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On December 21, the Meng Guangxun group of the Shanghai Pasteur Institute of the Chinese Academy of Sciences andThe Dimitri Lavillette team published a research paper SARS-CoV-2 spike engagement of ACE2 primes S2' site cleavage and fusion initiation in the international academic journal "Proceedings of the National Academy of Sciences"
.
The COVID-19 pandemic caused by the new coronavirus (SARS-CoV-2) infection has caused more than 275 million infections worldwide
.
The SARS-CoV-2 spike protein is not only functionally responsible for recognizing the receptors on the host cell, but also mediating the fusion of the cell membrane with the viral envelope, resulting in the virus infecting the host cell
The SARS-CoV-2 S protein monomer contains two fragments: the amino-terminal S1 subunit contains a receptor binding domain (RBD), which recognizes the host ACE2 receptor for initial docking; and the carboxy-terminal S2 subunit catalyzes viral and The fusion of the cell membrane allows the subsequent viral RNA genome to enter the infected cell for replication
.
In this study, researchers used a cell-cell fusion system and a pseudovirus infection model and found that after the spike protein binds to the receptor, it initiates a protease cleavage reaction in the cell, leading to the generation of S2' fragments and membrane fusion
This research work was mainly completed by Shanghai Pasteur Institute postdoctoral researcher Yu Shi, doctoral student Zheng Xu, etc.
under the joint guidance of Meng Guangxun and Dimitri Lavillette researcher; Shanghai Pasteur Institute researcher Wang Songji co-participated in this research
.
The research was supported by the China Postdoctoral Fund, the National Natural Science Foundation of China, the Chinese Academy of Sciences, Shanghai, and the Ministry of Science and Technology
Link to the paper: https://