Studies with Cross-Linking Reagents on the Oligomeric Form of the Paramyxovirus Fusion Protein
Identifieur interne : 001A22 ( Istex/Checkpoint ); précédent : 001A21; suivant : 001A23Studies with Cross-Linking Reagents on the Oligomeric Form of the Paramyxovirus Fusion Protein
Auteurs : Rosemary Russell [États-Unis] ; Reay G. Paterson [États-Unis] ; Robert A. Lamb [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1994.
Abstract
Abstract: 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 Mr ∼ 65, Mr ∼ 130, and Mr ∼ 195 kDa, suggesting F monomers, dimers, and trimers, respectively. The cross-linked F species of Mr ∼ 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.
Url:
DOI: 10.1006/viro.1994.1108
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: 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 Mr ∼ 65, Mr ∼ 130, and Mr ∼ 195 kDa, suggesting F monomers, dimers, and trimers, respectively. The cross-linked F species of Mr ∼ 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.</div>
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