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Zhang, Liping; Mann, Matthew; Syed, Zulfeqhar A; Reynolds, Hayley M; Tian, E; Samara, Nadine L; Zeldin, Darryl C; Tabak, Lawrence A; Ten Hagen, Kelly G
Proceedings of the National Academy of Sciences - PNAS, 11/2021, Letnik: 118, Številka: 47Journal Article
The SARS-CoV-2 coronavirus responsible for the global pandemic contains a novel furin cleavage site in the spike protein (S) that increases viral infectivity and syncytia formation in cells. Here, we show that -glycosylation near the furin cleavage site is mediated by members of the GALNT enzyme family, resulting in decreased furin cleavage and decreased syncytia formation. Moreover, we show that -glycosylation is dependent on the novel proline at position 681 (P681). Mutations of P681 seen in the highly transmissible alpha and delta variants abrogate -glycosylation, increase furin cleavage, and increase syncytia formation. Finally, we show that GALNT family members capable of glycosylating S are expressed in human respiratory cells that are targets for SARS-CoV-2 infection. Our results suggest that host -glycosylation may influence viral infectivity/tropism by modulating furin cleavage of S and provide mechanistic insight into the role of the P681 mutations found in the highly transmissible alpha and delta variants.
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