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Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

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Identification of Siglec Ligands Using a Proximity Labeling Method.

Lanyi Chang, Yi-Ju Chen, Chan-Yo Fan¹

¹Department of Chemistry, National Tsing Hua University , Hsinchu 300, Taiwan.

Journal of Proteome Research

|September 14, 2017

Summary

Researchers developed a proximity labeling method to identify Siglec ligands, crucial for immune system function. This technique successfully identified known and novel Siglec-15 ligands, advancing our understanding of immune cell interactions.

Keywords:

Siglec lectin ligand peroxidase proteomics proximity labeling sialic acid tyramide

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Area of Science:

Immunology
Glycobiology
Biochemistry

Background:

Sialic acid-binding immunoglobulin-like lectins (Siglecs) are key immune receptors involved in self-nonself discrimination.
Identifying Siglec ligands is crucial for understanding immune responses, but their weak interactions pose a significant challenge.

Purpose of the Study:

To develop and validate a proximity labeling method for efficient identification of Siglec ligands.
To discover novel Siglec-ligand interactions and understand their biological implications.

Main Methods:

Utilized a proximity labeling strategy based on tyramide radicalization to covalently label proteins near Siglec-peroxidase complexes.
Employed CD22 (Siglec-2) and Siglec-15 probes for proof-of-principle experiments and novel ligand discovery.
Validated findings through sialidase treatment, mutant probes, and protein-protein interaction network analysis.

Main Results:

Successfully identified known CD22 ligands (CD22, CD45, IgM) on B cells, confirming the method's validity.
Discovered CD44 as a novel Siglec-15 ligand on osteoclasts.
Revealed potential molecular clustering of CD22 ligands through network analysis.

Conclusions:

Proximity labeling is a powerful and versatile tool for identifying Siglec ligands and their interactions.
This method facilitates the study of Siglec-mediated biological processes and can be extended to other lectins.