Prefusion respiratory syncytial virus fusion glycoprotein (RSV F (prefusion))

The prefusion respiratory syncytial virus fusion glycoprotein is a **surface viral glycoprotein** found on the envelope of respiratory syncytial virus (RSV), existing in a metastable prefusion conformation prior to facilitating fusion of the viral and host cell membranes[1][2][3][4][6]. As a **class I viral fusion protein**, it comprises three F protein subunits assembled into a trimer and mediates the critical step of membrane fusion required for RSV entry into host cells[2][3][6]. The prefusion conformation exposes highly neutralization-sensitive antigenic sites, making it a major target for both **monoclonal antibody therapies** (e.g. nirsevimab, palivizumab) and the basis for current RSV vaccine design[3][4][6]. Structural rearrangement from the prefusion to postfusion state is essential for viral infectivity, and drugs that stabilize the prefusion form effectively inhibit infection. Mutations or modifications in this protein and its epitopes can impact disease severity, transmission, and the effectiveness of therapeutic or prophylactic interventions[3][4][6].

Other names

Respiratory syncytial virus fusion glycoprotein prefusion formRSV F protein prefusionPre-F RSV FPre-fusion Fprefusion F

Neutralization by monoclonal antibodies that block membrane fusion Small molecules that stabilize prefusion conformation and prevent conformational change required for fusion