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Title: EHV-1 and its interactions with cellular membranes
Author: McKenzie, Graeme
Awarding Body: University of Nottingham
Current Institution: University of Nottingham
Date of Award: 2013
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Equine herpes virus 1 (EHV-1) causes abortion and neurological disease in horses, largely through the infection of endothelial cells and consequent inflammation which leads to a disruption of the vascular supply to the pregnant uterus and spinal cord. Although many different cell types are susceptible to infection, it is the cell associated viraemia which disseminates virus to these sites of secondary replication. Therefore, in recent years a great deal of research has focused on understanding the binding and entry of EHV-1 to several mammalian cell types. Like other alphaherpes viruses, EHV-1 has been shown to utilise several binding receptors and uptake mechanisms to infect its many permissible cell types. In the current study the physical characteristics of EHV-1 were determined and the mechanism of viral binding and fusion into rabbit kidney 13 cells (RK13s) and resting and activated peripheral blood mononuclear cells (PBMC) was observed. EHV-1 was identified as being 266 nm in diameter and had a zeta potential of -33 mV. Heat inactivated (HI) EHV-1 was shown to co -localise with GM-1 suggesting that it may associate with lipid rafts. Following infection of PBMC collected from horses with homozygous major histocompatibility complex class 1 (MHC-1) serological haplotypes (A2, A3 and A9) withEHV-1 strain RacL11 expressing green fluorescent protein (GFP) in place of glycoprotein 2(.1gp2), no apparent difference in infection was observed. Various fluorescence ii based fusion and endocytosis experiments were carried out using HI EHV- l Ab4 to infect RK13s and equine PBMC to examine the mechanisms involved, but the techniques proved too insensitive. The data suggest that initially, EHV-l associates with rafts and that MHC- l haplotype has no effect on viral infection of PBMCs. It was concluded that heat inactivation may damage viral glycoproteins sufficiently to reduce viral fusion and that future experiments should use live, infectious virus. ii
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available