Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.796954
Title: Interactions of herpes simplex virus type-1 with the cell surface
Author: Wood, Lisa J.
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1994
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Abstract:
The present study was concerned with the characterisation of the herpes simplex virus type 1 (HSV-1) UL25 gene product and analysis of the phenotype of the HSV-1 mutant tsl204 which has a temperature sensitive (ts) mutation in the UL25 gene. Previous work by Addison et al. (1984) suggested that tsl204 was unable to penetrate the cell membrane at the non-permissive temperature (NPT). This early defect could be overcome by brief incubation of mutant infected cells at the permissive temperature (PT). Upon further incubation of mutant-infected cells at the NPT, low numbers of intermediate capsids lacking DNA assembled in the nucleus. No full capsids were observed, indicating that tsl204 also had a defect in the production of virus particles. Although the work presented here confirmed that tsl204 has a defect in a step prior to the onset of viral protein synthesis, the data indicated that tsl204 had an uncoating defect at the NPT. A rabbit polyclonal antiserum raised against an oligopeptide representing anamino acid sequence present in the UL25 polypeptide was used to study the synthesis, processing and location of the UL25 gene product. The antiserum recognized a 67,000MW protein in virus-infected cell extracts and in purified virions, suggesting that the UL25 protein was a structural component of the virion.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.796954  DOI: Not available
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