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Updated: Dec 5, 2025

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

Mapping glycan-mediated galectin-3 interactions by live cell proximity labeling.

Eugene Joeh¹, Timothy O'Leary¹, Weichao Li^1,2

¹Department of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458.

Proceedings of the National Academy of Sciences of the United States of America

|October 17, 2020

Summary

Researchers identified galectin-3

Keywords:

galectins glycan glycomics proteomics proximity labeling

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Identifying Cell Surface Markers of Primary Neural Stem and Progenitor Cells by Metabolic Labeling of Sialoglycan

Identifying Cell Surface Markers of Primary Neural Stem and Progenitor Cells by Metabolic Labeling of Sialoglycan

Published on: September 7, 2019

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Last Updated: Dec 5, 2025

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Author Spotlight: Unveiling the Structural and Dynamic Aspects of Glycan Molecular Recognition

Published on: May 17, 2024

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

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Published on: January 20, 2022

Identifying Cell Surface Markers of Primary Neural Stem and Progenitor Cells by Metabolic Labeling of Sialoglycan

Identifying Cell Surface Markers of Primary Neural Stem and Progenitor Cells by Metabolic Labeling of Sialoglycan

Published on: September 7, 2019

Area of Science:

Glycobiology and immunology research.
Focus on cellular glycoproteins and their interactions.

Background:

Galectin-3 is a key glycan-binding protein (GBP) involved in cell activation and immune regulation.
The specific cellular glycoproteins interacting with galectin-3 have remained unidentified.
Native 3D glycan presentation is crucial for understanding GBP interactions.

Purpose of the Study:

To identify galectin-3's glycoprotein receptors in live cells.
To map the glycan structures recognized by galectin-3.
To provide a foundation for developing targeted galectin-3 therapeutics.

Main Methods:

Integrated proximity labeling with quantitative mass spectrometry.
Studied live human hepatic stellate cells and peripheral blood mononuclear cells.
Preserved native glycan presentation and glycoprotein expression.

Main Results:

Successfully mapped galectin-3's glycan and glycoprotein interactors.
Identified specific cellular glycoproteins and their associated glycan structures.
Provided a live-cell, native system for studying galectin-3 interactions.

Conclusions:

The study identified key cellular glycoproteins interacting with galectin-3.
Understanding these interactions is vital for developing targeted therapies.
This work advances the field of galectin-3 research and therapeutic development.