Functional analysis of two baculovirus envelope proteins
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Date
2008
Authors
Yu, Ian-Ling
University of Lethbridge. Faculty of Arts and Science
Journal Title
Journal ISSN
Volume Title
Publisher
Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2008
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.
Description
xiii, 101 leaves : ill. (some col.) ; 28 cm. --
Keywords
Dissertations, Academic , Gene expression , Proteins -- Research , Baculoviruses -- Genetics