Respiratory syncytial virus fusion glycoprotein and attachment glycoprotein (RSV F and RSV G)

The respiratory syncytial virus fusion glycoprotein (F) is a class I viral fusion protein essential for viral entry by mediating the fusion of the viral envelope with the host cell membrane[7]. The F protein is synthesized as an inactive precursor (F0), which is activated by cleavage into F1 and F2 subunits that together form a trimeric structure, exposing the fusion peptide necessary for membrane merger[7][4][5]. The G (attachment) glycoprotein is responsible for viral attachment to host cells, especially ciliated airway epithelial cells, and is characterized by extensive glycosylation and mucin-like domains that aid immune evasion and host cell binding[1][2][9]. Both are major antigens targeted by neutralizing antibodies, and the F protein in particular is the leading antigen for monoclonal antibody therapy and vaccine development in RSV infection[1][3][5][7]. The diversity and post-translational modification of G can complicate immune recognition and vaccine efficacy, whereas the F protein's conserved epitopes are strong candidates for immunization[4][7]. RSV F and G glycoproteins remain primary molecular targets for current and future antiviral drugs and vaccine strategies due to their essential roles in viral infection and host interaction[1][3][5][7].

Other names

RSV F proteinRSV G proteinFusion glycoprotein (F)Attachment glycoprotein (G)

Neutralizing antibodies: Bind key epitopes on F protein to block fusion and entry (palivizumab, motavizumab, nirsevimab); Fusion inhibitors: Prevent conformational changes required for membrane fusion