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Updated: Aug 26, 2025

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Published on: June 14, 2022
Systematic analysis and comparison of O-glycosylation of five recombinant spike proteins in β-coronaviruses
Xuefang Dong1, Xiuling Li2, Cheng Chen1
1Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Abstract:
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.
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