COMMON ANTIGENIC EPITOPES ARE PRESENT ON HEAT-LABILE OLIGOMERS OF MDVGLYCOPROTEIN-B AND ON HSV GLYCOPROTEIN-B

The antigenic cross-reactivity between the Marek's disease virus glyco protein B (MDV gB) and glycoprotein B (gB) of herpes simplex virus typ e 1 and 2 (HSV1 and HSV2) was analysed by the immunoblotting method. W e studied cell lysates in both denatured and in undenatured form (i.e. , unheated) and reacted them with convalescent sera from chickens infe cted with the RBIB MDV strain and with human anti-HSV1 gB. Both sera d etected the heat-labile MDV gB and the HSV gB oligomers. In addition, monospecific antibodies to the MDV gB 230 kDa oligomer (strain CVI988) were immunoaffinity purified from both the chicken and the human sera . The chicken and human monospecific antibodies detected the homologou s and the heterologous gB oligomers in native MDV- and HSV1-infected c ell lysates. 15 human sera were tested by immunoblotting and by immuno fluorescence on HSV1-, CVI988-and herpes virus of turkeys (HVT)-infect ed cells. By both assays about half of the human sera reacted with MDV -infected cells. This study demonstrates that the MDV gB heat-labile o ligomers possess conformational epitopes shared with the human alpha-h erpes virus HSV1 and HSV2 gB heat-labile oligomers.