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==Applications==
Glycan arrays have been used to characterize previously unknown [[biochemical]] interactions. For example, photo-generated glycan arrays have been used to characterize the [[immunogenic]] properties of a [[tetrasaccharide]] found on the surface of [[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-pathogenhost–pathogen interactionsinteraction]]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 [[Hemagglutininhemagglutinin (influenza)|hemagglutinin]] of the [[Influenzainfluenza 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 customisedcustomized 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 arecan possiblybe combined with other techniques such as [[Surfacesurface Plasmonplasmon Resonanceresonance]] (SPR) to refine the characterisationcharacterization of [[Glycan-proteinglycan–protein interactionsinteraction|glycan-binding]]. For example, this combination led to demonstrate the calcium-dependent [[heparin]] binding of [[Annexinannexin A1]] that is involved in several biological processes including [[inflammation]], [[apoptosis]] and [[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==
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