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Journal of Virology, May 2003, p. 5639-5648, Vol. 77, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.10.5639-5648.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Transcriptional Regulatory Properties of Epstein-Barr Virus Nuclear Antigen 3C Are Conserved in Simian Lymphocryptoviruses

Bo Zhao,1,2,{dagger} Rozenn Dalbiès-Tran,1,{ddagger} Hua Jiang,3 Ingrid K. Ruf,1 Jeffery T. Sample,1,2 Fred Wang,3 and Clare E. Sample1,2*

Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38105,1 Department of Pathology, University of Tennessee College of Medicine, Memphis, Tennessee 38163,2 Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 021153

Received 10 December 2002/ Accepted 21 February 2003

Epstein-Barr virus (EBV) nuclear antigen 3C (EBNA-3C) is a large transcriptional regulator essential for EBV-mediated immortalization of B lymphocytes. We previously identified interactions between EBNA-3C and two cellular transcription factors, J{kappa} and Spi proteins, through which EBNA-3C regulates transcription. To better understand the contribution of these interactions to EBNA-3C function and EBV latency, we examined whether they are conserved in the homologous proteins of nonhuman primate lymphocryptoviruses (LCVs), which bear a strong genetic and biological similarity to EBV. The homologue of EBNA-3C encoded by the LCV that infects baboons (BaLCV) was found to be only 35% identical in sequence to its EBV counterpart. Of particular significance, this homology localized predominantly to the N-terminal half of the molecule, which encompasses the domains in EBNA-3C that interact with J{kappa} and Spi proteins. Like EBNA-3C, both BaLCV and rhesus macaque LCV (RhLCV) 3C proteins bound to J{kappa} and repressed transcription mediated by EBNA-2 through its interaction with J{kappa}. Both nonhuman primate 3C proteins were also able to activate transcription mediated by the Spi proteins in the presence of EBNA-2. Like EBNA-3C, a domain encompassing the putative basic leucine zipper motif of the BaLCV-3C protein directly interacted with both Spi-1 and Spi-B. Surprisingly, a recently identified motif in EBNA-3C that mediates repression was not identifiable in the BaLCV-3C protein. Finally, although the C terminus of BaLCV-3C bears minimal homology to EBNA-3C, it nonetheless contains a C-terminal domain rich in glutamine and proline that was able to function as a potent transcriptional activation domain, as does the C terminus of EBNA-3C. The conservation of these functional motifs despite poor overall homology among the LCV 3C proteins strongly suggests that the interactions of EBNA-3C with J{kappa} and Spi do indeed play significant roles in the life cycle of EBV.

* Corresponding author. Mailing address: Department of Biochemistry, St. Jude Children's Research Hospital, 332 N. Lauderdale St., Memphis, TN 38105. Phone: (901) 495-3416. Fax: (901) 525-8025. E-mail: clare.sample{at}stjude.org.

{dagger} Present address: Department of Microbiology and Molecular Genetics, Channing Laboratory, Harvard Medical School, Boston, MA 02115.

{ddagger} Present address: UMR 6073, Institut Nationale de La Recherche Agronomique, Centre National de la Recherche Scientifique, Université de Tours, Nouzilly F-37380, France.

Journal of Virology, May 2003, p. 5639-5648, Vol. 77, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.10.5639-5648.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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