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.
Keywords: Characterization; O-Glycosylation; Sialylation; Spike proteins; β-coronavirus.
【저자키워드】 Spike proteins, characterization, O-glycosylation, β-coronavirus., Sialylation, 【초록키워드】 Biological functions, SARS-CoV-2, Vaccine, spike, Spike protein, antiviral drug, D614G, membrane fusion, mutant, Coronavirus-2, S1 subunit, Analysis, acute respiratory syndrome, domains, cell entry, N-glycosylation, S proteins, help, S1 protein, β-CoVs, β-CoV, β-coronavirus, FIVE, characterized, functional, less, glycosylated, 【제목키워드】 Recombinant spike protein, Analysis, β-coronavirus, FIVE,