Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599737
Title: Studies of herpes simplex type 1 in polarized and non-polarized cells
Author: Griffiths, A.
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 1997
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Abstract:
The first steps in the life cycle of HSV-1 are attachment of the virus to the cell, followed by fusion of the virion envelope with the plasma membrane. Both of these events are mediated by virally encoded glycoproteins present in the virion envelope which interact with receptors on the cell surface. Evidence for the involvement of certain glycoproteins in each step has come from the use of viruses which are unable to correctly express the glycoprotein in question. To date four glycoproteins (gB, gD, gH and gL) have been shown to be essential for viral infectivity of fibroblast cells, and gC has been implicated in their efficient infection. However, during a natural infection the primary targets of the virus are polarized epithelial cells, and therefore such cells represent a more realistic system with which to study viral infectivity. Polarized epithelial cells are characterised by distinct apical and basolateral domains, each with a unique protein and lipid composition, and can be cultured in vitro. After demonstrating the polarity of the epithelial cells used in these studies, I was unable to demonstrate any phenotype for a range of viruses which did not express individual glycoproteins. Notably viruses which were unable to express gC were able to infect the apical surface of the polarized cells, conflicting with published data. Detailed characterisation of these viruses was undertaken in non-polarized cells, and no evidence for the involvement of gC in infectivity was observed, again contrary to current dogma. However, a role for gC in the efficient secretion of virus from cells was observed.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.599737  DOI: Not available
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