Torrance L
Virology Department, Scottish Crop Research Institute, Invergowrie, Dundee, United Kingdom.
Virology. 1992 Nov;191(1):485-9. doi: 10.1016/0042-6822(92)90216-c.
Pepscan hexapeptides prepared to the capsid protein amino acid sequence of potato leafroll luteovirus (PLRV) were tested against both polyclonal and monoclonal antibodies. Twelve continuous epitopes were identified: 11 were detected by two different PLRV polyclonal antisera, but only 4 were detected by both antisera. The 12th epitope reacted with monoclonal antibody BG3. The location of most of the epitopes did not correlate well with antigenic areas predicted by computer algorithms. Comparison of the amino acid sequences of PLRV and southern bean mosaic virus capsid proteins allowed a preliminary assignment of epitopes 4-12 to different regions of the putative S domain of the PLRV subunit. Five out of 14 monoclonal antibodies and both of the polyclonal antisera reacted with epitope 1 at the N-terminus. ELISA data indicated that even though the N-terminus is hydrophobic, it is exposed at the surface of the particles.
针对马铃薯卷叶黄矮病毒（PLRV）衣壳蛋白氨基酸序列制备的Pepscan六肽，对多克隆抗体和单克隆抗体进行了测试。鉴定出12个连续表位：11个被两种不同的PLRV多克隆抗血清检测到，但两种抗血清都检测到的只有4个。第12个表位与单克隆抗体BG3发生反应。大多数表位的位置与计算机算法预测的抗原区域相关性不佳。比较PLRV和南方菜豆花叶病毒衣壳蛋白的氨基酸序列，可将表位4 - 12初步定位到PLRV亚基假定S结构域的不同区域。14种单克隆抗体中有5种以及两种多克隆抗血清与N端的表位1发生反应。酶联免疫吸附测定（ELISA）数据表明，尽管N端具有疏水性，但它暴露在病毒颗粒表面。
