Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection

Journal of Virology

Volumn 79, Issue 20, 2005, Pages 12840-12851

  Simpson Holley, Martha ^a   Colgrove, Robert C ^a   Nalepa, Grzegorz ^a   Harper, J Wade ^a   Knipe, David M ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; G ACTIN; GREEN FLUORESCENT PROTEIN; LAMIN A; PROTEIN CDC14B; PROTEIN UL31; PROTEIN UL34; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; CHROMATIN; CONTROLLED STUDY; CYTOARCHITECTURE; HERPES SIMPLEX; HERPES SIMPLEX VIRUS 1; HOST CELL; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; VIRUS REPLICATION;

ACTINS; ANIMALS; CELL LINE; CELL NUCLEUS; CHROMATIN; CYTOPLASM; HERPES SIMPLEX; HERPESVIRUS 1, HUMAN; HUMANS; NUCLEAR LAMINA; NUCLEAR PROTEINS; PROTEIN-TYROSINE-PHOSPHATASE; TIME FACTORS; VIRAL PROTEINS; VIRUS REPLICATION;

HUMAN HERPESVIRUS 1;

EID: 26444466028     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.20.12840-12851.2005     Document Type: Article

References (53)

1. Bettinger, B. T., D. M. Gilbert, and D. C. Amberg. 2004. Actin up in the nucleus. Nat. Rev. Mol. Cell Biol. 5:410-415.
2. Browne, H., S. Bell, T. Minson, and D. W. Wilson. 1996. An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: evidence for reenvelopment during egress. J. Virol. 70:4311-4316.
3. L31 gene of herpes simplex virus 1 is a nuclear phosphoprotein which partitions with the nuclear matrix. J. Virol. 67:6348-6356.
4. Couchman, J. R., D. A. Rees, M. R. Green, and C. G. Smith. 1982. Fibronectin has a dual role in locomotion and anchorage of primary chick fibroblasts and can promote entry into the division cycle. J. Cell Biol. 93:402-410.
5. Dreger, C. K., A. R. Konig, H. Spring, P. Lichter, and H. Herrmann. 2002. Investigation of nuclear architecture with a domain-presenting expression system. J. Struct. Biol. 140:100-115.
6. Farina, A., R. Feederle, S. Raffa, R. Gonnella, R. Santarelli, L. Frati, A. Angeloni, M. R. Torrisi, A. Faggioni, and H. J. Delecluse. 2005. BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress. J. Virol. 79:3703-3712.
7. Forest, T., S. Barnard, and J. D. Baines. 2005. Active intranuclear movement of herpesvirus capsids. Nat. Cell Biol. 7:429-431.
8. Fuchs, W., B. G. Klupp, H. Granzow, N. Osterrieder, and T. C. Mettenleiter. 2002. The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions. J. Virol. 76:364-378.
9. Gonnella, R., A. Farina, R. Santarelli, S. Raffa, R. Feederle, R. Bei, M. Granato, A. Modesti, L. Frati, H. J. Delecluse, M. R. Torrisi, A. Angeloni, and A. Faggioni. 2005. Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: interactions with BFRF1 and with the nuclear lamina. J. Virol. 79:3713-3727.
10. Gonsior, S. M., S. Platz, S. Buchmeier, U. Scheer, B. M. Jockusch, and H. Hinssen. 1999. Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J. Cell Sci. 112:797-809.
11. Granzow, H., B. G. Klupp, W. Fuchs, J. Veits, N. Osterrieder, and T. C. Mettenleiter. 2001. Egress of alphaherpesviruses: comparative ultrastructural study. J. Virol. 75:3675-3684.
12. Hill, D. A., S. Chiosea, S. Jamaluddin, K. Roy, A. H. Fischer, D. D. Boyd, J. A. Nickerson, and A. N. Imbalzano. 2004. Inducible changes in cell size and attachment area due to expression of a mutant SWI/SNF chromatin remodeling enzyme. J. Cell Sci. 117:5847-5854.
13. Holaska, J. M., A. K. Kowalski, and K. L. Wilson. 2004. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PLoS Biol. 2:E231.
14. Ingber, D. E. 1993. Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 104:613-627.
15. Ingber, D. E. 1990. Fibronectin controls capillary endothelial cell growth by modulating cell shape. Proc. Natl. Acad. Sci. USA 87:3579-3583.
16. Ingber, D. E. 2003. Tensegrity 1. Cell structure and hierarchical systems biology. J. Cell Sci. 116:1157-1173.
17. Ingber, D. E., J. A. Madri, and J. Folkman. 1987. Endothelial growth factors and extracellular matrix regulate DNA synthesis through modulation of cell and nuclear expansion. In Vitro Cell Dev. Biol. 23:387-394.
18. Izumi, M., O. A. Vaughan, C. J. Hutchison, and D. M. Gilbert. 2000. Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells. Mol. Biol. Cell 11:4323-4337.
19. Klupp, B. G., H. Granzow, and T. C. Mettenleiter. 2000. Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product. J. Virol. 74:10063-10073.
20. Knipe, D. M., D. Senechek, S. A. Rice, and J. L. Smith. 1987. Stages in the nuclear association of the herpes simplex virus transcriptional activator protein ICP4. J. Virol. 61:276-284.
21. Lake, C. M., and L. M. Hutt-Fletcher. 2004. The Epstein-Barr virus BFRF1 and BFLF2 proteins interact and coexpression alters their cellular localization. Virology 320:99-106.
22. Liang, L., and J. D. Baines. 2005. Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein. J. Virol. 79:3797-3806.
