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Journal of Virology, March 2001, p. 2482-2487, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2482-2487.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Epstein-Barr Virus Nuclear Protein 2 Has at Least Two N-Terminal Domains That Mediate Self-Association

Shizuko Harada,dagger Ramana Yalamanchili, and Elliott Kieff*

Program in Virology and Departments of Medicine and Microbiology and Molecular Genetics, Channing Laboratory, Brigham and Women's Hospital and Harvard University, Boston, Massachusetts 02115

Received 1 September 2000/Accepted 28 November 2000

Previous genetic and biochemical analyses have indicated that the Epstein-Barr virus EBNA-2 amino terminus is important for primary B-lymphocyte growth transformation and may be involved in self-association. We now report that EBNA-2 has at least two domains, amino acids 1 to 60 and 96 to 210, which independently mediate homotypic association, 1 to 60 with 1 to 60 and 96 to 210 with 96 to 210. EBNA-2 self-association is likely to be critical to the ability of EBNA-2 to interact simultaneously with multiple cellular transcription factors, coactivators, and histone acetyltransferases through its RBPJkappa binding and acidic activating domains.

* Corresponding author. Mailing address: Program in Virology and Departments of Medicine and Microbiology and Molecular Genetics, Channing Laboratory, Brigham and Women's Hospital and Harvard University, 181 Longwood Ave., Boston, MA 02115. Phone: (617) 525-4252. Fax: (617) 525-4257. E-mail: ekieff{at}rics.bwh.harvard.edu.

dagger Present address: Department of Microbiology, St. Marianna University School of Medicine, Kawasaki 216-8511, Japan.

Journal of Virology, March 2001, p. 2482-2487, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2482-2487.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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