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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 IIalpha (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.

Titel:	Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production.
Autor/in / Beteiligte Person:	Lee, CP ; Huang, YH ; Lin, SF ; Chang, Y ; Chang, YH ; Takada, K ; Chen, MR
Zeitschrift:	Journal of virology, Jg. 82 (2008-12-01), Heft 23, S. 11913-26
Veröffentlichung:	Washington Dc : American Society For Microbiology ; <i>Original Publication</i>: Baltimore, American Society for Microbiology., 2008
Medientyp:	academicJournal
ISSN:	1098-5514 (electronic)
DOI:	10.1128/JVI.01100-08
Schlagwort:	Adenosine Triphosphatases metabolism Antigens, Neoplasm metabolism DNA Topoisomerases, Type II metabolism DNA-Binding Proteins metabolism HeLa Cells Humans Lamin Type A chemistry Lamin Type A physiology Membrane Proteins physiology Multiprotein Complexes metabolism Phosphorylation Protein Kinases physiology Virus Activation Herpesvirus 4, Human physiology Nuclear Lamina metabolism Protein Serine-Threonine Kinases physiology Viral Proteins physiology Virion physiology
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [J Virol] 2008 Dec; Vol. 82 (23), pp. 11913-26. <i>Date of Electronic Publication: </i>2008 Sep 24. MeSH Terms: Herpesvirus 4, Human / physiology ; Nuclear Lamina / metabolism ; Protein Serine-Threonine Kinases / physiology ; Viral Proteins / physiology ; Virion / *physiology ; Adenosine Triphosphatases / metabolism ; Antigens, Neoplasm / metabolism ; DNA Topoisomerases, Type II / metabolism ; DNA-Binding Proteins / metabolism ; HeLa Cells ; Humans ; Lamin Type A / chemistry ; Lamin Type A / physiology ; Membrane Proteins / physiology ; Multiprotein Complexes / metabolism ; Phosphorylation ; Protein Kinases / physiology ; Virus Activation References: J Biol Chem. 2001 Feb 23;276(8):5417-20. (PMID: 11136719) ; Lab Invest. 1990 Jun;62(6):713-24. (PMID: 2162997) ; Science. 2002 Aug 2;297(5582):854-7. (PMID: 12161659) ; J Virol. 2002 Sep;76(17):8939-52. (PMID: 12163613) ; J Virol. 2003 Feb;77(4):2359-68. (PMID: 12551973) ; Traffic. 2003 Mar;4(3):136-43. (PMID: 12656986) ; Chromosoma. 1990 Dec;100(1):67-9. (PMID: 2102440) ; J Virol Methods. 1991 Jun;33(1-2):47-52. (PMID: 1719014) ; FEBS Lett. 1991 Nov 4;292(1-2):205-9. (PMID: 1959608) ; FEBS Lett. 1992 Apr 13;301(1):111-4. (PMID: 1451779) ; Cancer Res. 1993 Aug 1;53(15):3591-6. (PMID: 8393377) ; Curr Biol. 1994 Nov 1;4(11):973-82. (PMID: 7874496) ; Eur J Biochem. 1995 Jul 15;231(2):491-7. (PMID: 7635160) ; Int Rev Cytol. 1995;162B:141-82. (PMID: 8557486) ; J Virol. 1999 Oct;73(10):8857-66. (PMID: 10482644) ; J Cell Sci. 1999 Oct;112 ( Pt 20):3463-75. (PMID: 10504295) ; Nat Rev Mol Cell Biol. 2005 Jan;6(1):21-31. (PMID: 15688064) ; J Virol. 2005 Mar;79(6):3703-12. (PMID: 15731264) ; J Virol. 2005 Mar;79(6):3713-27. (PMID: 15731265) ; J Gen Virol. 