title: pH-dependent solubility shift of rubella virus capsid protein.
abstract: The mechanism of capsid uncoating in rubella virus and other togaviridae is not well understood. This study presents data which suggest that rubella virus capsid undergoes a structural change from having hydrophilic to hydrophobic properties, between pH 5 and 5.5. Such a conformational change would allow capsid uncoating to occur within the lysosome, allowing RNA penetration to occur upon fusion of the viral envelope with the limiting membrane of the lysosome.
authors.affiliation: Department of Pathology, University of British Columbia, Vancouver, Canada.
authors.forename: C A
authors.initials: CA
authors.lastname: Mauracher
authors.forename: S
authors.initials: S
authors.lastname: Gillam
authors.forename: R
authors.initials: R
authors.lastname: Shukin
authors.forename: A J
authors.initials: AJ
authors.lastname: Tingle
mesh_terms: D000818:Animals; D001483:Base Sequence; D002213:Capsid / Q000737:chemistry / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D008247:Lysosomes / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009036:Moths / Q000382:microbiology; D017830:Octoxynol; D011092:Polyethylene Glycols; D011487:Protein Conformation; D012367:RNA, Viral / Q000737:chemistry; D012412:Rubella virus / Q000235:genetics*; D012995:Solubility
chemical_list: D012367:RNA, Viral; D011092:Polyethylene Glycols; D017830:Octoxynol; C010615:Nonidet P-40