tetano
Editor, Senior Moderator
Cell Rep
. 2023 Mar 15;42(4):112307.
doi: 10.1016/j.celrep.2023.112307. Online ahead of print.
The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
Joel D Allen[SUP] 1 [/SUP], Dylan P Ivory[SUP] 2 [/SUP], Sophie Ge Song[SUP] 3 [/SUP], Wan-Ting He[SUP] 3 [/SUP], Tazio Capozzola[SUP] 3 [/SUP], Peter Yong[SUP] 3 [/SUP], Dennis R Burton[SUP] 4 [/SUP], Raiees Andrabi[SUP] 3 [/SUP], Max Crispin[SUP] 5 [/SUP]
Affiliations
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.
Keywords: CP: Immunology; CP: Microbiology; N-linked glycosylation; SARS-CoV-2; glycan shielding; pan-coronavirus.
. 2023 Mar 15;42(4):112307.
doi: 10.1016/j.celrep.2023.112307. Online ahead of print.
The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
Joel D Allen[SUP] 1 [/SUP], Dylan P Ivory[SUP] 2 [/SUP], Sophie Ge Song[SUP] 3 [/SUP], Wan-Ting He[SUP] 3 [/SUP], Tazio Capozzola[SUP] 3 [/SUP], Peter Yong[SUP] 3 [/SUP], Dennis R Burton[SUP] 4 [/SUP], Raiees Andrabi[SUP] 3 [/SUP], Max Crispin[SUP] 5 [/SUP]
Affiliations
- PMID: 36972173
- 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.
Keywords: CP: Immunology; CP: Microbiology; N-linked glycosylation; SARS-CoV-2; glycan shielding; pan-coronavirus.