Eileen Clancy
Academic Appointments
- Postdoctoral Research fellow, Microbiology & Immunology
Key Documents
Contact Information
- Academic Offices
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Professional Overview
Professional Education
| Doctor of Philosophy: | Dalhousie University (2009) |
| Bachelor of Science, Honours: | University of Guelph, Microbiology (2003) |
Stanford Advisors
| Karla Kirkegaard: | Postdoctoral Faculty Sponsor |
Scientific Focus
Current Research Interests
Hepatitis A virus (HAV) is the sole member of genus hepatovirus in the Picornaviridae family. Although HAV is transmitted via the fecal-oral route, the primary site of replication for HAV is the liver where it causes acute viral hepatitis. HAV spreads from cell to cell in liver tissue without exhibiting any potent cytopathic effects. Thus it appears that, unlike other picornaviruses, the primary mechanism of HAV cell-to-cell spread may be via non-lytic routes.
Previous work in the Kirkegaard lab has described the AWOL (autophagosome-mediated exit without lysis) pathway as a potential mode of non-lytic release for poliovirus. During exit via AWOL, newly assembled virus particles in the cytoplasm are engulfed in double membrane vesicles that form during infection and act as the site of viral RNA replication. Subsequent fusion events at the plasma membrane then deliver the virus particles to the extracellular milieu without compromising membrane integrity. While the bulk of poliovirus spread is through cell lysis, I am currently investigating whether HAV spread may occur primarily via AWOL or a related mechanism.
Publications
- Neuron-to-neuron transmission of α-synuclein fibrils through axonal transport. Ann Neurol. 2012; (4): 517-24
- Helix-destabilizing, beta-branched, and polar residues in the baboon reovirus p15 transmembrane domain influence the modularity of FAST proteins. J Virol. 2011; (10): 4707-19
- Homomultimerization of the reovirus p14 fusion-associated small transmembrane protein during transit through the ER-Golgi complex secretory pathway. J Gen Virol. 2011; (Pt 1): 162-6
- Different activities of the reovirus FAST proteins and influenza hemagglutinin in cell-cell fusion assays and in response to membrane curvature agents. Virology. 2010; (1): 119-29
- Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion. J Virol. 2009; (7): 2941-50
- The p14 fusion-associated small transmembrane (FAST) protein effects membrane fusion from a subset of membrane microdomains. J Biol Chem. 2006; (42): 31778-89
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