Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.5K
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...
3.5K
Selectins01:25

Selectins

4.1K
Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
4.1K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

2.7K
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.7K
Protein Glycosylation01:25

Protein Glycosylation

9.2K
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...
9.2K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Synthesis of Cyclopropene-Modified Fatty Acids Allows Single-Cell Quantification of Uptake by Immune Cells.

Angewandte Chemie (International ed. in English)·2026
Same author

Homing pigeon navigation relies on superparamagnetic macrophages under overcast conditions.

Science (New York, N.Y.)·2026
Same author

Light and Enzymatic Cooperative Response in Supramolecular Fibers: A Synergistic Strategy for Potential Drug Delivery Applications.

Biomacromolecules·2026
Same author

Stimulus-Driven Remodeling of Microglial Endocannabinoid Metabolism Illuminates ABHD12 Function in Immunity.

ACS chemical neuroscience·2026
Same author

Phenotyping by Molecular Mobility: Low-Affinity Reversible Probes Enable Characterizing and Classifying Cells Populations by Single-Molecule Imaging.

Journal of the American Chemical Society·2026
Same author

Predicting Macrophage Spatial Localization from Single-Cell Transcriptomes to Uncover Disease Mechanisms.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026

Related Experiment Video

Updated: Jan 7, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

498

Subcellular glycan-mannose receptor binding kinetics correlate with myeloid cell function.

Kas Steuten1, Johannes J A Bakker1, Ward Doelman1

  • 1Department of Chemical Biology and Immunology, Leiden Institute of Chemistry, Leiden University, Leiden, the Netherlands.

Nature Communications
|December 26, 2025
PubMed
Summary

Glyco-PAINT-APP automates single-molecule lectin binding analysis in primary immune cells. This method reveals glycan-structure-activity relationships, crucial for understanding immune cell function.

More Related Videos

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

13.2K
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.7K

Related Experiment Videos

Last Updated: Jan 7, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
10:07

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

Published on: August 26, 2025

498
Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

13.2K
Engineering Antiviral Agents via Surface Plasmon Resonance
13:00

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

2.7K

Area of Science:

  • Immunology
  • Glycobiology
  • Biophysics

Background:

  • Single-molecule lectin binding kinetics in primary cells remain challenging to measure.
  • Understanding glycan interactions is vital for immune cell function and antigen presentation.

Purpose of the Study:

  • To develop an automated method for extracting subcellular glycan interaction kinetics.
  • To correlate glycan binding patterns with immune cell polarization and antigen uptake.

Main Methods:

  • Developed Glyco-PAINT-APP, an automated processing pipeline using Points Accumulation for Imaging in Nano-Topography (PAINT).
  • Employed algorithms for high-throughput, subcellular analysis of glycan binding dynamics.
  • Utilized synthetic glycans and glycosylated antigens for validation.

Main Results:

  • Demonstrated automatic correlation of glycan binding parameters with antigen uptake and cross-presentation efficiency in dendritic cells.
  • Uncovered subtle differences in mannose receptor (MR)-mediated glycan binding across various MR-expressing cells.
  • Provided insights into cell-intrinsic heterogeneity of glycan-structure-activity relationships.

Conclusions:

  • Glyco-PAINT-APP enables precise, automated analysis of subcellular glycan binding kinetics.
  • The method facilitates functional correlation studies between glycan interactions and immune cell behavior.
  • This approach advances our understanding of glycan roles in myeloid immune cells.