ArticleJournal of virology2001
Amino acids of Epstein-Barr virus nuclear antigen 3A essential for repression of Jkappa-mediated transcription and their evolutionary conservation.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Review
- An EBNA3C-deleted Epstein-Barr virus (EBV) mutant causes B-cell lymphomas with delayed onset in a cord blood-humanized mouse model.PLoS pathogens · 2018Article
- Epstein-Barr Virus Nuclear Antigen 3 (EBNA3) Proteins Regulate EBNA2 Binding to Distinct RBPJ Genomic Sites.Journal of virology · 2015Article
- Epstein-Barr virus nuclear antigen 3A partially coincides with EBNA3C genome-wide and is tethered to DNA through BATF complexes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The nucleotide polymorphisms within the Epstein-Barr virus C and Q promoters from nasopharyngeal carcinoma affect transcriptional activity in vitro.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2012Article
- Article
- Differential gene expression patterns of EBV infected EBNA-3A positive and negative human B lymphocytes.PLoS pathogens · 2009Article
- Epstein-Barr virus nuclear protein EBNA3C residues critical for maintaining lymphoblastoid cell growth.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Epstein-Barr virus EBNA-3C is targeted to and regulates expression from the bidirectional LMP-1/2B promoter.Journal of virology · 2006Article
- Epstein-Barr virus nuclear protein 3A domains essential for growth of lymphoblasts: transcriptional regulation through RBP-Jkappa/CBF1 is critical.Journal of virology · 2005Article
- Epstein-Barr Virus nuclear protein EBNA3A is critical for maintaining lymphoblastoid cell line growth.Journal of virology · 2003Article
- Transcriptional regulatory properties of Epstein-Barr virus nuclear antigen 3C are conserved in simian lymphocryptoviruses.Journal of virology · 2003Article
- EBNA3A association with RBP-Jkappa down-regulates c-myc and Epstein-Barr virus-transformed lymphoblast growth.Journal of virology · 2003Article
- Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase.BMC cell biology · 2002Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Epstein-Barr virus (EBV) nuclear antigen 3A (EBNA-3A) is essential for virus-mediated immortalization of B lymphocytes in vitro and is believed to regulate transcription of cellular and/or viral genes. One known mechanism of regulation is through its interaction with the cellular transcription factor Jkappa. This interaction downregulates transcription mediated by EBNA-2 and Jkappa. To identify the amino acids that play a role in this interaction, we have generated mutant EBNA-3A proteins. A mutant EBNA-3A protein in which alanine residues were substituted for amino acids 199, 200, and 202 no longer downregulated transcription. Surprisingly, this mutant protein remained able to coimmunoprecipitate with Jkappa. Using a reporter gene assay based on the recruitment of Jkappa by various regions spanning EBNA-3A, we have shown that this mutation abolished binding of Jkappa to the N-proximal region (amino acids 125 to 222) and that no other region of EBNA-3A alone was sufficient to mediate an association with Jkappa. To determine the biological significance of the interaction of EBNA-3A with Jkappa, we have studied its conservation in the simian lymphocryptovirus herpesvirus papio (HVP) by cloning HVP-3A, the homolog of EBNA-3A encoded by this virus. This 903-amino-acid protein exhibited 37% identity with its EBV counterpart, mainly within the amino-terminal half. HVP-3A also interacted with Jkappa through a region located between amino acids 127 and 223 and also repressed transcription mediated through EBNA-2 and Jkappa. The evolutionary conservation of this function, in proteins that have otherwise significantly diverged, argues strongly for an important biological role in virus-mediated immortalization of B lymphocytes.
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