title: 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.
authors.affiliation: Department of Molecular Biology, Karolinska Institute, Huddinge, Sweden.
authors.forename: B U
authors.initials: BU
authors.lastname: Barth
authors.forename: M
authors.initials: M
authors.lastname: Suomalainen
authors.forename: P
authors.initials: P
authors.lastname: Liljeström
authors.forename: H
authors.initials: H
authors.lastname: Garoff
mesh_terms: D000524:Alphavirus / Q000235:genetics / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002459:Cell Fusion; D002460:Cell Line; D002462:Cell Membrane / Q000382:microbiology; D006224:Cricetinae; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism; D012672:Semliki forest virus / Q000235:genetics / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000378:metabolism*
chemical_list: D046911:Macromolecular Substances; D012367:RNA, Viral; D014759:Viral Envelope Proteins