Fusion glycoprotein of respiratory syncytial virus (RSV F)

The **fusion glycoprotein of respiratory syncytial virus (RSV F)** is a **class I viral fusion protein** and a key envelope glycoprotein on the surface of RSV virions[4][5][7][8]. Synthesized as an inactive precursor (F0), RSV F undergoes proteolytic cleavage by host cell furin-like proteases, generating two subunits (F1 and F2) linked by disulfide bonds; activation exposes a hydrophobic fusion peptide critical for merging the viral envelope with host cell membranes[1][2][3][4]. Structurally, RSV F exists in a metastable prefusion form and a stable postfusion form, with neutralizing epitopes preferentially presented in the prefusion state[6][8]. The F protein is highly conserved, serves as the main target for neutralizing antibodies, and is the basis of several therapeutic monoclonal antibodies and vaccines for RSV prevention and treatment[5][7]. The protein’s function is essential for initiating RSV infection by enabling viral entry through membrane fusion, and it also promotes syncytium formation, facilitating viral spread[1][4][5][8].\n\nRSV F’s high importance as a drug target is reflected by its critical role in RSV disease pathogenesis and as the primary antigen for recent RSV vaccine approvals. Antibody- and vaccine-based interventions specifically targeting the prefusion conformation of RSV F show potent clinical efficacy[5][6][7][8].

Other names

Fusion protein of RSVRSV fusion glycoproteinF proteinRSV F proteinFusion glycoprotein

Neutralizing antibodies bind the prefusion conformation of F, preventing conformational changes required for membrane fusion and viral entry[5][7][8]. Some antibodies block fusion peptide exposure or trimer dissociation, stabilizing F in a non-fusogenic state[5][6][8]. Vaccines elicit antibodies that target specific exposed antigenic sites on the prefusion F protein, blocking infection[5][6][7].