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Research Article
1 December 1992

Alphavirus assembly and entry: role of the cytoplasmic tail of the E1 spike subunit

Abstract

The alphavirus Semliki Forest virus (SFV) matures by budding at the cell surface. This process is driven by interactions of its membrane protein heterodimer E2-E1 and the nucleocapsid. The virus penetrates into new cells by an E1-mediated membrane fusion event. The E1 subunit has a short, strongly positively charged cytoplasmic tail peptide (Arg-Arg) which is very conserved among different alphavirus E1 proteins. In this work, we have used in vitro mutagenesis of a full-size cDNA clone of SFV to study the role of the tail peptide of the E1 subunit in virus budding and fusion processes in baby hamster kidney cell culture. Our results suggest that the E1 tail plays no major role in SFV multiplication in animal cell culture.

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Published In

cover image Journal of Virology
Journal of Virology
Volume 66Number 12December 1992
Pages: 7560 - 7564
PubMed: 1331539

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Published online: 1 December 1992

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Authors

B U Barth
Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.
M Suomalainen
Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.
P Liljeström
Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.
H Garoff
Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.

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