title: Multiple glycosylated forms of the respiratory syncytial virus fusion protein are expressed in virus-infected cells.
abstract: Analysis of the respiratory syncytial virus (RSV) fusion (F) protein in RSV-infected Vero cells showed the presence of a single F1 subunit and at least two different forms of the F2 subunit, designated F2a (21 kDa) and F2b (16 kDa), which were collectively referred to as [F2](a/b). Enzymatic deglycosylation of [F2](a/b) produced a single 10 kDa product suggesting that [F2](a/b) arises from differences in the glycosylation pattern of F2a and F2b. The detection of [F2](a/b) was dependent upon the post-translational cleavage of the F protein by furin, since its appearance was prevented in RSV-infected Vero cells treated with the furin inhibitor dec-RVKR-cmk. Analysis by protein cross-linking revealed that the F1 subunit interacted with [F2](a/b), via disulphide bonding, to produce equivalent F protein trimers, which were expressed on the surface of infected cells. Collectively, these data show that multiple F protein species are expressed in RSV-infected cells.
authors.affiliation: MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK1.
authors.forename: Helen W McL
authors.initials: HWM
authors.lastname: Rixon
authors.affiliation: MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK1.
authors.forename: Craig
authors.initials: C
authors.lastname: Brown
authors.affiliation: MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK1.
authors.forename: Gaie
authors.initials: G
authors.lastname: Brown
authors.affiliation: MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK1.
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Sugrue
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism; D000818:Animals; D002522:Chlorocebus aethiops; D005643:Fucose / Q000378:metabolism; D005944:Glucosamine / Q000378:metabolism; D006031:Glycosylation; D006367:HeLa Cells; D006801:Humans; D008358:Mannose / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000378:metabolism; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D018113:Respiratory Syncytial Virus, Human / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000096:biosynthesis / Q000378:metabolism*; D014760:Viral Fusion Proteins / Q000096:biosynthesis / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D005643:Fucose; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D005944:Glucosamine; D008358:Mannose