Abstract
The majority of hybridomas that were 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 immuno-EM. Lectin affinity (ricin) and immunoaffinity (ID4C-1) was used to purify gp350/220 and this material was able to induce potent virus-neutralizing antibodies. Absorption of 4 human and 1 rabbit anti-Epstein-Barr virus sera with purified gp350/220 suggests that this is the primary component responsible for generating neutralizing antibodies in vivo.

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