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

Cell Rep. 2023 Mar 15;42(4):112307. doi: 10.1016/j.celrep.2023.112307. Online ahead of print.ABSTRACTAnimal 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.PMID:36972173 | PMC:PMC10015101 | DOI:10.1016/j.celrep.2023.112307

Source: IAVI Rep - March 27, 2023 Category: Infectious Diseases Authors: Joel D Allen Dylan P Ivory Sophie Ge Song Wan-Ting He Tazio Capozzola Peter Yong Dennis R Burton Raiees Andrabi Max Crispin Source Type: research