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1 Veterinary Infectious Disease Organization, University of Saskatchewan, Saskatoon, Saskatchewan, Canada S7N 5E3
2 Department of Virology-Immunology, Faculty of Veterinary Medicine, University of Liege, B-4000 Liege Sart Tilman, Belgium
3 Department of Macromolecular Chemistry and Analytical Science, SmithKline Beecham Biologicals, B-1330 Rixensart, Belgium
The glycoproteins of bovine herpesvirus 1 (BHV-1) play important roles in the interactions between virions and target cells. A 108 kDa glycoprotein, designated gII or gp108, has been identified by two different panels of monoclonal antibodies. The gII- and gp108-specific monoclonal antibodies were shown to react with the same protein, which was identified by N-terminal sequencing as the homologue of herpes simplex virus type 1 (HSV-1) gH. When BHV-1 gH was purified by immunoadsorbent chromatography, gL was co-purified. The gH-gL complex induced the production of antibodies that neutralized virus infectivity and inhibited virus penetration. Affinity-purified gH-gL did prevent penetration, but not attachment of BHV-1, which suggests that the gH-gL complex is essential for penetration of BHV-1 into susceptible cells.
Received 21 December 1995;
accepted 11 March 1996.
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