LOCALIZATION OF EPITOPES OF HERPES-SIMPLEX VIRUS TYPE-1 GLYCOPROTEIN-D
LOCALIZATION OF EPITOPES OF HERPES-SIMPLEX VIRUS TYPE-1 GLYCOPROTEIN-D
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DOI：
10.1128/jvi.53.2.634-644.1985
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发表时间：
1985-01-01
影响因子：
5.4
通讯作者：
COHEN, GH
中科院分区：
文献类型：
--
作者：
EISENBERG, RJ;LONG, D;COHEN, GH
确定了8组与单纯疱疹病毒糖蛋白D （gD）不同表位反应的单克隆抗体。其中之一，VII组抗体，被证明与成熟糖蛋白残基11-19 （gD预测序列残基36-44）内的型共连续表位发生反应。在目前的研究中，.apprx的结合位点。另外还定位了识别gD连续表位的抗体群。利用gD的截断形式以及二级结构和亲水性的计算机预测有助于定位这些表位和选择合成肽来模拟它们的反应性。II组抗体是常见的，与成熟糖蛋白残基268-287（预测序列残基293-312）内的表位反应。V组抗体是gD-1特异性的，与成熟蛋白的340 - 356残基内的表位反应（预测序列的365-381残基）。另外四组单克隆抗体似乎与gD-1的不连续表位发生反应，因为当糖蛋白被还原和烷基化变性时，这些抗体的反应性丧失。利用gD的截断形式将这4个表位定位到成熟蛋白的前260个氨基酸上。利用竞争实验评估不同对单克隆抗体的相对结合位置。在一些情况下，当1个抗体结合时，没有干扰另一组抗体的结合，表明表位是不同的。在其他情况下，存在竞争，表明这些表位可能共享一些共同的氨基酸。
Eight groups of monoclonal antibodies which react with distinct epitopes of herpes simplex virus glycoprotein D (gD) were defined. One of these, group VII antibody, was shown to react with a type-common continuous epitope within residues 11-19 of the mature glycoprotein (residues 36-44 of the predicted sequence of gD). In the current investigation, the sites of binding of .apprx. additional antibody groups which recognize continuous epitopes of gD were localized. The use of truncated forms of gD as well as computer predictions of secondary structure and hydrophilicity were instrumental in locating these epitopes and choosing synthetic peptides to mimic their reactivity. Group II antibodies, which are type common, react with an epitope within residues 268-287 of the mature glycoprotein (residues 293-312 of the predicted sequence). Group V antibodies, which are gD-1 specific, react with an epitope within residues 340 to 356 of the mature protein (residues 365-381 of the predicted sequence). Four additional groups of monoclonal antibodies appear to react with discontinuous epitopes of gD-1, since the reactivity of these antibodies was lost when the glycoprotein was denatured by reduction and alkylation. Truncated forms of gD were used to localize these 4 epitopes to the first 260 amino acids of the mature protein. Competition experiments were used to assess the relative positions of binding of various pairs of monoclonal antibodies. In several cases, when 1 antibody was bound, there was no interference with the binding of an antibody from another group, indicating that the epitopes were distinct. In other cases, there was competition, indicating that these epitopes might share some common amino acids.