Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.796489
Title: The protein products of herpes simplex virus type 1 genes UL31, UL45, UL46 and UL47
Author: McLean, Gordon William
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1990
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Abstract:
Herpes simplex virus type 1 (HSV-1), contains a large (153Kb) double-stranded DNA genome, the complete sequence of which has now been fully determined. Of the predicted open-reading frames (ORFs), a number have still to have a protein product assigned to them and their ability to encode a polypeptide confirmed. The availability of this sequence has allowed the use of short oligopeptides to generate antisera reactive with HSV-l proteins of which the peptide was predicted to form a part. This technique has been used successfully to identify a number of HSV-1 encoded polypeptides or to assign previously identified viral encoded proteins to their ORF. Unfortunately the antipeptide sera produced using the standard method whereby peptides are coupled to carrier proteins are often of low titre making experimentation difficult. Work presented here has shown that peptides presented in a branched form attached to a polylysine core were more immunogenic than monomeric peptides coupled to carrier proteins or peptides attached to a resin matrix. Branched peptides elicited both higher titre antipeptide and antiprotein immune reponses in rabbits. In addition, these responses were achieved after a single immunisation of peptide, whereas both other forms of antigen required two or more immunisations to produce a response. Branched peptides were also shown to be successful at producing high titre antipeptide responses in inbred mice when presented in combination with a "foreign" TH-cell epitope. Antisera generated in this study were used to identify the protein products of four HSV-1 genes namely; UL31, UL45, UL46 and UL47. The product of gene UL31 has an apparent Mr of 30,000.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.796489  DOI: Not available
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