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Biotechnol J. 2015 Jan;10(1):199-209. doi: 10.1002/biot.201400354. Epub 2014 Oct 31.

Glycoarrays with engineered phages displaying structurally diverse oligosaccharides enable high-throughput detection of glycan-protein interactions.

Author information

1
School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA; Department of Chemical Engineering, Hacettepe University, Beytepe, Ankara, Turkey; Bioengineering Division, Institute of Science, Hacettepe University, Beytepe, Ankara, Turkey.

Abstract

Glycan microarrays have become a powerful platform to investigate the interactions of carbohydrates with a variety of biomolecules. However, the number and diversity of glycans available for use in such arrays represent a key bottleneck in glycan array fabrication. To address this challenge, we describe a novel glycan array platform based on surface patterning of engineered glycophages that display unique carbohydrate epitopes. Specifically, we show that glycophages are compatible with surface immobilization procedures and that phage-displayed oligosaccharides retain the ability to be recognized by different glycan-binding proteins (e.g. antibodies and lectins) after immobilization. A key advantage of glycophage arrays is that large quantities of glycophages can be produced biosynthetically from recombinant bacteria and isolated directly from bacterial supernatants without laborious purification steps. Taken together, the glycophage array technology described here should help to expand the diversity of glycan libraries and provide a complement to the existing toolkit for high-throughput analysis of glycan-protein interactions.

KEYWORDS:

Filamentous phage; Functional glycomics; Glycan-binding protein; Glycoarray; Lectin

PMID:
25263089
PMCID:
PMC4314398
DOI:
10.1002/biot.201400354
[Indexed for MEDLINE]
Free PMC Article

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