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Factors affecting the non-structural functions of Rubella virus capsid Open Access


Other title
Cell Biology
Type of item
Degree grantor
University of Alberta
Author or creator
Willows, Steven D
Supervisor and department
Hobman, Tom (Cell Biology)
Examining committee member and department
Hobman, Tom (Cell Biology)
Simmen, Thomas (Cell Biology)
Goping, Ing Swie (Biochemistry)
Shmulevitz, Maya (Medical Microbiology and Immunology)
Jean, François (Microbiology and Immunology)
Department of Cell Biology

Date accepted
Graduation date
Doctor of Philosophy
Degree level
During infection, the host cell environment must be altered to accommodate viral replication. These alterations include hijacking cellular membranes as well as other components to form viral replication compartments and attenuating the host defenses to prevent virus detection and elimination. While DNA viruses can encode single purpose proteins dedicated for these functions, RNA viruses have a more limited coding capacity and instead utilize proteins with multiple functions. Rubella virus, a single-stranded, positive-sense RNA virus in the family Togaviridae, is one example. The capsid protein of this virus, which forms the protective protein shell around the genomic RNA in the virion, also fulfils several non-structural roles during infection. While previous studies have revealed several host proteins that are associated with these non-structural roles, more work is needed in order to fully understand how capsid alters the host cell environment. In this thesis, I investigated factors that affect the ability of capsid to inhibit apoptosis, a mechanism used to limit viral replication and eliminate infected cells within multicellular organisms. I found that phosphorylation and membrane association of capsid are important for its anti-apoptotic function, with both being necessary to prevent sequestration of capsid in RNA rich regions of the cell. Furthermore, I discovered that a canonical binding site for protein phosphatase 1 (PP1) is important for the anti-apoptotic function of capsid as well as its role in virion assembly. Finally, I showed that the capsid protein antagonizes innate immune signaling, a function that is dependent on its PP1-binding site.
This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for the purpose of private, scholarly or scientific research. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
Citation for previous publication
Willows, S.D., Ilkow, C.S. and Hobman, T.C. (2014) Phosphorylation and membrane-association of the Rubella virus capsid protein are important for its anti-apoptotic function. Cell Microbiol. 16(8): 1201-10.

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