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The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2

The animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the impact of SARS-CoV-2. Vaccines remain successful at limiting severe disease and death, however the continued emergence of SARS-CoV-2 variants, together with the potential for further coron...

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Autores principales: Allen, Joel D., Ivory, Dylan, Ge Song, Sophie, He, Wan-ting, Capozzola, Tazio, Yong, Peter, Burton, Dennis R., Andrabi, Raiees, Crispin, Max
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9435400/
https://www.ncbi.nlm.nih.gov/pubmed/36052375
http://dx.doi.org/10.1101/2022.08.24.505118
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author Allen, Joel D.
Ivory, Dylan
Ge Song, Sophie
He, Wan-ting
Capozzola, Tazio
Yong, Peter
Burton, Dennis R.
Andrabi, Raiees
Crispin, Max
author_facet Allen, Joel D.
Ivory, Dylan
Ge Song, Sophie
He, Wan-ting
Capozzola, Tazio
Yong, Peter
Burton, Dennis R.
Andrabi, Raiees
Crispin, Max
author_sort Allen, Joel D.
collection PubMed
description The animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the impact of SARS-CoV-2. Vaccines remain successful at limiting severe disease and death, however the continued emergence of SARS-CoV-2 variants, together with the potential for further coronavirus zoonosis, motivates the search for pan-coronavirus vaccines that induce broadly neutralizing antibodies. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of several sarbecovirus glycan shields. Many N-linked glycan attachment sites are shared by all sarbecoviruses, and the processing state of certain sites is highly conserved. However, there are significant differences in the processing state at several glycan sites that surround the receptor binding domain. Our studies reveal similarities and differences in the glycosylation of sarbecoviruses and show how subtle changes in the protein sequence can have pronounced impacts on the glycan shield.
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spelling pubmed-94354002022-09-02 The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2 Allen, Joel D. Ivory, Dylan Ge Song, Sophie He, Wan-ting Capozzola, Tazio Yong, Peter Burton, Dennis R. Andrabi, Raiees Crispin, Max bioRxiv Article The animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the impact of SARS-CoV-2. Vaccines remain successful at limiting severe disease and death, however the continued emergence of SARS-CoV-2 variants, together with the potential for further coronavirus zoonosis, motivates the search for pan-coronavirus vaccines that induce broadly neutralizing antibodies. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of several sarbecovirus glycan shields. Many N-linked glycan attachment sites are shared by all sarbecoviruses, and the processing state of certain sites is highly conserved. However, there are significant differences in the processing state at several glycan sites that surround the receptor binding domain. Our studies reveal similarities and differences in the glycosylation of sarbecoviruses and show how subtle changes in the protein sequence can have pronounced impacts on the glycan shield. Cold Spring Harbor Laboratory 2022-08-25 /pmc/articles/PMC9435400/ /pubmed/36052375 http://dx.doi.org/10.1101/2022.08.24.505118 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
spellingShingle Article
Allen, Joel D.
Ivory, Dylan
Ge Song, Sophie
He, Wan-ting
Capozzola, Tazio
Yong, Peter
Burton, Dennis R.
Andrabi, Raiees
Crispin, Max
The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
title The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
title_full The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
title_fullStr The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
title_full_unstemmed The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
title_short The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2
title_sort diversity of the glycan shield of sarbecoviruses closely related to sars-cov-2
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9435400/
https://www.ncbi.nlm.nih.gov/pubmed/36052375
http://dx.doi.org/10.1101/2022.08.24.505118
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