Abstract
The purified Mr 340,000 glycoprotein component of Epstein-Barr (EB) virus-induced membrane antigen complex incorporated into liposomes was shown to be a potent immunogen in mice. High-titer antisera were induced that (i) are specific for membrane antigen components without absorption, (ii) bind the antigens induced by three different EB virus isolates, and (iii) neutralize the ability of the virus to transform fetal cord blood lymphocytes in vitro. The development of this immunogenic form of purified antigen provides an important step towards a potential subunit vaccine against Epstein-Barr virus infection.
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