Identification of a poliovirus neutralization epitope through use of neutralizing antiserum raised against a purified viral structural protein.
Identification of a poliovirus neutralization epitope through use of neutralizing antiserum raised against a purified viral structural protein.
复制标题
通过使用针对纯化的病毒结构蛋白产生的中和抗血清来鉴定脊髓灰质炎病毒中和表位。
DOI：
10.1016/0042-6822(83)90297-0
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发表时间：
1983
期刊：
影响因子：
3.7
通讯作者：
Wimmer,E
中科院分区：
文献类型：
--
作者：
Emini,EA;Dorner,AJ;Dorner,LF;Jameson,BA;Wimmer,E
纯化脊髓灰质炎病毒结构蛋白VP4，制备兔抗VP4血清。除抗VP4活性外，还发现该血清含有显著的抗VP3和抗病毒体活性。血清还有效地中和了病毒感染性。获得不可中和的变体的容易性表明中和是由于与单个病毒体表位结合的抗体群体。抗原饱和和免疫沉淀实验表明，该表位的抗体也负责血清的抗病毒体和抗VP3活性，以及部分抗VP4活性。最有可能存在于VP3上的中和表位的鉴定，其与变性VP4上的位点交叉反应，是首次报道这种表位在除VP1之外的脊髓灰质炎病毒结构蛋白上。
VP4, one of the poliovirus structural proteins, was purified and used to prepare rabbit anti-VP4 serum. In addition to the anti-VP4 activity, this serum was also found to contain significant anti-VP3 and antivirion activities. The serum also effectively neutralized viral infectivity. The ease with which nonneutralizable variants were obtained indicated that neutralization was due to an antibody population which bound to a single virion epitope. Antigen saturation and immunoprecipitation experiments demonstrated that antibody to this epitope was also responsible for the serum's antivirion and anti-VP3 activities, as well as for a part of the anti-VP4 activity. The identification of a neutralization epitope most probably present on VP3, which cross-reacts with a site on denatured VP4, is the first report of such an epitope on a poliovirus structural protein other than VP1.