國家衛生研究院 NHRI:Item 3990099045/14409
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    題名: Glycosylation and S-palmitoylation regulate SARS-CoV-2 spike protein intracellular trafficking
    作者: Tien, CF;Tsai, WT;Chen, CH;Chou, HJ;Zhang, MM;Lin, JJ;Lin, EJ;Dai, SS;Ping, YH;Yu, CY;Kuo, YP;Tsai, WH;Chen, HW;Yu, GY
    貢獻者: National Institute of Infectious Diseases and Vaccinology;Institute of Molecular and Genomic Medicine
    摘要: 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 (611)LYQD(614) and cysteine-rich motifs in S protein maturation and virus infectivity. Our results show that (LY612)-L-611 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.
    日期: 2022-08-19
    關聯: iScience. 2022 Aug 19;25(8):Article number 104709.
    Link to: http://dx.doi.org/10.1016/j.isci.2022.104709
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=2589-0042&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000828908700005
    Cited Times(Scopus): https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85134544514
    顯示於類別:[余冠儀] 期刊論文
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