Principles of SARS-CoV-2 glycosylation
Principles of SARS-CoV-2 glycosylation
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.
Chawla, Himanshi
07b9e983-4c35-4314-999d-fe3222a6c03b
Fadda, Elisa
93020f1b-a98f-4f07-ab6c-4a1cc3810ba5
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
August 2022
Chawla, Himanshi
07b9e983-4c35-4314-999d-fe3222a6c03b
Fadda, Elisa
93020f1b-a98f-4f07-ab6c-4a1cc3810ba5
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Chawla, Himanshi, Fadda, Elisa and Crispin, Max
(2022)
Principles of SARS-CoV-2 glycosylation.
Current Opinion in Structural Biology, 75, [102402].
(doi:10.1016/j.sbi.2022.102402).
Abstract
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.
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e-pub ahead of print date: 19 May 2022
Published date: August 2022
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This work was supported by the International AIDS Vaccine Initiative (IAVI) through the Collaboration for AIDS Vaccine Discovery (CAVD) grant, INV-008352/OPP1153692 funded by the Bill and Melinda Gates Foundation . The Science Foundation of Ireland ( 20/FFP-P/8809 ) is gratefully acknowledged for financial support. The opinions, findings and conclusions or recommendations expressed in this material are those of the author(s) and do not necessarily reflect the views of the Science Foundation Ireland.
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© 2022 The Authors
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Local EPrints ID: 470423
URI: http://eprints.soton.ac.uk/id/eprint/470423
ISSN: 0959-440X
PURE UUID: b3dd306d-faa6-413d-9462-22c52f09713d
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Date deposited: 10 Oct 2022 16:58
Last modified: 17 Mar 2024 03:57
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Elisa Fadda
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