| Literature DB >> 6287039 |
D A Thorley-Lawson, C A Poodry.
Abstract
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.Entities:
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Year: 1982 PMID: 6287039 PMCID: PMC256176
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103