pH-dependent solubility shift of rubella virus capsid protein.
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.
Mauracher
C A
CA
Department of Pathology, University of British Columbia, Vancouver, Canada.
Gillam
S
S
Shukin
R
R
Tingle
A J
AJ
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
D012367:RNA, Viral; D011092:Polyethylene Glycols; D017830:Octoxynol; C010615:Nonidet P-40