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The fusion glycoprotein F (RSV-F) is a major surface protein of the human respiratory syncytial virus (RSV) essential for viral entry. It mediates membrane fusion between the viral envelope and host cell membrane. Synthesized as an inactive precursor F0, it is cleaved into F1 and F2 subunits forming a trimeric functional form. The prefusion conformation is a metastable state exposing key antigenic sites for neutralizing antibody recognition, making it a crucial target for vaccine development. RSV-F facilitates fusion during initial infection and cell-to-cell spread via syncytium formation. The prefusion conformation contains six major antigenic sites (Ø and I–V). Stabilization of RSV-F in its prefusion form is pivotal for effective RSV vaccine design. It is encoded by the *F* gene on the negative-sense RNA genome and is relatively conserved among strains.
Neutralizing antibody binding to prefusion-specific epitopes to prevent membrane fusion.
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