Cell-based glycan arrays for probing glycan–glycan binding protein interactions

Jennie Grace Briard, Hao Jiang, Kelley W. Moremen, Matthew Scott Macauley () and Peng Wu ()
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Jennie Grace Briard: The Scripps Research Institute
Hao Jiang: Ocean University of China
Kelley W. Moremen: University of Georgia
Matthew Scott Macauley: The Scripps Research Institute
Peng Wu: The Scripps Research Institute

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract Glycan microarrays provide a high-throughput means of profiling the interactions of glycan-binding proteins with their ligands. However, the construction of current glycan microarray platforms is time consuming and expensive. Here, we report a fast and cost-effective method for the assembly of cell-based glycan arrays to probe glycan–glycan-binding protein interactions directly on the cell surface. Chinese hamster ovary cell mutants with a narrow and relatively homogeneous repertoire of glycoforms serve as the foundation platforms to develop these arrays. Using recombinant glycosyltransferases, sialic acid, fucose, and analogs thereof are installed on cell-surface glycans to form cell-based arrays displaying diverse glycan epitopes that can be probed with glycan-binding proteins by flow cytometry. Using this platform, high-affinity glycan ligands are discovered for Siglec-15—a sialic acid-binding lectin involved in osteoclast differentiation. Incubating human osteoprogenitor cells with cells displaying a high-affinity Siglec-15 ligand impairs osteoclast differentiation, demonstrating the utility of this cell-based glycan array technology.

Date: 2018
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DOI: 10.1038/s41467-018-03245-5

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