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Journal of Virology, April 2004, p. 3919-3929, Vol. 78, No. 8
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.8.3919-3929.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030,1 Institut für Molekulare Immunologie, GSF Forschungszentrum für Umwelt und Gesundheit, Munich, Germany2
Received 18 September 2002/ Accepted 7 January 2004
Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2), a direct transcriptional activator of viral and cellular genes, is required for EBV-induced B-cell transformation. The functional role of conserved regions within the amino terminus of the protein preceding the poly-proline region has yet to be fully characterized. Thus, we tested whether the EBNA2 amino-terminal 30 amino acid residues, containing evolutionarily conserved region 1, are required for stimulating viral and cellular gene expression necessary for B-cell transformation in a viral transcomplementation assay. We found that these residues are required for its ability to induce LMP-1 expression in lymphoblastoid cell lines (LCLs), to stimulate LMP-1 promoter reporter plasmids in transient-cotransfection assays, and to rescue LCL growth following inactivation of endogenous wild-type EBNA2 protein. Deletion of amino acid residues 3 to 30 also impaired its ability to self-associate in coimmunoprecipitation assays. These data indicate that EBNA2 residues 3 to 30 comprise an essential domain required for induction of LMP-1 expression and, consequently, for maintenance of the immortalized phenotype of LCLs. The ability to self-associate into dimers or multimers conferred by this domain may be an important mechanism for these effects.
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