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The Respiratory syncytial virus (RSV) fusion (F) glycoprotein is a critical surface protein responsible for mediating viral entry into host cells by facilitating the fusion of the viral envelope with the host cell membrane (UniProt: P03420). Antigenic site II is a highly conserved, discontinuous epitope located on the F1 subunit of the F protein, which is present in both the pre-fusion and post-fusion conformations (PubMed: 23640882). This site is the primary target for Palivizumab, the first monoclonal antibody approved for the prevention of severe RSV disease in high-risk infants (PubMed: 9371549). By binding to site II, therapeutic antibodies sterically hinder the structural rearrangements of the F protein required for membrane fusion, effectively neutralizing the virus (PubMed: 17449884).}
Monoclonal antibodies bind to antigenic site II on the RSV F protein, preventing the conformational change from the pre-fusion to the post-fusion state, thereby inhibiting viral-cell membrane fusion and viral entry.
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