SYNTHESIS AND PROCESSING OF BOVINE HERPESVIRUS-1 GLYCOPROTEIN-H

The translation product of the bovine herpesvirus-1 (BHV-1) gH gene wa s identified and characterized. Synthetic peptides were used to genera te specific antisera and a glycoprotein of 108K was precipitated by on e of the antisera. Cross-immunoprecipitations with monoclonal antibodi es to BHV-1 glycoprotein gp108 and the anti-gH peptide antiserum demon strated that gp108 is the translation product of the gH open reading f rame. Glycoprotein gH synthesis and intracellular processing was analy zed in infected Madin-Darby bovine kidney cells using anti-gp108 monoc lonal antibodies. Glycoprotein gH is expressed as a beta-gamma protein and could be detected by radioimmunoprecipitation as early as 2 hr po stinfection. Cotranslational N-glycosylation of gH is essential for th e recognition by monoclonal antibodies, suggesting that N-linked glyca ns are involved in protein folding or that they are targets for most o f monoclonal antibodies used in this study. (C) 1995 Academic Press, I nc.