Kishishita M, Luka J, Vroman B, Poduslo J F, Pearson G R
Virology. 1984 Mar;133(2):363-75. doi: 10.1016/0042-6822(84)90402-1.
A monoclonal antibody designated L2 was produced against a late intracellular protein induced by Epstein-Barr virus (EBV). This protein was expressed in cells producing virus but not in EBV genome-positive nonproducer cell lines, EBV genome-negative cell lines, or producer cultures cultivated in the presence of phosphonoacetic acid as determined by immunofluorescence. In addition, the antibody did not react with the membranes of infected cells indicating that it was not directed against an EBV-induced membrane antigen component. The monoclonal antibody was shown to recognize a glycoprotein with a molecular weight of approximately 125K by SDS-polyacrylamide gel electrophoresis. This glycoprotein was consistently found to be slightly larger when isolated from the P3HR-1 cell line as opposed to the B-95-8 cell line. A similar difference was also noted by comparison of peptide maps of this protein isolated by immunoaffinity chromatography from the two cell lines. Serological studies indicated that this 125K glycoprotein was a major component of the viral capsid-antigen (VCA) complex as defined by immunofluorescence.
一种名为L2的单克隆抗体是针对由爱泼斯坦-巴尔病毒（EBV）诱导产生的一种晚期细胞内蛋白制备的。通过免疫荧光测定，这种蛋白在产生病毒的细胞中表达，但在EBV基因组阳性的非生产细胞系、EBV基因组阴性细胞系或在膦甲酸存在下培养的生产性培养物中不表达。此外，该抗体不与受感染细胞的膜发生反应，表明它不是针对EBV诱导的膜抗原成分。通过SDS-聚丙烯酰胺凝胶电泳显示，该单克隆抗体识别一种分子量约为125K的糖蛋白。与从B-95-8细胞系中分离相比，从P3HR-1细胞系中分离时，这种糖蛋白始终略大。通过免疫亲和层析从这两种细胞系中分离该蛋白的肽图比较也发现了类似的差异。血清学研究表明，这种125K糖蛋白是免疫荧光所定义的病毒衣壳抗原（VCA）复合物的主要成分。
