Palmitoylation of a processed form of hepatitis C virus core protein by host dhhc enzymes

Authors: Filion, Audrey
Advisor: Leclerc, DenisMajeau, Nathalie
Abstract: As previously demonstrated, a fatty acid group is post-translationnally added on the residue C172 of Hepatitis C virus (HCV) core protein and this modification, termed palmitoylation, is required for viral assembly. In eukaryotes, palmitoylation is performed by a family of enzymes sharing a closely related DHHC motif. The purpose of this study was to identify which of the 23 mammalian DHHCs could perform palmitoyl acyltransferase activity on the HCV core protein. First, we characterized the expression and localization of DHHC enzymes in human hepatocytes. Then we evaluated the variation in core palmitoylation levels when each cellular DHHC proteins was over-expressed or repressed. This screen identified five enzymes with PAT activity on HCV core protein; DHHC 1, 2, 3, 6 and 7. Their co-localization with the viral protein was also demonstrated. These findings pave the way for future studies on the role of core palmitoylation during the HCV infection.
Document Type: Mémoire de maîtrise
Issue Date: 2013
Open Access Date: 19 April 2018
Grantor: Université Laval
Collection:Thèses et mémoires

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