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

作者：Zhuanchang Wu, Zhaoying Zhang, Xin Wang, Jing Zhang, Caiyue Ren, Yuming Li, Lifen Gao, Xiaohong Liang, Pei‐Hui Wang, Chunhong Ma · 发表于：Signal Transduction and Targeted Therapy · 年份：2021 · DOI：10.1038/s41392-021-00651-y · 被引用次数：84 · 研究领域：SARS-CoV-2 and COVID-19 Research、COVID-19 Clinical Research Studies、Computational Drug Discovery Methods

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the unprecedented coronavirus disease 2019 (COVID-19). SARS-CoV-2 entry into host cells is mediated by the viral transmembrane spike (S) glycoprotein that forms homotrimers protruding from the viral surface. S protein comprises two functional subunits S1 and S2, responsible for binding to host receptor angiotensin-converting enzyme 2 (ACE2) and the membrane fusion of SARS-CoV-2 with host cell membranes, respectively. Membrane fusion is necessary for release of viral genome RNA into the host cell cytoplasm. The entry of SARS-CoV-2 is a complex process that requires the concerted action of receptor-binding and proteolytic processing of S protein to promote virus-cell fusion. 1 After cleavage, the heptad repeat 1 (HR1) and 2 (HR2) domains in S2 subunit interact with each other to form a six-helix bundle (6-HB) fusion core and insert into the target cell membrane, thus bringing the viral and cell membrane into close apposition for fusion and infection. 2 However, regulatory mechanisms of S-mediated membrane fusion are still less known.