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dc.contributor.supervisorCao, Jingxin (Medical Microbiology)en_US
dc.contributor.authorDick, Kevin James
dc.date.accessioned2011-09-08T14:56:10Z
dc.date.available2011-09-08T14:56:10Z
dc.date.issued2011-09-08
dc.identifier.urihttp://hdl.handle.net/1993/4852
dc.description.abstractVaccinia virus E3 protein is known to bind double-stranded RNA and mediate interferon resistance. Alanine scanning mutagenesis was performed on its dsRNA binding domain, sufficient for wild-type tropism and immune suppression in vitro, and dsRNA binding and host range function assayed. Residues involved in dsRNA binding were required for host range function; however, seven dsRNA binding mutants were unable to rescue ΔE3L replication. Utilizing recombinant viruses, non-rescue mutants were unable to inhibit protein Kinase R phosphorylation despite dsRNA binding. Furthermore, host range was found to correlate with cytokine suppression and replication in IFN stimulated Huh7R cells. Additionally, no direct association was found between dsRNA binding and PKR interaction, refining the suppression model. Novel protein-protein interactions were discovered between E3 and cellular proteins via differential gel electrophoresis. This study represents the first full mapping of E3 residues involved in dsRNA binding and tropism, forming a basis for future study.en_US
dc.language.isoengen_US
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectVirologyen_US
dc.subjectInnate Immunityen_US
dc.subjectPoxvirusen_US
dc.titleMutational analysis of the dsRNA binding domain of Vaccinia Virus E3 proteinen_US
dc.typeinfo:eu-repo/semantics/masterThesis
dc.typemaster thesisen_US
dc.degree.disciplineMedical Microbiologyen_US
dc.contributor.examiningcommitteeBabiuk, Shawn (Immunology) Yao, Xiao-Jian (Medical Microbiology)en_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.noteOctober 2011en_US


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