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Virology. 1991 Apr;181(2):773-7.

pH-dependent solubility shift of rubella virus capsid protein.

Author information

1
Department of Pathology, University of British Columbia, Vancouver, Canada.

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.

PMID:
2014651
DOI:
10.1016/0042-6822(91)90916-y
[Indexed for MEDLINE]

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