α-Dystroglycan (α-DG) is uniquely modified on O-mannose sites by a repeating disaccharide (-Xylα1,3-GlcAβ1,3-)_n 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-linked glycoprotein was converted into a IIH6-positive Laminin-binding glycoprotein. Engineering of the surface of cells deficient for either α-DG or O-mannosylation with matriglycans of sufficient length recovers infection with a Lassa-pseudovirus. Finally, free matriglycan in a dose and length dependent manner inhibits viral infection of wildtype cells. These results indicate that matriglycan alone is necessary and sufficient for IIH6 staining, Laminin and LASV GP1 binding, and Lassa-pseudovirus infection and support a model in which it is a tunable receptor for which increasing chain length enhances ligand-binding capacity.

α-Dystroglycan (α-DG)通过重复二糖 (-Xylα1,3-GlcAβ1,3-)在O -甘露糖位点进行独特修饰，_称为基质聚糖，它是含有层粘连蛋白-G 结构域的蛋白质的受体，被用于用于感染的旧世界沙粒病毒。我们使用化学酶法合成的基质聚糖作为微阵列打印，展示了与层粘连蛋白、拉沙病毒 GP1 和临床重要抗体 IIH6 的长度依赖性结合。利用酶工程方法，将N连接糖蛋白转化为 IIH6 阳性层粘连蛋白结合糖蛋白。缺乏 α-DG 或O的细胞表面工程-具有足够长度的基质聚糖的甘露糖基化恢复了拉沙假病毒的感染。最后，游离基质聚糖以剂量和长度依赖性方式抑制野生型细胞的病毒感染。这些结