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

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, the...

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Autores principales: Wang, Shuaishuai, Chen, Congcong, Guan, Minhui, Liu, Ding, Wan, Xiu-Feng, Li, Lei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8116747/
https://www.ncbi.nlm.nih.gov/pubmed/33996901
http://dx.doi.org/10.3389/fmolb.2021.645999
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author Wang, Shuaishuai
Chen, Congcong
Guan, Minhui
Liu, Ding
Wan, Xiu-Feng
Li, Lei
author_facet Wang, Shuaishuai
Chen, Congcong
Guan, Minhui
Liu, Ding
Wan, Xiu-Feng
Li, Lei
author_sort Wang, Shuaishuai
collection PubMed
description 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.
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spelling pubmed-81167472021-05-14 Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans Wang, Shuaishuai Chen, Congcong Guan, Minhui Liu, Ding Wan, Xiu-Feng Li, Lei Front Mol Biosci Molecular Biosciences 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. Frontiers Media S.A. 2021-04-29 /pmc/articles/PMC8116747/ /pubmed/33996901 http://dx.doi.org/10.3389/fmolb.2021.645999 Text en Copyright © 2021 Wang, Chen, Guan, Liu, Wan and Li. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Wang, Shuaishuai
Chen, Congcong
Guan, Minhui
Liu, Ding
Wan, Xiu-Feng
Li, Lei
Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
title Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
title_full Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
title_fullStr Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
title_full_unstemmed Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
title_short Terminal Epitope-Dependent Branch Preference of Siglecs Toward N-Glycans
title_sort terminal epitope-dependent branch preference of siglecs toward n-glycans
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8116747/
https://www.ncbi.nlm.nih.gov/pubmed/33996901
http://dx.doi.org/10.3389/fmolb.2021.645999
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