ArticleNature communications2024
Sequential glycosylations at the multibasic cleavage site of SARS-CoV-2 spike protein regulate viral activity.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Central role of glycosylation processes in human genetic susceptibility to SARS-CoV-2 infections with Omicron variants.Nature genetics · 2026Article
- Interferon-stimulated gene GALNT2 restricts respiratory virus infections.Nature microbiology · 2026Article
- Data Processing and Analysis in Positional Proteomics.Proteomics · 2025Review
- O-GlcNAcylation at S659 enhances SARS-CoV-2 spike protein stability and pseudoparticle packaging efficiency.Microbiology spectrum · 2025Article
- SARS-CoV-2 ORF3a drives dynamic dense body formation for optimal viral infectivity.Nature communications · 2025Article
- The Binding of Brazilin fromInternational journal of molecular sciences · 2025Article
- Article
- SUMOylation of SARS-CoV-2 spike protein is a key target for broad-spectrum antiviral therapy.Theranostics · 2025Article
- Pre-pandemic artificial MERS analog of polyfunctional SARS-CoV-2 S1/S2 furin cleavage site domain is unique among spike proteins of genus Betacoronavirus.BMC genomic data · 2024Article
- O-glycosylation of SARS-CoV-2 spike protein by host O-glycosyltransferase strengthens its trimeric structure.Acta biochimica et biophysica Sinica · 2024Article
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Authors and funding
21 authors.
Funding
Abstract
The multibasic furin cleavage site at the S1/S2 boundary of the spike protein is a hallmark of SARS-CoV-2 and plays a crucial role in viral infection. However, the mechanism underlying furin activation and its regulation remain poorly understood. Here, we show that GalNAc-T3 and T7 jointly initiate clustered O-glycosylations in the furin cleavage site of the SARS-CoV-2 spike protein, which inhibit furin processing, suppress the incorporation of the spike protein into virus-like-particles and affect viral infection. Mechanistic analysis reveals that the assembly of the spike protein into virus-like particles relies on interactions between the furin-cleaved spike protein and the membrane protein of SARS-CoV-2, suggesting a possible mechanism for furin activation. Interestingly, mutations in the spike protein of the alpha and delta variants of the virus confer resistance against glycosylation by GalNAc-T3 and T7. In the omicron variant, additional mutations reverse this resistance, making the spike protein susceptible to glycosylation in vitro and sensitive to GalNAc-T3 and T7 expression in human lung cells. Our findings highlight the role of glycosylation as a defense mechanism employed by host cells against SARS-CoV-2 and shed light on the evolutionary interplay between the host and the virus.
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