Luka J, Kreofsky T, Pearson G R, Hennessy K, Kieff E
J Virol. 1984 Dec;52(3):833-8. doi: 10.1128/JVI.52.3.833-838.1984.
A 62,000-dalton (62K) cell protein reacts with antisera to the 72K polypeptide of the Epstein-Barr virus nuclear antigen (EBNA) in immunoblots. This protein was initially detected in EBNA-negative as well as EBNA-positive cell lines with anti-EBNA-positive human sera. A monoclonal antibody raised against the 72K EBNA and an antiserum from a rabbit immunized with the glycine-alanine domain of EBNA also reacted with the cellular protein. The cellular protein was partially purified from Epstein-Barr virus genome-positive and -negative cell lines. Absorption experiments identified a shared antigenic determinant between the 72K EBNA and 62K cellular protein. A comparison of the 62K protein and EBNA by protease digestion did not reveal similar peptides.
一种62,000道尔顿(62K)的细胞蛋白在免疫印迹中与抗爱泼斯坦-巴尔病毒核抗原(EBNA)的72K多肽的抗血清发生反应。该蛋白最初是在EBNA阴性以及EBNA阳性细胞系中用抗EBNA阳性的人血清检测到的。一种针对72K EBNA产生的单克隆抗体以及用EBNA的甘氨酸-丙氨酸结构域免疫的兔子的抗血清也与该细胞蛋白发生反应。该细胞蛋白从爱泼斯坦-巴尔病毒基因组阳性和阴性细胞系中进行了部分纯化。吸收实验确定了72K EBNA和62K细胞蛋白之间存在共同的抗原决定簇。通过蛋白酶消化对62K蛋白和EBNA进行比较,未发现相似的肽段。