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Cell Surface Glycoengineering - HAP1 Cells

ABSTRACT: Cell Surface Glycoengineering of HAP1 Cells using CMP-Neu5Ac Derivatives

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: M. Osman Sheikh

LAB HEAD: Dr. Lance Wells

PROVIDER: PXD024251 | Pride | 2022-06-26

REPOSITORIES: Pride

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			Action	DRS
	1-ProteomicsResultsSummary.xlsx	Xlsx
	20180828-18mer-SEEL.1PerProNoContams_results.txt	Txt
	DAG1-18mer-1.raw	Raw
	DAG1-18mer-2.raw	Raw
	DAG1-18mer-3.raw	Raw

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Publications

Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function.

Sheikh M Osman MO Capicciotti Chantelle J CJ Liu Lin L Praissman Jeremy J Ding Dahai D Mead Daniel G DG Brindley Melinda A MA Willer Tobias T Campbell Kevin P KP Moremen Kelley W KW Wells Lance L Boons Geert-Jan GJ

Nature communications 20220624 1

α-Dystroglycan (α-DG) is uniquely modified on O-mannose sites by a repeating disaccharide (-Xylα1,3-GlcAβ1,3-)<sub>n</sub> termed matriglycan, which is a receptor for laminin-G domain-containing proteins and employed by old-world arenaviruses for infection. Using chemoenzymatically synthesized matriglycans printed as a microarray, we demonstrate length-dependent binding to Laminin, Lassa virus GP1, and the clinically-important antibody IIH6. Utilizing an enzymatic engineering approach, an N-link ...[more]

PMID: 35750689

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