Eisenberg R J, Ponce de Leon M, Cohen G H
J Virol. 1980 Aug;35(2):428-35. doi: 10.1128/JVI.35.2.428-435.1980.
We studied the synthesis and processing of the type-common glycoprotein gD in herpes simplex virus type 2 (HSV-2) and compared it structurally to glycoprotein gD of herpes simplex virus type 1 (HSV-1). We demonstrated that in HSV-2, gD undergoes posttranslational processing from a lower-molecular-weight precursor (pgD51) to a higher-molecular-weight product (gD56). Tryptic peptide analysis by cation-exchange chromatography indicated that this processing step altered neither the methionine nor the arginine tryptic peptide profile of gD of HSV-2. Comparative tryptic peptide analysis of gD of HSV-1 and HSV-2 showed that the methionine and arginine tryptic peptide profiles of these two proteins were very similar, but not identical. Some of the resolved peptides coeluted from the cation-exchange column, suggesting that some amino acid sequences of the two proteins might be very similar. However, each protein also appeared to possess several type-specific tryptic peptides. The structural similarity of these two glycoproteins correlates well with their antigenic cross-reactivity since monoprecipitin antibody to gD of HSV-1 also immunoprecipitates gD of HSV-2 and neutralizes the infectivity of both viruses to approximately the same extent.
我们研究了单纯疱疹病毒2型（HSV - 2）中共同型糖蛋白gD的合成与加工，并在结构上与单纯疱疹病毒1型（HSV - 1）的糖蛋白gD进行了比较。我们证明，在HSV - 2中，gD经历了从较低分子量前体（pgD51）到较高分子量产物（gD56）的翻译后加工。通过阳离子交换色谱法进行的胰蛋白酶肽分析表明，这一加工步骤既未改变HSV - 2的gD的甲硫氨酸胰蛋白酶肽谱，也未改变其精氨酸胰蛋白酶肽谱。对HSV - 1和HSV - 2的gD进行的比较胰蛋白酶肽分析表明，这两种蛋白质的甲硫氨酸和精氨酸胰蛋白酶肽谱非常相似，但并不完全相同。一些分离出的肽从阳离子交换柱上共同洗脱，表明这两种蛋白质的一些氨基酸序列可能非常相似。然而，每种蛋白质似乎也都拥有几种类型特异性的胰蛋白酶肽。这两种糖蛋白的结构相似性与其抗原交叉反应性密切相关，因为针对HSV - 1的gD的单沉淀抗体也能免疫沉淀HSV - 2的gD，并在大致相同程度上中和两种病毒的感染性。
