Purified Epstein-Barr virus Mr 340,000 glycoprotein induces potent virus-neutralizing antibodies when incorporated in liposomes.
AUTOR(ES)
North, J R
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=347368Documentos Relacionados
- Recombinant vaccinia virus induces neutralising antibodies in rabbits against Epstein-Barr virus membrane antigen gp340.
- Proteins of purified Epstein-Barr virus
- Proteins of Epstein-Barr virus. I. Analysis of the polypeptides of purified enveloped Epstein-Barr virus.
- Monoclonal antibody against a 250,000-dalton glycoprotein of Epstein-Barr virus identifies a membrane antigen and a neutralizing antigen.
- Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo.