2007 Dec;88(Pt 12):3234-43. (PMID: 18024891) ; Nature. 2007 Nov 29;450(7170):695-701. (PMID: 18046406) ; J Gen Virol. 2008 Apr;89(Pt 4):884-95. (PMID: 18343828) ; J Virol. 2000 Apr;74(7):3093-104. (PMID: 10708424) ; Oncogene. 2000 May 4;19(19):2331-7. (PMID: 10822384) ; Biotechniques. 2000 Nov;29(5):970-2. (PMID: 11084856) ; Mol Biol Cell. 2000 Dec;11(12):4323-37. (PMID: 11102526) ; J Cell Sci. 2001 Jan;114(Pt 1):9-19. (PMID: 11112685) ; J Virol. 2005 May;79(9):5880-5. (PMID: 15827205) ; J Biol Chem. 2005 Sep 30;280(39):33357-67. (PMID: 15975922) ; J Gen Virol. 2005 Dec;86(Pt 12):3215-25. (PMID: 16298966) ; J Virol. 2006 Jan;80(1):494-504. (PMID: 16352573) ; J Virol. 2006 Feb;80(3):1476-86. (PMID: 16415024) ; Virology. 2006 Apr 10;347(2):261-76. (PMID: 16427676) ; J Virol. 2006 Jun;80(11):5125-34. (PMID: 16698993) ; Physiol Rev. 2006 Jul;86(3):967-1008. (PMID: 16816143) ; Curr Opin Microbiol. 2006 Aug;9(4):423-9. (PMID: 16814597) ; J Virol. 2006 Oct;80(20):10064-72. (PMID: 17005684) ; J Virol. 2007 Mar;81(5):2459-71. (PMID: 17182691) ; J Virol. 2007 May;81(10):5166-80. (PMID: 17360754) ; J Virol. 2007 May;81(10):5407-12. (PMID: 17360761) ; J Virol. 2007 Jun;81(12):6459-70. (PMID: 17428859) ; Curr Opin Cell Biol. 2007 Jun;19(3):298-304. (PMID: 17466505) ; J Gen Virol. 2007 Oct;88(Pt 10):2642-50. (PMID: 17872514) ; Cell Host Microbe. 2007 Jun 14;1(4):275-86. (PMID: 18005708) ; J Gen Virol. 2003 Dec;84(Pt 12):3381-92. (PMID: 14645919) ; J Virol. 2004 Jan;78(1):399-412. (PMID: 14671121) ; J Virol. 2004 Jun;78(11):5564-75. (PMID: 15140953) ; Mol Biol Cell. 2004 Jul;15(7):3296-308. (PMID: 15146063) ; Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. (PMID: 15302935) ; Am J Anat. 1966 Jul;119(1):129-45. (PMID: 6007824) ; Nature. 1986 Feb 6-12;319(6053):463-8. (PMID: 3453101) ; Proc Natl Acad Sci U S A. 1986 Sep;83(17):6450-4. (PMID: 3462705) ; Nature. 1986 Oct 9-15;323(6088):560-4. (PMID: 3762708) ; J Virol. 1990 Apr;64(4):1507-16. (PMID: 2157039) ; Cell. 1990 May 18;61(4):561-77. (PMID: 2188730) ; Cell. 1990 May 18;61(4):579-89. (PMID: 2344612) ; Cell. 1990 May 18;61(4):591-602. (PMID: 2188731) ; J Virol. 2001 Sep;75(18):8803-17. (PMID: 11507225) Substance Nomenclature: 0 (Antigens, Neoplasm) ; 0 (BFRF1 protein, Human herpesvirus 4) ; 0 (DNA-Binding Proteins) ; 0 (Lamin Type A) ; 0 (Membrane Proteins) ; 0 (Multiprotein Complexes) ; 0 (Viral Proteins) ; 0 (condensin complexes) ; 0 (lamin C) ; EC 2.7.- (Protein Kinases) ; EC 2.7.1.- (BGLF4 protein, Epstein-Barr virus) ; EC 2.7.1.- (UL13 protein, Simplexvirus) ; EC 2.7.11.1 (Protein Serine-Threonine Kinases) ; EC 3.6.1.- (Adenosine Triphosphatases) ; EC 5.99.1.3 (DNA Topoisomerases, Type II) Entry Date(s): Date Created: 20080926 Date Completed: 20081125 Latest Revision: 20211203 Update Code: 20231215 PubMed Central ID: PMC2583647

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Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production.