Evidence that the fusion protein of respiratory syncytial virus exists as a dimer in its native form. Brief report.
The quaternary structure of respiratory syncytial virus (RSV) fusion protein has been studied. Crosslinking studies were done to stabilize the noncovalently associated proteins. These stable, heat-resistant, covalently linked complexes were analyzed by sodium dodecyl sulfate-polyacrylamide electrophoresis. In situ crosslinking studies demonstrated that the fusion protein of RSV exists as a dimer in its native form on the surface of infected cells. The purified protein was also found to be present predominantly as a dimer. In addition, the results suggest that F1 subunits may play a role in the dimerization of the fusion protein.
Praxis Biologics, Virology Research, Rochester, New York.
R G
RG
Arumugham
S W
SW
Hildreth
P R
PR
Paradiso
D000956:Antigens, Viral; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D015707:HN Protein; D011487:Protein Conformation; D012136:Respiratory Syncytial Viruses; D013388:Succinimides; D014759:Viral Envelope Proteins; D014764:Viral Proteins
D000956:Antigens, Viral; D003432:Cross-Linking Reagents; D015707:HN Protein; D013388:Succinimides; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C116204:attachment protein G; C035759:3,3'-dithiobis(sulfosuccinimidyl propionate)