Abstract
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.
Original language | English |
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Pages (from-to) | 308-313 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 366 |
Issue number | 2 |
DOIs | |
Publication status | Published - Feb 8 2008 |
Externally published | Yes |
ASJC Scopus Subject Areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Keywords
- Attachment protein
- Biotinylation
- Fusion protein
- Protein cross-linking
- Respiratory syncytial virus
- Surface labelling
- Virus glycoproteins