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J Gen Virol 63 (1982), 481-485; DOI 10.1099/0022-1317-63-2-481
© 1982 Society for General Microbiology

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Identification of the Envelope Surface Glycoproteins of Equine Herpesvirus Type 1

Lloyd W. Turtinen and George P. Allen

Department of Veterinary Science University of Kentucky, Lexington, Kentucky 40546, U.S.A.

The structural polypeptides of purified enveloped virions of the Army 183 strain of equine herpesvirus type 1 (EHV-1) were examined by different analytical techniques to identify the envelope glycoproteins. Glycoproteins were identified by electrophoretic analysis in polyacrylamide slab gels of virus labelled in vivo with [3H]glucosamine or labelled enzymically in vitro with either UDP-[14C]galactose or sodium [3H]borohydride. Fluorograms revealed eleven glycoproteins (mol. wt. 260000, 150000, 138000, 90000, 87000, 65000, 62000, 60000, 50000, 46000, and 24000). These glycoproteins probably correspond to virion protein (VP) 1–2, 9b, 10, 13, 14, 16, 17, 18, 21, 22a and 25 respectively, as designated in two other EHV-1 strains. In addition, a poorly resolved glucosamine-rich region (mol. wt. 250000 to 200000) corresponded to VP 3 to 8. The two isotopic surface labelling methods revealed that all the virus glycoproteins were exposed on the envelope surface.

Keywords: EHV-1, envelope glycoprotein, surface labelling, [3H]glucosamine labelling

Received 23 March 1982; accepted 30 June 1982.


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The Truncated Form of Glycoprotein gp2 of Equine Herpesvirus 1 (EHV-1) Vaccine Strain KyA Is Not Functionally Equivalent to Full-Length gp2 Encoded by EHV-1 Wild-Type Strain RacL11
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[Abstract] [Full Text] [PDF]




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