Studies with cross-linking reagents on the oligomeric form of the paramyxovirus fusion protein.
The oligomeric form of the paramyxovirus simian virus 5 (SV5) fusion (F) glycoprotein has been examined by using chemical cross-linking and sucrose density gradient fractionation. In addition, chemical cross-linking was used to examine the kinetics of assembly of the F oligomer. Analysis by SDS-PAGE on 3.5% gels of the cross-linked F molecules indicated three major species with calculated molecular weights of M(r) approximately 65, M(r) approximately 130, and M(r) approximately 195 kDa, suggesting F monomers, dimers, and trimers, respectively. The cross-linked F species of M(r) approximately 195 kDa migrated on gels faster than influenza virus hemagglutinin trimers and between the dimeric and tetrameric forms of paramyxovirus hemagglutinin-neuraminidase (HN). Furthermore, the F protein oligomer was found to sediment slower than the HN tetramer on sucrose gradient centrifugation. SDS-PAGE analysis of the cross-linked F protein of Newcastle disease virus and human parainfluenza virus 3 showed a pattern very similar to that found for SV5. The data are consistent with those expected for the paramyxovirus F protein being a homotrimer.
Russell
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R
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500.
Paterson
R G
RG
Lamb
R A
RA
D000818:Animals; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D009522:Newcastle disease virus / Q000737:chemistry; D011233:Precipitin Tests; D018108:Respirovirus / Q000737:chemistry*; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000187:drug effects
D003432:Cross-Linking Reagents; D014760:Viral Fusion Proteins