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. / xiii, 101 leaves : ill. (some col.) ; 28 cm. --
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:ALU.w.uleth.ca/dspace#10133/680 |
| Date | January 2008 |
| Creators | Yu, Ian-Ling, University of Lethbridge. Faculty of Arts and Science |
| Contributors | Lung, Oliver |
| Publisher | Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2008, Arts and Science, Department of Biological Sciences |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | en_US |
| Detected Language | English |
| Type | Thesis |
| Relation | Thesis (University of Lethbridge. Faculty of Arts and Science) |
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