Glycosylation and S-palmitoylation regulate SARS-CoV-2 spike protein intracellular trafficking.

ABSTRACT: Post-translational modifications (PTMs), such as glycosylation and palmitoylation, are critical to protein folding, stability, intracellular trafficking, and function. Understanding regulation of PTMs of SARS-CoV-2 spike (S) protein could help the therapeutic drug design. Herein, the VSV vector was used to produce SARS-CoV-2 S pseudoviruses to examine the roles of the ⁶¹¹LYQD⁶¹⁴ and cysteine-rich motifs in S protein maturation and virus infectivity. Our results show that ⁶¹¹LY⁶¹² mutation alters S protein intracellular trafficking and reduces cell surface expression level. It also changes S protein glycosylation pattern and decreases pseudovirus infectivity. The S protein contains four cysteine-rich clusters with clusters I and II as the main pal

SUBMITTER: Tien CF 

PROVIDER: S-EPMC9250814 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature