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The spike glycoprotein (S protein) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a large trimeric membrane protein expressed on the viral surface[1][5][9]. It mediates viral entry by binding to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells, which leads to membrane fusion and delivery of viral genetic material into the cell[1][2][3][4][7]. The S protein is heavily glycosylated, highly immunogenic, and serves as the primary antigenic target for neutralizing antibodies and vaccines against COVID-19[1][3][8]. Structurally, it contains S1 and S2 subunits that are responsible for receptor binding and membrane fusion, respectively, with the receptor-binding domain (RBD) in S1 being crucial for ACE2 attachment[2][3][5][7]. As such, it is the focus of most COVID-19 vaccines and therapeutic antibodies[3][5][8].
Antibody neutralization of receptor-binding domain (RBD) to block ACE2 binding; Vaccine-elicited immunity targeting the spike protein; Inhibition of spike-ACE2 interaction; Inhibition of spike protein fusion activity
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