Eberle R, Black D, Hilliard J K
Department of Veterinary Parasitology, Microbiology, and Public Health, College of Veterinary Medicine, Oklahoma State University, Stillwater.
Arch Virol. 1989;109(3-4):233-52. doi: 10.1007/BF01311084.
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.
对六种人类和非人灵长类动物所特有的疱疹病毒的表面糖蛋白抗原的抗原相关性进行了检测。抗病毒血清与感染细胞表面表达的病毒抗原的结合表明，1型单纯疱疹病毒（HSV 1）、2型单纯疱疹病毒（HSV 2）、猿猴病毒8（SA8）和猴疱疹病毒（B病毒）的表面抗原表现出广泛的交叉反应性。从南美灵长类动物分离出的两种病毒，即赛氏疱疹病毒1（HVS 1）和蛛猴疱疹病毒1（HVA 1），其表面抗原在抗原反应性上相对更具病毒特异性。在有和没有补体存在的情况下进行的终点中和试验证实了这些结果。病毒蛋白的免疫沉淀用于鉴定那些代表交叉反应性表面抗原的蛋白。通过针对六种灵长类疱疹病毒中每一种病毒的抗血清，从感染了这六种病毒的细胞中免疫沉淀出一种分子量约为110,000 - 125,000道尔顿（110 - 125 k）的糖蛋白。使用单特异性抗血清，这些糖蛋白被证明在抗原性上与HSV的gB糖蛋白相关。尽管这些糖蛋白在所有六种病毒中在抗原性上是保守的，但针对gB糖蛋白的抗体并不能交叉中和异源病毒。通过针对HSV 1、HSV 2、SA8和B病毒中每一种病毒的抗血清，从感染这些病毒的细胞中沉淀出一种分子量约为60 - 70 k的糖蛋白。这些SA8和B病毒的糖蛋白被证明在抗原性上与HSV 1和HSV 2的gD糖蛋白相关，并参与这些病毒之间的交叉中和。针对HVS 1和HVA 1的抗血清不识别这些gD糖蛋白，并且针对其他四种病毒的抗血清也不能从感染HVS 1或HVA 1的细胞中沉淀出分子量相似的糖蛋白。使用HSV糖蛋白基因探针进行的Southern印迹杂交证实了所有猿猴病毒中gB糖蛋白的保守性以及SA8和B病毒中gD基因的保守性。然而，通过针对HVS 1和HVA 1中任何一种病毒的抗血清，从感染这两种病毒的细胞中沉淀出一种分子量约为75 - 80 k的糖蛋白。此外，还为其中五种病毒鉴定出了至少一种在反应性上似乎主要具有病毒特异性的糖蛋白。
