The RSV F and G glycoproteins interact to form a complex on the surface of infected cells.
In this study, the interaction between the respiratory syncytial virus (RSV) fusion (F) protein, attachment (G) protein, and small hydrophobic (SH) proteins was examined. Immunoprecipitation analysis suggested that the F and G proteins exist as a protein complex on the surface of RSV-infected cells, and this conclusion was supported by ultracentrifugation analysis that demonstrated co-migration of surface-expressed F and G proteins. Although our analysis provided evidence for an interaction between the G and SH proteins, no evidence was obtained for a single protein complex involving all three of the virus proteins. These data suggest the existence of multiple virus glycoprotein complexes within the RSV envelope. Although the stimulus that drives RSV-mediated membrane fusion is unknown, the association between the G and F proteins suggest an indirect role for the G protein in this process.
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
Kit-Wei
KW
Low
Timothy
T
Tan
Ken
K
Ng
Boon-Huan
BH
Tan
Richard J
RJ
Sugrue
D001665:Binding Sites; D006528:Carcinoma, Hepatocellular / Q000821:virology*; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism* / Q000821:virology*; D006801:Humans; D046912:Multiprotein Complexes / Q000378:metabolism; D011485:Protein Binding; D012136:Respiratory Syncytial Viruses / Q000502:physiology*; D014760:Viral Fusion Proteins / Q000378:metabolism*
D046912:Multiprotein Complexes; D014760:Viral Fusion Proteins