Biology:Glycan array
Glycan arrays,[1] like that offered by the Consortium for Functional Glycomics (CFG), National Center for Functional Glycomics (NCFG) and Z Biotech, LLC, 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 microarrays. Glycan arrays are composed of various oligosaccharides and/or polysaccharides immobilised on a solid support in a spatially-defined arrangement.[2] This technology provides the means of studying glycan-protein interactions in a high-throughput environment. These natural or synthetic (see carbohydrate synthesis) glycans are then incubated with any glycan-binding protein such as lectins, cell surface receptors or possibly a whole organism such as a virus. Binding is quantified using 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.[3]
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.[4] Hence, glycan array technology can be used to study the specificity of host-pathogen interactions. [5]
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 [6] as well as customised arrays.[7] Cross-platform benchmarks led to highlight the effect of glycan presentation and spacing on binding.[8]
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.[9]
References
- ↑ "Photochemical Micropatterning of Carbohydrates on a Surface". Langmuir 22: 2899–2905. 2006. doi:10.1021/la0531042.
- ↑ "Glycan arrays: recent advances and future challenges". Curr Opin Chem Biol 13 (4): 406–413. Oct 2009. doi:10.1016/j.cbpa.2009.06.021. PMID 19625207.
- ↑ Mehta, Akul Y; Tilton, Catherine A; Muerner, Lukas; von Gunten, Stephan; Heimburg-Molinaro, Jamie; Cummings, Richard D (14 November 2023). "Reusable glycan microarrays using a microwave assisted wet-erase (MAWE) process". Glycobiology. doi:10.1093/glycob/cwad091. PMID 37962922.
- ↑ "Photogenerated glycan arrays identify immunogenic sugar moieties of Bacillus anthracis exosporium". Proteomics 7: 180–184. 2007. doi:10.1002/pmic.200600478.
- ↑ "Glycan arrays as tools for infectious disease research". Curr Opin Chem Biol 18: 38–45. Feb 2014. doi:10.1016/j.cbpa.2013.11.013. PMID 24534751.
- ↑ "Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus". Science 312 (5772): 404–410. Apr 2006. doi:10.1126/science.1124513. PMID 16543414. Bibcode: 2006Sci...312..404S.
- ↑ "Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray". Nat Biotechnol 27 (9): 797–799. Sep 2009. doi:10.1038/nbt0909-797. PMID 19741625.
- ↑ "Cross-platform comparison of glycan microarray formats". Glycobiology 24 (6): 507–17. Jun 2014. doi:10.1093/glycob/cwu019. PMID 24658466.
- ↑ "Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin". Biochemistry 50 (13): 2650–9. Apr 2011. doi:10.1021/bi101121a. PMID 21370880.
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