Studies with Cross-Linking Reagents on the Oligomeric Form of the Paramyxovirus Fusion Protein

Rosemary Russell, Reay G. Paterson, Robert A. Lamb*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

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.

Original languageEnglish (US)
Article number71108
Pages (from-to)160-168
Number of pages9
JournalVirology
Volume199
Issue number1
DOIs
StatePublished - Feb 15 1994

ASJC Scopus subject areas

  • Virology

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