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

Chih Feng Tien, Wan Ting Tsai, Chun Hwa Chen, Hui Ju Chou, Mingzi M. Zhang, Jhe Jhih Lin, En Ju Lin, Shih Syong Dai, Yueh Hsin Ping, Chia Yi Yu, Yi Ping Kuo, Wei Hsiang Tsai, Hsin Wei Chen, Guann Yi Yu*


研究成果: Article同行評審

6 引文 斯高帕斯(Scopus)


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 palmitoylation sites. Mutations of clusters I and II disrupt S protein trafficking from ER-to-Golgi, suppress pseudovirus production, and reduce spike-mediated membrane fusion activity. Taken together, glycosylation and palmitoylation orchestrate the S protein maturation processing and are critical for S protein-mediated membrane fusion and infection.

出版狀態Published - 19 8月 2022


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