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The spike (S) protein of Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is a large, trimeric, class I viral fusion glycoprotein that decorates the surface of the virus. It plays a central role in mediating viral entry into host cells and is a primary target for vaccine and therapeutic development. The S protein mediates attachment to ACE2 on human cells via its RBD in S1. After binding, conformational changes trigger cleavage at specific sites by host proteases (e.g., furin or TMPRSS2), separating S1 from S2. The exposed fusion machinery in S2 then facilitates merging of viral and cellular membranes—an essential step for infection. It induces strong humoral (antibody-mediated) and cellular immune responses during infection and is targeted by neutralizing antibodies; thus central to vaccine design efforts against SARS-CoV.
Antibody neutralization of receptor binding; inhibition of membrane fusion
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