Analysis of bovine respiratory syncytial virus envelope glycoproteins in cell fusion.

TitleAnalysis of bovine respiratory syncytial virus envelope glycoproteins in cell fusion.
Publication TypeJournal Article
Year of Publication1997
AuthorsPastey M, Samal SK
JournalThe Journal of general virology
Volume78 ( Pt 8)
Pagination1885-9
Date Published1997 Aug
ISSN0022-1317
KeywordsAnimals, beta-Galactosidase, Cattle, Cell Fusion, Gene Expression Regulation, Viral, Genes, Viral, Glycoproteins, Hela Cells, Humans, Oligodeoxyribonucleotides, Recombinant Fusion Proteins, Respiratory Syncytial Virus, Bovine, Respiratory Syncytial Virus, Human, Respiratory Syncytial Viruses, Sheep, Transcriptional Activation, Transfection, Viral Envelope Proteins, Viral Fusion Proteins, Viral Matrix Proteins
Abstract

To compare the requirements for respiratory syncytial virus (RSV)-mediated cell fusion, the fusion (F), attachment (G) and small hydrophobic (SH) glycoproteins of bovine RSV (BRSV), ovine RSV (ORSV) and human RSV (HRSV) were expressed individually or coexpressed in either homologous or heterologous combinations in HeLa cells, using the vaccinia virus-T7 polymerase transient expression system. Cell fusion was examined by a reporter gene activation assay. Although the expression of the F protein alone or coexpression of the F and G proteins or the F and SH proteins induced cell fusion, coexpression of F, G and SH proteins induced extensive cell fusion. Coexpression of various combinations of envelope glycoproteins of BRSV, ORSV and HRSV indicated that substitution of heterologous SH protein affects the effective fusigenic properties of the BRSV F protein far more than that obtained by substituting the heterologous G protein.

Alternate JournalJ. Gen. Virol.