【摘 要】
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Dear Editor,rnSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)has become a severe threat to global health.1 The spike (S) protein on the surface of SARS-CoV-2 exploits angiotensin-converting enzyme 2 (ACE2) as cellular receptor and mediates th
【机 构】
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Center for Infectious Disease Research,Westlake Laboratory of Life Sciences and Biomedicine,Key Labo
论文部分内容阅读
Dear Editor,rnSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)has become a severe threat to global health.1 The spike (S) protein on the surface of SARS-CoV-2 exploits angiotensin-converting enzyme 2 (ACE2) as cellular receptor and mediates the fusion of the viral and the host cell membrane during infection.1,2 The activation of the S protein requires the receptor-binding domain(RBD) binding to the peptidase domain (PD) of ACE2 and the cleavage by host proteases into the N-terminal S1 subunit and the C-terminal S2 subunit.2-4 An additional furin cleavage site “RRAR”present in the S1/S2 cleavage region of SARS-CoV-2,which is absent in SARS-CoV that shares about 80％ sequence identity with SARS-CoV-2 and caused an epidemic in 2002-2003,might help accelerate the activation of the S protein.S1 consists of the N-terminal domain (NTD),the RBD,subdomain 1 and 2 (SD1 andSD2).
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