A panel of monoclonal antibodies (MAbs) specific to glycoprotein D (gD) of Aujeszky's disease virus (ADV, Suid herpesvirus 1) was produced and characterized. MAbs were used to identify 9 topologically different epitopes and epitopic groups on gD. The majority of the identified epitopes were conformational. Most gD-specific MAbs possessed virus-neutralizing activity in the presence and absence of the complement. MAbs neutralized the virus at the stage of its penetration into the cell and inhibited the cell-to-cell spread of viruses. Two immunodominant epitopes and one immunodominant domain that induce the most prominent humoral immune response were identified when the animals were infected and immunized. A method was developed for affinity purification of ADV glycoprotein D. Immunization of mice with affinity-purified gD induced a strong humoral immune response and protected mice against lethal ADV challenge. In passive immunization, the majority of gD-specific MAbs protected mice against infection. The findings confirm the important role of ADV glycoprotein D in inducing protective anti-ADV immunity.
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