Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein part 11



The distal S1 subunit comprices the receptor-binding domain(s) and contributes to stabilization of the prefusion state of the membrane-anchored S2 subunit that contains the fusion machinery. For all CoVs, S is further cleaved by host proteases at the so-called S2 site located immediately upstream of the fusion peptide. This cleavage has been proposed to activate the protein for membrane fusion via extensive irreversible conformational changes.  As a result, coronavirus entry into susceptible cells  is a complex process that requires the concerted action of receptor-binding  and proteolytic processing of the S protein to promote virus-cell fusion.

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