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Bovine herpesvirus 1 (BHV-1) glycoprotein gill functions both as a major virus attachment protein and haemagglutinating protein. Here we constructed recombinant baculovirus incorporating the BHV-1 gill coding sequence to characterize the expression, function and immunogenicity of the glycoprotein in insect cells. The recombinant gill had an Mr of 72K and seemed to form homodimers. The gill was expressed on the surface of insect cells and a rosette formation assay demonstrated haemadsorbing activity of the glycoprotein. Antigenic authenticity of the recombinant gill was confirmed by a panel of monoclonal antibodies specific for the glycoprotein produced in mammalian cells. Antisera raised to recombinant gill neutralized the infectivity of BHV-1. These data suggest that recombinant gill produced in insect cells may be a useful immunogen in a BHV-1 vaccine.
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