Comparative studies of the structural proteins and glycoproteins of equine herpesviruses 2 and 5.
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 radioimmunoprecipitations, 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.
Agius
C T
CT
School of Veterinary Science, University of Melbourne, Parkville, Australia.
Crabb
B S
BS
Telford
E A
EA
Davison
A J
AJ
Studdert
M J
MJ
D000818:Animals; D000914:Antibodies, Viral; D001483:Base Sequence; D015153:Blotting, Western; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D006736:Horses / Q000276:immunology; D007668:Kidney; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011817:Rabbits / Q000276:immunology; D018140:Varicellovirus / Q000737:chemistry*; D015678:Viral Structural Proteins / Q000096:biosynthesis / Q000276:immunology / Q000302:isolation & purification*
D000914:Antibodies, Viral; D015678:Viral Structural Proteins