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Title: Sequence analysis of selected regions of the equine herpesvirus 4 genome
Author: Riggio, Marcello Pasquale
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1990
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The gene encoding glycoprotein gB of EHV-4 strain 1942 was located within a BamHI genomic library by a combination of dot blot and Southern blot hybridisation using probes derived from the HSV-1 gB DNA sequence, and its DNA sequence determined. The major portion of the gene mapped to a 2.9kb fragment at the left-hand end of BamHI-C with the transcriptional control domains and start of the coding sequences of the gene located at the right-hand end of BamHI-M. The unprocessed EHV-4 gB protein was predicted to be 975 amino acids (110kDa) in size and composed of an unusually long amino-terminal signal sequence, a hydrophilic surface domain containing 11 potential N-linked glycosylation sites and 10 cysteine residues, a hydrophobic transmembrane domain thought to span the membrane three times and a highly charged carboxyl-terminal cytoplasmic anchor domain. A potential internal proteolytic cleavage site was identified near the centre of the protein. The EHV-4 gB protein demonstrated high levels of conservation of primary amino acid sequence with other herpesvirus gB-like proteins. Furthermore, the conservation of all cysteine residues and some N-linked glycosylation sites in the surface domain between the gB-like proteins suggested possible conservation of secondary and tertiary structures. The gB-like proteins may have a similar, conserved function across the herpesviruses.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available