# Glycan array

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'''Glycan arrays''',<ref name="Carbohydrate Microarrays">{{cite journal|vauthors=Carroll GT, Wang D, Turro NJ, Koberstein JT|title=Photochemical Micropatterning of Carbohydrates on a Surface|journal=Langmuir|date=2006|volume=22|issue=6 |pages=2899–2905|doi=10.1021/la0531042|pmid=16519501 }}</ref> like that offered by the [Consortium for Functional Glycomics](/source/Consortium_for_Functional_Glycomics) (CFG), [National Center for Functional Glycomics](/source/National_Center_for_Functional_Glycomics) (NCFG) and Z Biotech, contain [carbohydrate](/source/carbohydrate) compounds that can be screened with [lectin](/source/lectin)s, [antibodies](/source/antibodies) or [cell receptor](/source/cell_receptor)s to define carbohydrate specificity and identify [ligand](/source/ligand)s. Glycan array screening works in much the same way as other microarrays used, for instance, to study gene expression ([DNA microarrays](/source/DNA_microarrays)) or protein interaction ([protein microarray](/source/protein_microarray)s).

Glycan arrays are composed of various [oligosaccharide](/source/oligosaccharide)s and [polysaccharide](/source/polysaccharide)s immobilized on a solid support in a spatially defined arrangement.<ref name="Glycan arrays: recent advances and future challenges">{{cite journal|vauthors=Oyelaran O, Gildersleeve JC|title=Glycan arrays: recent advances and future challenges|journal=Curr Opin Chem Biol|date=Oct 2009|volume=13|issue=4|pages=406–413|doi=10.1016/j.cbpa.2009.06.021|pmid=19625207|pmc=2749919 }}</ref> This technology provides the means of studying [glycan–protein interaction](/source/glycan%E2%80%93protein_interaction)s in a [high-throughput](/source/high-throughput_biology) environment. These natural or synthetic (see [carbohydrate synthesis](/source/carbohydrate_synthesis)) glycans are then incubated with any glycan-binding protein such as lectins, [cell surface receptor](/source/cell_surface_receptor)s or possibly a whole organism such as a [virus](/source/virus). Binding is quantified using [fluorescence](/source/fluorescence)-based detection methods. Certain types of glycan microarrays can even be re-used for multiple samples using a method called microwave assisted wet-erase.<ref>{{cite journal |last1=Mehta |first1=Akul Y |last2=Tilton |first2=Catherine A |last3=Muerner |first3=Lukas |last4=von Gunten |first4=Stephan |last5=Heimburg-Molinaro |first5=Jamie |last6=Cummings |first6=Richard D |title=Reusable glycan microarrays using a microwave assisted wet-erase (MAWE) process |journal=Glycobiology |date=14 November 2023 |volume=34 |issue=2 |doi=10.1093/glycob/cwad091 |pmid=37962922|pmc=10969520 }}</ref>

==Applications==
Glycan arrays have been used to characterize previously unknown [biochemical](/source/biochemical) interactions. For example, photo-generated glycan arrays have been used to characterize the [immunogenic](/source/immunogenic) properties of a [tetrasaccharide](/source/tetrasaccharide) found on the surface of [anthrax](/source/anthrax) spores.<ref name="Anthrax">{{cite journal|vauthors=Wang D, Carroll GT, Turro NJ, Koberstein JT, Kováč P, Saksena R, Adamo R, Herzenberg LA, Herzenberg LA, Steinman L|title=Photogenerated glycan arrays identify immunogenic sugar moieties of Bacillus anthracis exosporium|journal=Proteomics|date=2007|volume=7|issue=2 |pages=180–184|doi=10.1002/pmic.200600478|doi-access=free|pmid=17205603 }}</ref> Hence, glycan array technology can be used to study the specificity of [host–pathogen interaction](/source/host%E2%80%93pathogen_interaction)s.<ref name="Glycan arrays as tools for infectious disease research">{{cite journal|vauthors=Geissner A, Anish C, Seeberger PH|title=Glycan arrays as tools for infectious disease research|journal=Curr Opin Chem Biol|date=Feb 2014|volume=18|pages=38–45|doi=10.1016/j.cbpa.2013.11.013|pmid=24534751}}</ref>

Early on, glycan arrays were proven useful in determining the specificity of the [hemagglutinin](/source/hemagglutinin_(influenza)) of the [influenza A virus](/source/influenza_A_virus) binding to the host and distinguishing across different strains of flu (including avian from mammalian). This was shown with CFG arrays<ref name="Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus">{{cite journal|vauthors=Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC, Wilson IA|title=Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus|journal=Science|date=Apr 2006|volume=312|issue=5772|pages=404–410|doi=10.1126/science.1124513|pmid=16543414|bibcode=2006Sci...312..404S|doi-access=}}</ref> as well as customized arrays.<ref name="Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate  microarray">{{cite journal|vauthors=Childs RA, Palma AS, Wharton S, Matrosovich T, Liu Y, Chai W, Campanero-Rhodes MA, Zhang Y, Eickmann M, Kiso M, Hay A, Matrosovich M, Feizi T|title=Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray|journal=Nat Biotechnol|date=Sep 2009 |volume=27|issue=9|pages=797–799|doi=10.1038/nbt0909-797|pmid=19741625|pmc=3771066}}</ref> 
Cross-platform benchmarks led to highlight the effect of glycan presentation and spacing on binding.<ref name="Cross-platform comparison of glycan microarray formats">{{cite journal |vauthors=Wang L, Cummings RD, Smith DF, Huflejt M, Campbell CT, Gildersleeve JC, Gerlach JQ, Kilcoyne M, Joshi L, Serna S, Reichardt NC, Parera Pera N, Pieters RJ, Eng W, Mahal LK|title=Cross-platform comparison of glycan microarray formats|journal= Glycobiology |date= Jun 2014|volume=24|issue=6|pages=507–17|doi=10.1093/glycob/cwu019|pmid= 24658466 |pmc=4001710}}</ref>

Glycan arrays can be combined with other techniques such as [surface plasmon resonance](/source/surface_plasmon_resonance) (SPR) to refine the characterization of [glycan-binding](/source/glycan%E2%80%93protein_interaction). For example, this combination led to demonstrate the calcium-dependent [heparin](/source/heparin) binding of [annexin A1](/source/annexin_A1) that is involved in several biological processes including [inflammation](/source/inflammation), [apoptosis](/source/apoptosis) and [membrane trafficking](/source/membrane_trafficking).<ref name="Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin">{{cite journal |vauthors=Horlacher T, Noti C, de Paz JL, Bindschädler P, Hecht ML, Smith DF, Fukuda MN, Seeberger PH|title=Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin|journal=Biochemistry|date=Apr 2011|volume=50|issue=13|pages=2650–9|doi=10.1021/bi101121a|pmid= 21370880 |pmc=3068229}}</ref>

==References==
{{Reflist}}

Category:Microarrays
Category:Glycobiology
Category:Glycomics
Category:Carbohydrates

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Adapted from the Wikipedia article [Glycan array](https://en.wikipedia.org/wiki/Glycan_array) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Glycan_array?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.