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Published online ahead of print on 25 March 2009 as doi:10.1099/vir.0.010462-0
Journal of General Virology 2009;90:1575.

A more recent version of this article appeared on July 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.010462-0
© 2009 Society for General Microbiology
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Epstein-Barr Virus Protein Kinase BGLF4 Interacts with Viral Transactivator BZLF1 and Regulates Its Transactivation Activity

Risa Asai1, Ai Kato2 and Yasushi Kawaguchi1,3

1 Institute of Medical Science, The University of Tokyo;
2 Nagoya University Graduate School of Medicine

3 E-mail: ykawagu{at}ims.u-tokyo.ac.jp

BGLF4 is a serine-threonine protein kinase encoded by Epstein-Barr virus and one of the physiological BGLF4 substrates is viral transactivator BZLF1. In the present study, we demonstrated that alanine substitution of serine residue at position 209 (S209A) in the BZLF1 abrogated phosphorylation of the protein by BGLF4 in vitro. The S209A mutation in BZLF1 as well as K102I mutation in BGLF4, which inactivated catalytic activity of the viral kinase, also inhibited formation of a stable BGLF4-BZLF1 complex and down-regulation of BZLF1 auto-transactivation activity mediated by BGLF4. Our results indicated that formation of a stable complex with BGLF4-BZLF1 enabled down-regulation of BZLF1 auto-regulation activity and it appeared that BGLF4 phosphorylation of BZLF1 might be involved in these processes.

Received 21 January 2009; accepted 23 March 2009.




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