Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia.
The fusion (F) and hemagglutinin-neuraminidase (HN) glycoproteins of the paramyxovirus simian virus 5 (SV5) were expressed individually or coexpressed in CV-1 cells by using SV40-based vectors and recombinant vaccinia viruses. The extent of detectable fusion in a syncytium formation assay was found to be affected by the expression system used. In addition, when HN was coexpressed with F, it was found that the expression vector system influenced the contribution of HN in forming syncytia. The abilities of the SV5, human parainfluenza virus type 3, and Newcastle disease virus F glycoproteins to cause fusion, when expressed alone or coexpressed with HN, were directly compared by using the SV40-based vector system in CV-1 cells. The F proteins exhibited various degrees of fusion activity independent of HN expression, but the formation of syncytia could be enhanced to different extents by the coexpression of the homotypic HN protein.
Horvath
C M
CM
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500.
Paterson
R G
RG
Shaughnessy
M A
MA
Wood
R
R
Lamb
R A
RA
D002460:Cell Line; D003001:Cloning, Molecular; D015726:Giant Cells / Q000382:microbiology*; D015707:HN Protein / Q000502:physiology*; D010252:Paramyxoviridae / Q000472:pathogenicity / Q000502:physiology*; D014760:Viral Fusion Proteins / Q000502:physiology*
D015707:HN Protein; D014760:Viral Fusion Proteins