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Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans

Authors :
Shuaishuai Wang
Congcong Chen
Minhui Guan
Ding Liu
Xiu-Feng Wan
Lei Li
Source :
Frontiers in Molecular Biosciences, Frontiers in Molecular Biosciences, Vol 8 (2021)
Publication Year :
2021
Publisher :
Frontiers Media S.A., 2021.

Abstract

Siglecs are sialic acid–binding immunoglobulin-like lectins that play vital roles in immune cell signaling. Siglecs help the immune system distinguish between self and nonself through the recognition of glycan ligands. While the primary binding specificities of Siglecs are known to be divergent, their specificities for complex glycans remain unclear. Herein, we determined N-glycan binding profiles of a set of Siglecs by using a complex asymmetric N-glycan microarray. Our results showed that Siglecs had unique terminal epitope-dependent branch preference when recognizing asymmetric N-glycans. Specifically, human Siglec-3, -9, and -10 prefer the α1-3 branch when Siaα2-6Galβ1-4GlcNAc terminal epitope serves as the binding ligand but prefer the opposite α1-6 branch when Siaα2-3Galβ1-4GlcNAc epitope serves as the ligand. Interestingly, Siglec-10 exhibited dramatic binding divergence toward a pair of Neu5Ac-containing asymmetric N-glycan isomers, as well as their Neu5Gc-containing counterparts. This new information on complex glycan recognition by Siglecs provides insights into their biological roles and applications.

Details

Language :
English
ISSN :
2296889X
Volume :
8
Database :
OpenAIRE
Journal :
Frontiers in Molecular Biosciences
Accession number :
edsair.doi.dedup.....aebe6acc596c1659ecbeffe0a1a88a7f