Abstract

The novel coronavirus SARS-CoV-2, the infective agent causing COVID-19, is having a global impact both in terms of human disease as well as socially and economically. Its heavily glycosylated spike glycoprotein is fundamental for the infection process, via its receptor-binding domains interaction with the glycoprotein angiotensin-converting enzyme 2 on human cell surfaces. We therefore utilized an integrated glycomic and glycoproteomic analytical strategy to characterize both N- and O- glycan site-specific glycosylation within the receptor-binding domain. We demonstrate the presence of complex-type N-glycans with unusual fucosylated LacdiNAc at both sites N331 and N343 and a single site of O-glycosylation on T323.

中文翻译：

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SARS-CoV-2穗糖蛋白受体结合结构域的位点特异性表征

摘要

新型冠状病毒SARS-CoV-2是引起COVID-19的传染因子，在人类疾病以及社会和经济方面均具有全球影响。它的高度糖基化的刺突糖蛋白通过其受体结合结构域与人细胞表面上的糖蛋白血管紧张素转化酶2相互作用，成为感染过程的基础。因此，我们利用整合的糖组学和糖蛋白组学分析策略来表征受体结合域内的N-和O-聚糖位点特异性糖基化。我们展示了复杂类型的N-聚糖与非常规岩藻糖基化的LacdiNAc在两个站点N331和N343以及T323上一个O-糖基化的单个站点的存在。