Herpesvirus of turkeys (HVT) is frequently used to protect chickens against Marek's disease (MD). The HVT and MDV native antigen B complex shares common epitopes. To determine whether these oligomers present virus-neutralizing domains, monospecific antibodies to the HVT and MDV native 230 kDa oligomers were produced. The monospecific antibody immunopurified from an anti-HVT avian serum neutralized the in vitro infectivity of the oncogenic isolate MDV-B and the vaccine strains CVI988, SB1 and HVT and immunoblotted the 230 kDa oligomers of HVT and CVI988. As a result of the immunofluorescence analysis on infected cells, the monospecific antibody revealed foci of diffuse cytoplasmic immunofluorescence. A second monospecific antibody to the heat-stable 130 kDa monomer of HVT had limited neutralizing activity against HVT and CVI988 only, immunoblotted only the native HVT oligomer, and was not active in immunofluorescence. The monospecific antibody to the MDV-B 230 kDa oligomer neutralized and immunoblotted only the two MDV-1 strains but stained cells infected with MDVs of the three serotypes in immunofluorescence. It is concluded that the cross-protective neutralizing epitopes of HVT are located on heat-labile oligomeric forms of antigen B.