaluate the Degradation Activity of Plant Biomass-Degrading Enzymes
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2025
This video demonstrates an assay to screen enzymes effective in degrading complex polysaccharides in plant biomass using insoluble chromogenic biomass or ICB. The enzymes hydrolyze ICB to release soluble dye-linked oligosaccharides, and the enzyme activity is assessed by colorimetric analysis of the reaction product.
FAQs
As glycoproteins move through the secretory pathway, enzymes trim and remodel their attached carbohydrate structures. The resulting processing state records where the glycoprotein has traveled and how extensively its N-linked glycans have been modified. This makes glycan maturation useful for interpreting protein trafficking and distinguishing newly synthesized or incompletely processed forms from structures that have progressed further through the pathway.
Their processing state can reflect whether a newly synthesized protein has folded appropriately and passed endoplasmic-reticulum quality-control steps. Changes in the attached glycans therefore provide information about the relationship between glycosylation and protein maturation. In biology research, examining these structures helps connect carbohydrate processing with the fate of glycoproteins before they continue through the secretory pathway.
High-mannose glycans can affect protein stability and create recognition features for lectins, which are proteins that bind specific carbohydrate structures. Those interactions may alter how glycoproteins associate with cells or other biological molecules. Consequently, glycan composition is not merely a processing record; it can also contribute to functional differences in recognition, persistence, and cellular interactions.
It can provide a molecular indication of the glycoprotein’s maturation, trafficking, and quality-control history. A structure that remains in a high-mannose state may reflect an earlier stage of secretory-pathway processing, whereas remodeling indicates further enzymatic action. Interpreting this state alongside protein behavior helps researchers investigate how biosynthesis and intracellular handling influence glycoprotein function.
Analysis can support studies of glycoprotein biosynthesis by revealing how carbohydrate structures change as proteins mature and move through the secretory pathway. It can also help examine relationships among glycan processing, protein folding, quality control, and trafficking. These measurements are valuable when researchers need to connect molecular glycan patterns with broader cellular or protein-level outcomes.
Their processing patterns can help researchers investigate defects that disrupt glycoprotein glycosylation. Because the structures are linked to biosynthesis, folding, quality control, and trafficking, abnormal processing may provide insight into where glycan maturation is altered. Studying these changes contributes to understanding the molecular basis of congenital disorders of glycosylation and their effects on glycoprotein biology.
High-mannose glycans can participate in lectin-mediated recognition and interactions between glycoproteins, cells, or pathogens, making them relevant to immune recognition and viral entry research. In biopharmaceutical development, their analysis supports characterization and quality assessment of glycoprotein products. The same structural information can therefore address both biological mechanisms and consistency of engineered protein preparations.