Glycan array: Difference between revisions

Revision as of 08:38, 9 August 2017

Revision as of 11:35, 9 August 2017

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Glycan arrays, like that offered by the [[Consortium for Functional Glycomics]] (CFG), contain carbohydrate compounds that can be screened with lectins, antibodies or cell receptors to define carbohydrate specificity and identify ligands. Glycan array screening works in much the same way as other microarray that is used for instance to study gene expression [[DNA microarrays]] or protein interaction [[Protein microarray]]s.

Glycan arrays are composed of various [[oligosaccharides]] and/or [[polysaccharides]] immobilised 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=406-413406–413|doi=10.1016/j.cbpa.2009.06.021|pmid=19625207|pmc=PMC2749919 }}</ref> This technology provides the means of studying glycan-protein interactions in ana high-throughput environment. These natural or synthetic (see [[carbohydrate synthesis]]) glycans are then incubated with any glycan-binding protein such as [[lectin]]s, [[cell surface receptor]]s or possibly a whole organism such as a [[virus]]. Binding is quantified using fluorescence-based detection methods.

==Applications==

The glycan array technology has been and still is applied to study the specificity of [[host-pathogen interactions]].

<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=38-4538–45|doi=10.1016/j.cbpa.2013.11.013|pmid=24534751|pmc=}}</ref>

Early on, glycan arrays were proven useful in determining the specificity of the [[Hemagglutinin (influenza)]] of the [[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|pages=404-410404–410|doi=10.1126/science.1124513|pmid=16543414}}</ref> as well as customised 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=797-799797–799|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=507-17507–17|doi=10.1093/glycob/cwu019|pmid= 24658466 |pmc=4001710}}</ref>

Glycan arrays are possibly combined with other techniques such as [[Surface Plasmon Resonance]] (SPR) to refine the characterisation of glycan-binding. For example, this combination led to demonstrate the calcium-dependent heparin binding of [[Annexin 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=2650-92650–9|doi=10.1021/bi101121a|pmid= 21370880 |pmc=3068229}}</ref>

==References==

{{Reflist}}

[[Category:Microarrays ]]

[[Category:Microarrays ]]

[[Category:Glycobiology| ]]

[[Category:Glycomics]]