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    Principles of SARS-CoV-2 glycosylation

    Chawla, Himanshi and Fadda, Elisa and Crispin, Max (2022) Principles of SARS-CoV-2 glycosylation. Current Opinion in Structural Biology, 75 (102402). pp. 1-9. ISSN 0959-440X

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    The structure and post-translational processing of the SARS-CoV-2 spike glycoprotein (S) is intimately associated with the function of the virus and of sterilising vaccines. The surface of the S protein is extensively modified by glycans, and their biosynthesis is driven by both the wider cellular context, and importantly, the underlining protein structure and local glycan density. Comparison of virally derived S protein with both recombinantly derived and adenovirally induced proteins, reveal hotspots of protein-directed glycosylation that drive conserved glycosylation motifs. Molecular dynamics simulations revealed that, while the S surface is extensively shielded by N-glycans, it presents regions vulnerable to neutralising antibodies. Furthermore, glycans have been shown to influence the accessibility of the receptor binding domain and the binding to the cellular receptor. The emerging picture is one of unifying, principles of S protein glycosylation and an intimate role of glycosylation in immunogen structure and efficacy.

    Item Type: Article
    Keywords: Principles; SARS; CoV-2; glycosylation;
    Academic Unit: Faculty of Science and Engineering > Chemistry
    Faculty of Science and Engineering > Research Institutes > Hamilton Institute
    Faculty of Science and Engineering > Research Institutes > Human Health Institute
    Item ID: 17866
    Identification Number:
    Depositing User: Elisa Fadda
    Date Deposited: 21 Nov 2023 14:48
    Journal or Publication Title: Current Opinion in Structural Biology
    Publisher: Elsevier
    Refereed: Yes
    Use Licence: This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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