Respiratory Syncytial Virus Fusion glycoprotein F0 (RSV F)

The Respiratory Syncytial Virus Fusion glycoprotein F0 (RSV F) is one of the two major glycoproteins on the surface of the RSV virion, alongside the attachment glycoprotein (G)[1][2]. RSV F is a membrane-anchored glycoprotein that mediates viral entry into host cells by causing the virion membrane to fuse with the target cell membrane[1][4]. RSV F is synthesized as an inactive precursor (F0) that is processed by furin-like proteases at two sites to generate three polypeptides: the N-terminal fragment (F2), a 27-amino-acid glycopeptide (pep27), and the C-terminal fragment (F1)[6]. The mature, active protein exists as a trimer of F2-F1 heterodimers, folded into a compact prefusion conformation (pre-F) on the viral envelope[6]. The F protein undergoes dramatic structural rearrangements during the fusion process, transitioning from a metastable prefusion form to a highly stable postfusion conformation[3][4]. This conformational change is essential for viral entry, as it brings the viral and cellular membranes into close proximity, allowing fusion to occur[4]. The F1 subunit contains all the elements needed to promote fusion, including the fusion peptide (FP), two heptad repeats, and the transmembrane domain[6]. The RSV F protein contains three N-linked glycosylation sites (at positions N27, N70, and N500) and seven disulfide bonds, four of which are highly conserved across the Paramyxoviridae family[3][5]. The protein is the major target for antiviral drug development and is one of the primary antigens targeted by neutralizing antibodies induced by infection[1][2]. RSV F can promote fusion in cell culture without the G protein, although the G protein targets the ciliated cells of the airways during natural infection[1][5]. The protein contains multiple neutralizing epitopes, making it an important target for vaccine development[4][6].

Other names

F glycoproteinRSV Fusion proteinF0 glycoprotein

Neutralizing antibodies bind to specific epitopes on the F protein, preventing conformational changes required for fusion Fusion inhibitors prevent the structural rearrangement from prefusion to postfusion conformation