Relatedness of glycoproteins expressed on the surface of simian herpes-virus virions and infected cells to specific HSV glycoproteins.

The antigenic relatedness of the surface glycoprotein antigens of six herpesviruses indigenous to human and nonhuman primates was examined. Binding of anti-viral sera to viral antigens expressed on the surface of infected cells demonstrated that the surface antigens of herpes simplex virus type 1 (HSV 1), HSV 2, simian agent 8 (SA8), and Herpesvirus simiae (B virus) exhibit extensive cross-reactivity. Surface antigens of two viruses isolated from South American primates, H. saimiri 1 (HVS 1) and H. ateles 1 (HVA 1), were comparatively more virus-specific in their antigenic reactivity. Endpoint neutralization tests performed in the presence and absence of complement confirmed these results. Immunoprecipitation of viral proteins was used to identify those representing cross-reactive surface antigens. A glycoprotein of approximately 110,000-125,000 Daltons (110-125 k) was immunoprecipitated from cells infected with each of the six primate herpesvirus by antisera to each of the viruses. Using monospecific antisera, these glycoproteins were shown to be antigenically related to the gB glycoproteins of HSV. Although these glycoproteins were antigenically conserved among all six viruses, antibodies to the gB glycoproteins did not cross-neutralize heterologous viruses. A glycoprotein of approximately 60-70 k was precipitated from HSV 1, HSV 2, SA8, and B virus infected cells by antisera to each of these four viruses. These SA8 and B virus glycoproteins were shown to be antigenically related to the gD glycoproteins of HSV 1 and HSV 2 and to be involved in cross-neutralization among these viruses. Antisera to HVS 1 and HVA 1 did not recognize these gD glycoproteins nor was a glycoprotein of similar molecular weight precipitable from HVS 1 or HVA 1 infected cells by antisera to the other four viruses. Southern blot hybridizations using probes for HSV glycoprotein genes confirmed the conservation of the gB glycoproteins among all the simian viruses and of the gD gene in SA8 and B virus. A glycoprotein of approximately 75-80 k was, however, precipitated from HVS 1 and HVA 1 infected cells by antisera to either of these two viruses. In addition, at least one glycoprotein which appeared to be predominantly virus-specific in its reactivity was identified for five of the viruses.