Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China; Ganjiang Chinese Medicine Innovation Center, Nanchang, 330000, PR China.
Anal Chim Acta. 2022 Oct 16;1230:340394. doi: 10.1016/j.aca.2022.340394. Epub 2022 Sep 16.
β-coronaviruses (β-CoVs), representative with severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), depend on their highly glycosylated spike proteins to mediate cell entry and membrane fusion. Compared with the extensively identified N-glycosylation, less is known about O-glycosylation of β-CoVs S proteins, let alone its biological functions. Herein we comprehensively characterized O-glycosylation of five recombinant β-CoVs S1 subunits and revealed the macro- and micro-heterogeneity nature of site-specific O-glycosylation. We also uncovered the O-glycosylation differences between SARS-CoV-2 and its natural D614G mutant on functional domains. This work describes the systematic O-glycosylation analysis of β-CoVs S1 proteins and will help to guide the related vaccines and antiviral drugs development.
β 冠状病毒（β-CoVs），以严重急性呼吸系统综合征冠状病毒 2 型（SARS-CoV-2）为代表，依赖其高度糖基化的刺突蛋白来介导细胞进入和膜融合。与广泛鉴定的 N-糖基化相比，β-CoVs S 蛋白的 O-糖基化知之甚少，更不用说其生物学功能了。在此，我们全面描述了 5 种重组β-CoV S1 亚基的 O-糖基化，并揭示了 O-糖基化在特定位点的宏观和微观异质性。我们还揭示了 SARS-CoV-2 与其天然 D614G 突变体在功能域上的 O-糖基化差异。这项工作描述了对β-CoVs S1 蛋白的系统 O-糖基化分析，将有助于指导相关疫苗和抗病毒药物的开发。
