Identification and isolation of the main component (gp350-gp220) of Epstein-Barr virus responsible for generating neutralizing antibodies in vivo.
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.
D000818:Animals; D000914:Antibodies, Viral / Q000096:biosynthesis*; D002051:Burkitt Lymphoma / Q000276:immunology*; D006023:Glycoproteins / Q000276:immunology* / Q000302:isolation & purification; D004854:Herpesvirus 4, Human / Q000276:immunology*; D006801:Humans; D007124:Immunoenzyme Techniques; D008854:Microscopy, Electron; D009500:Neutralization Tests; D011817:Rabbits; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000276:immunology* / Q000302:isolation & purification
D000914:Antibodies, Viral; D006023:Glycoproteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins