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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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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. |
format | Online Article Text |
id | pubmed-8116747 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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