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Journal of Virology, December 2008, p. 11913-11926, Vol. 82, No. 23
0022-538X/08/$08.00+0     doi:10.1128/JVI.01100-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Epstein-Barr Virus BGLF4 Kinase Induces Disassembly of the Nuclear Lamina To Facilitate Virion Production{triangledown}

Chung-Pei Lee,1 Yu-Hao Huang,1 Su-Fang Lin,2 Yao Chang,3 Yu-Hsin Chang,1 Kenzo Takada,4 and Mei-Ru Chen1*

Graduate Institute and Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan,1 Institute of Cancer Research,2 Division of Clinical Research, National Health Research Institutes, Zhunan, Taiwan,3 Department of Tumor Virology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan4

Received 25 May 2008/ Accepted 16 September 2008

DNA viruses adopt various strategies to modulate the cellular environment for efficient genome replication and virion production. Previously, we demonstrated that the BGLF4 kinase of Epstein-Barr virus (EBV) induces premature chromosome condensation through the activation of condensin and topoisomerase II{alpha} (C. P. Lee, J. Y. Chen, J. T. Wang, K. Kimura, A. Takemoto, C. C. Lu, and M. R. Chen, J. Virol. 81:5166-5180, 2007). In this study, we show that BGLF4 interacts with lamin A/C and phosphorylates lamin A protein in vitro. Using a green fluorescent protein (GFP)-lamin A system, we found that Ser-22, Ser-390, and Ser-392 of lamin A are important for the BGLF4-induced disassembly of the nuclear lamina and the EBV reactivation-mediated redistribution of nuclear lamin. Virion production and protein levels of two EBV primary envelope proteins, BFRF1 and BFLF2, were reduced significantly by the expression of GFP-lamin A(5A), which has five Ser residues replaced by Ala at amino acids 22, 390, 392, 652, and 657 of lamin A. Our data indicate that BGLF4 kinase phosphorylates lamin A/C to promote the reorganization of the nuclear lamina, which then may facilitate the interaction of BFRF1 and BFLF2s and subsequent virion maturation. UL kinases of alpha- and betaherpesviruses also induce the disassembly of the nuclear lamina through similar sites on lamin A/C, suggesting a conserved mechanism for the nuclear egress of herpesviruses.

* Corresponding author. Mailing address: No. 1, 1st Sec. Jen-Ai Road, Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Taipei 10051, Taiwan. Phone: 886-2-23123456, ext. 88298. Fax: 886-2-23915293. E-mail: mrc{at}ntu.edu.tw

{triangledown} Published ahead of print on 24 September 2008.

Journal of Virology, December 2008, p. 11913-11926, Vol. 82, No. 23
0022-538X/08/$08.00+0     doi:10.1128/JVI.01100-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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