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J Gen Virol 75 (1994), 2707-2717; DOI 10.1099/0022-1317-75-10-2707
© 1994 Society for General Microbiology
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Comparative studies of the structural proteins and glycoproteins of equine herpesviruses 2 and 5

C. T. Agius1, B. S. Crabb1, E. A. R. Telford2, A. J. Davison2 and M. J. Studdert1

1 School of Veterinary Science, The University of Melbourne, Parkville, Melbourne 3052, Australia
and2 MRC Virology Unit, Institute of Virology, University of Glasgow, Glasgow G11 5JR, U.K.

The structural proteins of equine herpesvirus 2 (EHV-2) and EHV-5, recently shown to be gammaherpesviruses, were identified and compared. Labelled proteins and glycoproteins were separated by SDS-PAGE and although EHV-2 and EHV-5 had similar protein profiles, bands in some positions were virus-specific. Six glycoproteins, with distinct profiles, were identified for both EHV-2 and EHV-5. Rabbit antisera to EHV-2 and EHV-5 and horse antiserum to EHV-2 were used in radio-immunoprecipitations, Western blot analysis and ELISA to investigate the immunogenicity and cross-reactivity of virus proteins. These analyses revealed that while EHV-2 and EHV-5 proteins share many common epitopes, they also possess type-specific epitopes. A 0.71 kb region of the EHV-2 glycoprotein B (gB) gene was expressed as a fusion protein in Escherichia coli. Antiserum raised in a rabbit to the EHV-2 fusion protein was used to identify a 64K EHV-2 protein as EHV-2 gB. Antiserum to EHV-2 gB was used to identify a 66K EHV-5 protein as EHV-5 gB. These proteins, which may represent subunits of gB rather than the entire molecule, appear the most immunodominant of the structural virion proteins as identified by Western blot.

Received 10 November 1993; accepted 8 June 1994.




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