Eisenberg R J, Long D, Pereira L, Hampar B, Zweig M, Cohen G H
J Virol. 1982 Feb;41(2):478-88. doi: 10.1128/JVI.41.2.478-488.1982.
We examined the properties of 17 monoclonal antibodies to glycoprotein gD of herpes simplex type 1 (HSV-1) (gD-1) and HSV-2 (gD-2). The antibodies recognized eight separate determinants of gD, based on differences in radioimmuno-precipitation and neutralization assays. The determinants were distributed as follows: three were gD-1 specific, one was gD-2 specific, and four were type common. Several type-specific and type-common determinants appeared to be involved in neutralization. We developed a procedure for examining the effect that binding of monoclonal antibody has on proteolysis of native gD-1 by Staphylococcus aureus protease V8. We showed that several different patterns of protease V8 cleavage were obtained, depending on the monoclonal antibody used. The proteolysis patterns were generally consistent with the immunological groupings. With four groups of antibodies, we found that fragments of gD-1 remained bound to antibody after V8 treatment. A 38,000-dalton fragment remained bound to antibodies in three different groups of monoclonal antibodies. This fragment appeared to contain one type-common and two type-specific determinants. A 12,000-dalton fragment remained bound to antibodies belonging to one type-common group of monoclonal antibodies. Tryptic peptide analysis revealed that the 12,000-dalton fragment represented a portion of the 38,000-dalton fragment and was enriched in a type-common arginine tryptic peptide.
我们检测了17种针对单纯疱疹病毒1型（HSV-1）糖蛋白gD（gD-1）和HSV-2糖蛋白gD（gD-2）的单克隆抗体的特性。基于放射免疫沉淀和中和试验的差异，这些抗体识别gD的8个不同决定簇。这些决定簇分布如下：3个是gD-1特异性的，1个是gD-2特异性的，4个是两型共有的。几种型特异性和型共有决定簇似乎参与了中和作用。我们开发了一种程序来检测单克隆抗体结合对金黄色葡萄球菌蛋白酶V8对天然gD-1进行蛋白水解的影响。我们发现，根据所使用的单克隆抗体不同，可获得几种不同的蛋白酶V8切割模式。蛋白水解模式通常与免疫学分组一致。对于四组抗体，我们发现V8处理后gD-1片段仍与抗体结合。在三组不同的单克隆抗体中，一个38000道尔顿的片段仍与抗体结合。该片段似乎包含一个型共有和两个型特异性决定簇。一个12000道尔顿的片段仍与属于一个型共有单克隆抗体组的抗体结合。胰蛋白酶肽分析表明，12000道尔顿的片段代表38000道尔顿片段的一部分，并且富含一个型共有的精氨酸胰蛋白酶肽。
