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dc.contributor.supervisor Lung, Oliver Yu, Ian-Ling University of Lethbridge. Faculty of Arts and Science 2008-10-27T17:37:54Z 2008-10-27T17:37:54Z 2008
dc.description xiii, 101 leaves : ill. (some col.) ; 28 cm. -- en
dc.description.abstract Budded virions of AcMNPV can enter a variety of non-host cells, a characteristic likely due to the presence of GP64, an envelope protein found on a small subset of baculoviruses. Results show that AcMNPV's tropism for vertebrate cells can be restricted - a prerequisite for using AcMNPV for targeted in vivo gene delivery - by replacing the gp64 gene with SeF from SeMNPV. Unlike the relatively well characterized GP64 protein, the significance and function of the F homolog (Ac23, a pathogenicity factor), is poorly understood. How Ac23 might contribute to the faster speed of kill was examined by comparing occlusion bodies and occlusion-derived virions (ODV) of Ac23null mutant viruses with control viruses at the ultrastructural level. The results show that Ac23null mutant produces a significantly higher percentage of ODVs with single or lower number of nucleocapsids than controls, suggesting Ac23 may play a role in multicapsid envelopment of ODVs. en
dc.language.iso en_US en
dc.publisher Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2008 en
dc.relation.ispartofseries Thesis (University of Lethbridge. Faculty of Arts and Science) en
dc.subject Dissertations, Academic en
dc.subject Gene expression en
dc.subject Proteins -- Research en
dc.subject Baculoviruses -- Genetics en
dc.title Functional analysis of two baculovirus envelope proteins en
dc.type Thesis en
dc.publisher.faculty Arts and Science en
dc.publisher.department Department of Biological Sciences en Masters

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