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PMID: 1602561 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Biological activity of paramyxovirus fusion proteins: factors influencing formation of syncytia.

Journal of virology ·Vol. 66 ·No. 7 ·1992-07-00 ·Pages 4564-9

Horvath CM, Paterson RG, Shaughnessy MA, Wood R, Lamb RA

Abstract

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.

MeSH Terms
Cell Line Cloning, Molecular Giant Cells/microbiology HN Protein/physiology Paramyxoviridae/pathogenicity,physiology Viral Fusion Proteins/physiology
Chemicals
HN Protein Viral Fusion Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Horvath C M
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500.
Paterson R G
Shaughnessy M A
Wood R
Lamb R A
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1992-07-00
Pages
4564-9
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC241269
Subset
IM
Grants
NIAID NIH HHS · AI-23173 · United States
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