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Originally published as JGV in Press, 10.1099/vir.0.010462-0 on March 25, 2009 J Gen Virol 90 (2009), 1575-1581; DOI 10.1099/vir.0.010462-0

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Epstein–Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity

Risa Asai1,2, Ai Kato2 and Yasushi Kawaguchi1,2

1 Division of Viral Infection, Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108-8639, Japan
2 Department of Virology, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550, Japan

Correspondence
Yasushi Kawaguchi
ykawagu{at}ims.u-tokyo.ac.jp

BGLF4 is a serine/threonine protein kinase encoded by Epstein–Barr virus. One of the physiological substrates of BGLF4 is viral transactivator BZLF1. In the present study, it was demonstrated that alanine substitution of the serine residue at position 209 (S209A) in BZLF1 eliminated phosphorylation of the protein by BGLF4 in vitro. The S209A mutation in BZLF1, as well as a K102I mutation in BGLF4, which inactivated catalytic activity of the viral kinase, also inhibited formation of a stable BGLF4–BZLF1 complex and downregulation of BZLF1 autotransactivation activity mediated by BGLF4. These results indicate that formation of a stable complex of BGLF4–BZLF1 enables downregulation of BZLF1 autoregulation activity and it appears that BGLF4 phosphorylation of BZLF1 may be involved in these processes.






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