The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. 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 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response.
CP: Immunology, CP: Microbiology, glycan shielding, N-linked glycosylation, pan-coronavirus, SARS-CoV-2
112307
Allen, Joel D.
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Ivory, Dylan P.
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Song, Sophie Ge
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He, Wan-ting
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Capozzola, Tazio
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Yong, Peter
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Burton, Dennis R.
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Andrabi, Raiees
b2a7432d-df2b-4d79-bfeb-00d3b02ec65c
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
25 April 2023
Allen, Joel D.
c89d5569-7659-4835-b535-c9586e956b3a
Ivory, Dylan P.
e8a77800-8dc7-4272-ab28-060de46bb278
Song, Sophie Ge
c542b4d8-32f5-49c0-9607-eca981e31b96
He, Wan-ting
c532ea3d-67d9-4791-a3a8-3eec756f19c2
Capozzola, Tazio
f019dbc2-f175-4ea2-8513-677c50a16d48
Yong, Peter
e2b2764a-3285-4211-9a75-dc9f538ef6a2
Burton, Dennis R.
a628ce77-b694-4e3c-86a5-11f4e20e1c7c
Andrabi, Raiees
b2a7432d-df2b-4d79-bfeb-00d3b02ec65c
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Allen, Joel D., Ivory, Dylan P., Song, Sophie Ge, He, Wan-ting, Capozzola, Tazio, Yong, Peter, Burton, Dennis R., Andrabi, Raiees and Crispin, Max
(2023)
The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2.
Cell Reports, 42 (4), , [112307].
(doi:10.1016/j.celrep.2023.112307).
Abstract
Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. 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 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response.
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e-pub ahead of print date: 15 March 2023
Published date: 25 April 2023
Additional Information:
Funding Information:
This work was supported by the International AIDS Vaccine Initiative (IAVI) through grant INV-008352/OPP1153692 funded by the Bill and Melinda Gates Foundation (to M.C.). We also gratefully acknowledge support from the University of Southampton Coronavirus Response Fund (to M.C.), a donation from the Bright Future Trust (to M.C), NIH NIAID CHAVD (UM1 AI44462 to D.R.B.), NIH NIAID ( R01AI170928 to R.A.), the IAVI Neutralizing Antibody Center, and the Bill and Melinda Gates Foundation (OPP 1170236 and INV-004923 to D.R.B.). This work was also supported by the John and Mary Tu Foundation and the James B. Pendleton Charitable Trust (to D.R.B.).
Publisher Copyright:
© 2023 The Author(s)
Keywords:
CP: Immunology, CP: Microbiology, glycan shielding, N-linked glycosylation, pan-coronavirus, SARS-CoV-2
Identifiers
Local EPrints ID: 476074
URI: http://eprints.soton.ac.uk/id/eprint/476074
ISSN: 2211-1247
PURE UUID: c873be24-4026-400a-b9ce-975554dde68f
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Date deposited: 12 Apr 2023 10:26
Last modified: 06 Jun 2024 02:11
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Contributors
Author:
Dylan P. Ivory
Author:
Sophie Ge Song
Author:
Wan-ting He
Author:
Tazio Capozzola
Author:
Peter Yong
Author:
Dennis R. Burton
Author:
Raiees Andrabi
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