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Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins

Glycans and glycan binding proteins (GBPs or lectins) are essential components in almost every aspect of immunology. Investigations of the interactions between glycans and GBPs have greatly advanced our understanding of the molecular basis of these fundamental immunological processes. In order to be...

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Autores principales: Gao, Chao, Wei, Mohui, McKitrick, Tanya R., McQuillan, Alyssa M., Heimburg-Molinaro, Jamie, Cummings, Richard D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6923789/
https://www.ncbi.nlm.nih.gov/pubmed/31921763
http://dx.doi.org/10.3389/fchem.2019.00833
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author Gao, Chao
Wei, Mohui
McKitrick, Tanya R.
McQuillan, Alyssa M.
Heimburg-Molinaro, Jamie
Cummings, Richard D.
author_facet Gao, Chao
Wei, Mohui
McKitrick, Tanya R.
McQuillan, Alyssa M.
Heimburg-Molinaro, Jamie
Cummings, Richard D.
author_sort Gao, Chao
collection PubMed
description Glycans and glycan binding proteins (GBPs or lectins) are essential components in almost every aspect of immunology. Investigations of the interactions between glycans and GBPs have greatly advanced our understanding of the molecular basis of these fundamental immunological processes. In order to better study the glycan-GBP interactions, microscope glass slide-based glycan microarrays were conceived and proved to be an incredibly useful and successful tool. A variety of methods have been developed to better present the glycans so that they mimic natural presentations. Breakthroughs in chemical biology approaches have also made available glycans with sophisticated structures that were considered practically impossible just a few decade ago. Glycan microarrays provide a wealth of valuable information in immunological studies. They allow for discovery of detailed glycan binding preferences or novel binding epitopes of known endogenous immune receptors, which can potentially lead to the discovery of natural ligands that carry the glycans. Glycan microarrays also serve as a platform to discover new GBPs that are vital to the process of infection and invasion by microorganisms. This review summarizes the construction strategies and the immunological applications of glycan microarrays, particularly focused on those with the most comprehensive sets of glycan structures. We also review new methods and technologies that have evolved. We believe that glycan microarrays will continue to benefit the growing research community with various interests in the field of immunology.
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spelling pubmed-69237892020-01-09 Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins Gao, Chao Wei, Mohui McKitrick, Tanya R. McQuillan, Alyssa M. Heimburg-Molinaro, Jamie Cummings, Richard D. Front Chem Chemistry Glycans and glycan binding proteins (GBPs or lectins) are essential components in almost every aspect of immunology. Investigations of the interactions between glycans and GBPs have greatly advanced our understanding of the molecular basis of these fundamental immunological processes. In order to better study the glycan-GBP interactions, microscope glass slide-based glycan microarrays were conceived and proved to be an incredibly useful and successful tool. A variety of methods have been developed to better present the glycans so that they mimic natural presentations. Breakthroughs in chemical biology approaches have also made available glycans with sophisticated structures that were considered practically impossible just a few decade ago. Glycan microarrays provide a wealth of valuable information in immunological studies. They allow for discovery of detailed glycan binding preferences or novel binding epitopes of known endogenous immune receptors, which can potentially lead to the discovery of natural ligands that carry the glycans. Glycan microarrays also serve as a platform to discover new GBPs that are vital to the process of infection and invasion by microorganisms. This review summarizes the construction strategies and the immunological applications of glycan microarrays, particularly focused on those with the most comprehensive sets of glycan structures. We also review new methods and technologies that have evolved. We believe that glycan microarrays will continue to benefit the growing research community with various interests in the field of immunology. Frontiers Media S.A. 2019-12-13 /pmc/articles/PMC6923789/ /pubmed/31921763 http://dx.doi.org/10.3389/fchem.2019.00833 Text en Copyright © 2019 Gao, Wei, McKitrick, McQuillan, Heimburg-Molinaro and Cummings. http://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 Chemistry
Gao, Chao
Wei, Mohui
McKitrick, Tanya R.
McQuillan, Alyssa M.
Heimburg-Molinaro, Jamie
Cummings, Richard D.
Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins
title Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins
title_full Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins
title_fullStr Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins
title_full_unstemmed Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins
title_short Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins
title_sort glycan microarrays as chemical tools for identifying glycan recognition by immune proteins
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6923789/
https://www.ncbi.nlm.nih.gov/pubmed/31921763
http://dx.doi.org/10.3389/fchem.2019.00833
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