Thorley-Lawson D A, Poodry C A
J Virol. 1982 Aug;43(2):730-6. doi: 10.1128/JVI.43.2.730-736.1982.
The majority of hybridomas we have characterized against Epstein-Barr virions react with the major glycoproteins gp350 and gp220 (gp350/220). One of these antibodies, ID4C-1, neutralizes virus infection in vitro. The presence of gp350/220 on the viral envelope could be confirmed directly by immunoelectron microscopy. We used lectin affinity (ricin) and immunoaffinity (ID4C-1) to purify gp350/220 and show that this material is able to induce potent virus-neutralizing antibodies. Absorption of four human and one rabbit anti-Epstein-Barr virus sera with purified gp350/220 suggests that this is the primary component responsible for generating neutralizing antibodies in vivo.
我们已鉴定出的大多数针对爱泼斯坦-巴尔病毒粒子的杂交瘤与主要糖蛋白gp350和gp220(gp350/220)发生反应。其中一种抗体ID4C-1可在体外中和病毒感染。通过免疫电子显微镜可直接证实病毒包膜上存在gp350/220。我们利用凝集素亲和法(蓖麻毒素)和免疫亲和法(ID4C-1)纯化gp350/220,并证明该物质能够诱导产生强效的病毒中和抗体。用纯化的gp350/220吸收四份人抗爱泼斯坦-巴尔病毒血清和一份兔抗爱泼斯坦-巴尔病毒血清表明,这是在体内产生中和抗体的主要成分。