Monoclonal antibodies against 3 different glycoproteins of bovine herpesvirus type 1 (BHV-1) involved in virus neutralization were used in indirect immunofluorescence (IIF) tests to characterize the appearance and transport to the plasma membrane of virus antigens in the infected cells. Antibodies against gp 117 and gp 71 glycoproteins first showed pronounced ring-like nuclear fluorescence at 4 hours post-infection (PI), followed by staining of the perinuclear region, presumably the Golgi apparatus. In contrast, antibody against gp 87 produced staining in cell-to-cell junctional areas at 3 hours PI before any staining close to the nucleus. The expression of the 3 glycoproteins at the surface of the infected cells was confirmed by the use of monoclonal antibodies having neutralizing activity, but not by non-neutralizing antibodies against gp 117 and gp 71. Non-neutralizing antibody against gp 87 detected the surface fluorescence only in those cells showing marked degeneration. Inhibition of glycosylation of the viral glycoproteins with tunicamycin (TM) was followed by interference with transport of gp 117 and gp 87 to the plasma membrane. On the other hand, gp 71 was incorporated into the plasma membrane despite the lack of N-linked glycosylation.