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The spike (S) glycoprotein is a large, trimeric transmembrane protein found on the surface of SARS-like coronaviruses, including SARS-CoV and SARS-CoV-2. It is the most prominent structural protein and mediates viral entry into host cells by binding to specific cell surface receptors and facilitating membrane fusion. The S glycoprotein assembles as a homotrimer protruding from the viral envelope. Each monomer consists of two main functional subunits: S1 (containing the NTD and RBD, responsible for receptor binding) and S2 (containing elements required for membrane fusion). A furin cleavage site between S1 and S2 allows host proteases to activate the protein. The S glycoprotein is highly immunogenic and a major target of neutralizing antibodies and vaccines. Mutations in the spike protein can affect infectivity, antibody recognition, and vaccine efficacy.
Blockage of receptor binding, inhibition of membrane fusion
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