23. Martelli, A. M., E. Falcieri, M. Zweyer, R. Bortul, G. Tabellini, A. Cappellini, L. Cocco, and L. Manzoli. 2002. The controversial nuclear matrix: a balanced point of view. Histol. Histopathol. 17:1193-1205.
24. Monier, K., J. C. Armas, S. Etteldorf, P. Ghazal, and K. F. Sullivan. 2000. Annexation of the interchromosomal space during viral infection. Nat. Cell Biol. 2:661-665.
25. Muranyi, W., J. Haas, M. Wagner, G. Krohne, and U. H. Koszinowski. 2002. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 297:854-857.
26. Nalepa, G., and J. W. Harper. 2004. Visualization of a highly organized intranuclear network of filaments in living mammalian cells. Cell Motil. Cytoskelet. 59:94-108.
27. Nikolova, V., C. Leimena, A. C. McMahon, J. C. Tan, S. Chandar, D. Jogia, S. H. Kesteven, J. Michalicek, R. Otway, F. Verheyen, S. Rainer, C. L. Stewart, D. Martin, M. P. Feneley, and D. Fatkin. 2004. Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice. J. Clin. Investig. 113:357-369.
28. Olins, A. L., and D. E. Olins. 2004. Cytoskeletal influences on nuclear shape in granulocytic HL-60 cells. BMC Cell Biol. 5:30.
29. Pederson, T. 2000. Diffusional protein transport within the nucleus: a message in the medium. Nat. Cell Biol. 2:E73-E74.
30. Pederson, T. 2000. Half a century of "the nuclear matrix." Mol. Biol. Cell 11:799-805.
31. Pederson, T., and U. Aebi. 2002. Actin in the nucleus: what form and what for? J. Struct. Biol. 140:3-9.
32. Quinlan, M. P., L. B. Chen, and D. M. Knipe. 1984. The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication. Cell 36:857-868.
33. Rabut, G., V. Doye, and J. Ellenberg. 2004. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat. Cell Biol. 6:1114-1121.
34. L34. J. Virol. 78:5564-5575.
35. L34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J. Virol. 75:8803-8817.
36. S3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J. Virol. 76:8939-8952.
37. Roizman, B., and D. M. Knipe. 2001. Herpes simplex viruses and their replication, p. 2399-2460. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
38. L34 gene product is required for viral envelopment. J. Virol. 74:117-129.
39. Schwartz, J., and B. Roizman. 1969. Concerning the egress of herpes simplex virus from infected cells: electron and light microscope observations. Virology 38:42-49.
40. Scott, E. S., and P. O'Hare. 2001. Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection. J. Virol. 75:8818-8830.
41. L34 gene products promote the late maturation of viral replication compartments to the nuclear periphery. J. Virol. 78:5591-5600.
42. Sims, J. R., S. Karp, and D. E. Ingber. 1992. Altering the cellular mechanical force balance results in integrated changes in cell, cytoskeletal and nuclear shape. J. Cell Sci. 103:1215-1222.
43. Swanson, J. A., M. Lee, and P. E. Knapp. 1991. Cellular dimensions affecting the nucleocytoplasmic volume ratio. J. Cell Biol. 115:941-948.
44. Taylor, T. J., E. E. McNamee, C. Day, and D. M. Knipe. 2003. Herpes simplex virus replication compartments can form by coalescence of smaller compartments. Virology 309:232-247.
45. Uprichard, S. L., and D. M. Knipe. 1997. Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites. Virology 229:113-125.
46. Visintin, R., K. Craig, E. S. Hwang, S. Prinz, M. Tyers, and A. Amon. 1998. The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation. Mol. Cell 2:709-718.
47. Ward, P. L., W. O. Ogle, and B. Roizman. 1996. Assemblons: nuclear structures defined by aggregation of immature capsids and some tegument proteins of herpes simplex virus 1. J. Virol. 70:4623-4631.
48. Wasser, M., and W. Chia. 2000. The EAST protein of drosophila controls an expandable nuclear endoskeleton. Nat. Cell Biol. 2:268-275.
49. Whealy, M. E., A. K. Robbins, F. Tufaro, and L. W. Enquist. 1992. A cellular function is required for pseudorabies virus envelope glycoprotein processing and virus egress. J. Virol. 66:3803-3810.
50. Wild, P., M. Engels, C. Senn, K. Tobler, U. Ziegler, E. M. Schraner, E. Loepfe, M. Ackermann, M. Mueller, and P. Walther. 2005. Impairment of nuclear pores in bovine herpesvirus 1-infected MDBK cells. J. Virol. 79:1071-1083.
51. Yamauchi, Y., C. Shiba, F. Goshima, A. Nawa, T. Murata, and Y. Nishiyama. 2001. Herpes simplex virus type 2 UL34 protein requires UL31 protein for its relocation to the internal nuclear membrane in transfected cells. J. Gen. Virol. 82:1423-1428.
52. Yang, L., T. Guan, and L. Gerace. 1997. Lamin-binding fragment of LAP2 inhibits increase in nuclear volume during the cell cycle and progression into S phase. J. Cell Biol. 139:1077-1087.
53. Ye, G. J., and B. Roizman. 2000. The essential protein encoded by the UL31 gene of herpes simplex virus 1 depends for its stability on the presence of UL34 protein. Proc. Natl. Acad. Sci. USA 97:11002-11007.