This quantitative relative accessibility analysis, along with the visual inspection of Figure1, suggests that the net structural consequence of FCS is the insertion of a furin cleavage site into Cheng et al. In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into the S1 and S2 subunits is required for activation. The mutations at this site in the spike protein may be of advantage for the virus to undergo proteolytic cleavage by a large number of host enzymes in its evolution. 40 glycoproteins, the spike protein is synthesised as a precursor that must be cleaved in order to perform 41 its membrane fusogenic activity. This study investigated the antiviral potential of targeting furin-mediated SARS-CoV-2 spike (S) protein cleavage. The spike protein of SARS-CoV-2 has a very special feature, a segment of four amino acids called a furin cleavage site. Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity Lanying Du , a Richard Y. Kao , a Yusen Zhou , b Yuxian He , c Guangyu Zhao , a, b Charlotte Wong , a Shibo Jiang , c Kwok-Yung Yuen , a Dong-Yan Jin , d and Bo-Jian Zheng a, This antibody detects full-length protein, and also detects the S1 fragment generated by furin cleavage. This cleavage site helps in opening the virus such that it can easily enter a human cell. (D) Sequence comparison of the spike proteins from SARS-CoV-2, SARS-CoV, and two bat SARS-like coronaviruses in a region at the S1/S2 boundary. SARS-CoV-2 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. Depending on the sequence of spike at the S1/S2 junction, the 42 cleavage occurs during trafficking of spike in Un-til recently, FCoVs were thought to have uncleaved spike Mutation in Spike Protein Cleavage Site and Pathogenesis find that cleavage of the furin substrate site in the viral spike protein is critical for virus production and cytopathic effects. The virus spike protein needs to be in the pre-fusion conformation in order to attach to 1. This would account for its relatively high infection rate and initially mild symptoms. In addition, this protein is highly glycosylated as it contains 21 to 35 N-glycosylation sites. Prior to and after attachment, the S needs to be activated by cellular proteases (e.g. Upon receptor-binding, proteolytic cleavage occurs at S1/S2 cleavage site and two heptad repeats (HR) of S2 stalk form a six-helix bundle structure triggering the release of the fusion peptide. A furin cleavage site allows the virus to use furin in the human body as an enzyme to dissolve its coating so it can release its genetic material to infect cells. In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into the S1 and S2 subunits is required for activation. Introduction of a cleavage site in MHV-2 spike protein induces the formation of syncytia at neutral pH. SARS-CoV-2 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. SARS-CoV-2 spike protein structure. Hoffmann and colleagues show that the pandemic SARS-CoV-2 harbors a highly cleavable S1/S2 cleavage site not found in closely related coronaviruses. In the first phase it infects cells through the furin protein, thanks to its spike protein cleavage. We offer various antigens based on the SARS-CoV-2 spike protein and its subunits: the spike monomer, the spike trimer, the furin cleavage site, the receptor binding domain, as well as the S2 domain. 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