4.7 Letter

Palmitoylation of SARS-CoV-2 S protein is essential for viral infectivity

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Summary: The SARS-CoV-2 spike glycoprotein has evolved features such as the furin cleavage site and D614G mutation to balance virus infectivity, stability, cytopathicity, and antibody vulnerability, while the endodomain of the S2 subunit is not essential for virus entry or syncytium formation. Metalloprotease inhibitors can suppress S-mediated cell-cell fusion, but not virus entry, suggesting a role for host proteases in activating the S glycoprotein during syncytium formation. This understanding of SARS-CoV-2 S glycoprotein interactions with host cells provides insights into virus transmission and pathogenicity.

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