title: Bacteriophage ϕ6 nucleocapsid surface protein 8 interacts with virus-specific membrane vesicles containing major envelope protein 9.
abstract: Enveloped double-stranded RNA (dsRNA) bacterial virus Pseudomonas phage ϕ6 has been developed into an advanced assembly system where purified virion proteins and genome segments self-assemble into infectious viral particles, inferring the assembly pathway. The most intriguing step is the membrane assembly occurring inside the bacterial cell. Here, we demonstrate that the middle virion shell, made of protein 8, associates with the expanded viral core particle and the virus-specific membrane vesicle.
authors.affiliation: Department of Biosciences, University of Helsinki, Biocenter 2, Helsinki, Finland.
authors.forename: L Peter
authors.initials: LP
authors.lastname: Sarin
authors.forename: Jari J
authors.initials: JJ
authors.lastname: Hirvonen
authors.forename: Pasi
authors.initials: P
authors.lastname: Laurinmäki
authors.forename: Sarah J
authors.initials: SJ
authors.lastname: Butcher
authors.forename: Dennis H
authors.initials: DH
authors.lastname: Bamford
authors.forename: Minna M
authors.initials: MM
authors.lastname: Poranen
mesh_terms: D017126:Bacteriophage phi 6 / Q000502:physiology*; D036022:Capsid Proteins / Q000378:metabolism*; D050356:Lipid Metabolism; D011485:Protein Binding; D014759:Viral Envelope Proteins / Q000378:metabolism*; D019065:Virus Assembly
chemical_list: D036022:Capsid Proteins; D014759:Viral Envelope Proteins