Functional analysis of the N-linked glycans within the fusion protein of respiratory syncytial virus.
The respiratory syncytial virus fusion (F) protein is initially expressed as a single polypeptide chain (F0). The F0 subsequently undergoes posttranslational cleavage-by-cell protease activity to produce the F1 and F2 subunits. Each of the two subunits within the mature F protein is modified by the addition of N-linked glycans. The individual N-linked glycans on the F protein were selectively removed by using site-directed mutagenesis to mutate the individual glycan-acceptor sites. In this way the role of these individual glycans in targeting of the F protein to the cell surface, and on the ability of the F protein to induce membrane fusion, was examined.
Li
Ping
P
MRC Virology Unit, Institute of Virology, Glasgow, UK.
McL Rixon
Helen W
HW
Brown
Gaie
G
Sugrue
Richard J
RJ
D000818:Animals; D002522:Chlorocebus aethiops; D006367:HeLa Cells; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology*; D011134:Polysaccharides / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism*; D012136:Respiratory Syncytial Viruses / Q000235:genetics / Q000378:metabolism*; D014709:Vero Cells; D014760:Viral Fusion Proteins / Q000235:genetics / Q000378:metabolism*
D011134:Polysaccharides; D021122:Protein Subunits; D014760:Viral Fusion Proteins