Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection

Journal of Virology

Volumn 73, Issue 8, 1999, Pages 6769-6781

  Pomeranz, Lisa E ^a   Blaho, John A ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PHOSPHOPROTEIN;

ANIMAL CELL; ARTICLE; CELL LEVEL; CELLULAR DISTRIBUTION; DISEASE ACTIVITY; ELECTROPHORETIC MOBILITY; GENE TRANSLOCATION; HERPES SIMPLEX VIRUS 1; HERPES VIRUS INFECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS; VERO CELL; VIRION;

EID: 0032775897     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.8.6769-6781.1999     Document Type: Article

References (43)

1. Avitabile, E., S. Di Gaeta, M. R. Torrisi, P. L. Ward, B. Roizman, and G. Campadelli-Fiume. 1995. Redistribution of microtubules and Golgi apparatus in herpes simplex virus-infected cells and their role in viral exocytosis. J. Virol. 69:7472-7482.
2. Barker, D. E., and B. Roizman. 1990. Identification of three genes nonessential for growth in cell culture near the right terminus of the unique sequences of long component of herpes simplex virus 1. Virology 177:684-691.
3. Blaho, J. A., N. Michael, V. Kang, N. Aboul-Ela, M. E. Smulson, M. K. Jacobson, and B. Roizman. 1992. Differences in the poly(ADP-ribosyl)ation patterns of ICP4, the herpes simplex virus major regulatory protein, in infected cells and in isolated nuclei. J. Virol. 64:6398-6407.
4. Blaho, J. A., C. Mitchell, and B. Roizman. 1994. An amino acid sequence shared by the herpes simplex virus 1 alpha regulatory proteins 0, 4, 22, and 27 predicts the nucleotidylylation of the UL21, UL31, UL47, and UL49 gene products. J. Biol. Chem. 269:17401-17410.
5. Blaho, J. A., and B. Roizman. 1998. Analyses of HSV proteins for posttranslational modifications and enzyme functions, p. 237-256. In S. M. Brown and A. R. Maclean (ed.), Methods in molecular medicine: herpes simplex virus protocols, vol. 10. Humana Press Inc., Totowa, N.J.
6. Blaho, J. A., C. S. Zong, and K. A. Mortimer. 1997. Tyrosine phosphorylation of the herpes simplex virus type 1 regulatory protein ICP22 and a cellular protein which shares antigenic determinants with ICP22. J. Virol. 71:9828-9832.
7. Boehmer, P. E., and I. R. Lehman. 1997. Herpes simplex virus DNA replication. Annu. Rev. Biochem. 66:347-384.
8. Braun, D. K., B. Roizman, and L. Pereira. 1984. Characterization of post-translational products of herpes simplex virus gene 35 proteins binding to the surfaces of full capsids but not empty capsids. J. Virol. 49:142-153.
9. 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.
10. Burkham, J., D. M. Coen, and S. K. Weller. 1998. ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase. J. Virol. 72:10100-10100.
11. Campadelli, G., R. Brandimarti, C. Di Lazzaro, P. L. Ward, B. Roizman, and M. R. Torrisi. 1993. Fragmentation and dispersal of Golgi proteins and redistribution of glycnproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1. Proc. Natl. Acad. Sci. USA 90:2798-2802.
12. Chang, Y. E., and B. Roizman. 1993. The product of the UL31 gene of herpes simplex virus 1 is a nuclear phosphoprotein which partitions with the nuclear matrix. J. Virol. 67:6348-6356.
13. de Bruyn Kops, A., S. L. Uprichard, M. Chen, and D. M. Knipe. 1998. Comparison of the intranuclear distributions of herpes simplex virus proteins involved in various viral functions. Virology 252:162-178.
14. Ejercito, P. M., E. D. Kieff, and B. Roizman. 1968. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J. Gen. Virol. 2:357-64.
15. Elliott, G., G. Mouzakitis, and P. O'Hare. 1995. VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells. J. Virol. 69:7932-7941.
16. Elliott, G., and P. O'Hare. 1998. Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules, J. Virol. 72:6448-6455.
17. Elliott, G., and P. O'Hare. 1997. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88:223-233.
18. Elliott, G., D. O'Reilly, and P. O'Hare. 1996. Phosphorylation of the herpes simplex virus type 1 tegument protein VP22. Virology 226:140-145.
19. Elliott, G. D., and D. M. Meredith. 1992. The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49. J. Gen. Virol. 73:723-726.
20. Fang, B., B. Xu, P. Kock, and J. A. Roth. 1998. Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells. Gene Ther. 5:1420-1424.
21. Hall, L. M., K. G. Draper, R. J. Frink, R. H. Costa, and E. K. Wagner. 1982. Herpes simplex virus mRNA species mapping in EcoRI fragment I. J. Virol. 43:594-607.
22. Herold, B. C., D. WuDunn, N. Soltys, and P. G. Spear. 1991. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J. Virol. 65:1090-1098.
23. Honess, R. W., and B. Roizman. 1974. Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. J. Virol. 14:8-19.
24. Honess, R. W., and B. Roizman. 1975. Regulation of herpesvirus macromolecular synthesis: sequential transition of polypeptide synthesis requires functional viral polypeptides. Proc. Natl. Acad. Sci. USA 72:1276-1280.
25. 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.
26. Knopf, K. W., and H. C. Kaerner. 1980. Virus-specific basic phosphoproteins associated with herpes simplex virus type 1 (HSV-1) particles and the chromatin of HSV-1-infected cells. J. Gen. Virol. 46:405-414.
27. Liang, X., B. Chow, Y. Li, C. Raggo, D. Yoo, S. Attah-Poku, and L. A. Babiuk. 1995. Characterization of bovine herpesvirus 1 UL49 homolog gene and product: bovine herpesvirus 1 UL49 homolog is dispensable for virus growth. J. Virol. 69:3863-3867.
28. Liptak, L. M., S. L. Uprichard, and D. M. Knipe. 1996. Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures. J. Virol. 70:1759-1767.
29. Lukonis, C. J., J. Burkham, and S. K. Weller. 1997. Herpes simplex virus type 1 prereplicative sites are a heterogeneous population: only a subset are likely to be precursors to replication compartments. J. Virol. 71:4771-4781.
30. Morrison, E. E., A. J. Stevenson, Y. F. Wang, and D. M. Meredith. 1998 Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells. J. Gen. Virol. 79: 2517-2528.
31. Morrison, E. E., Y. F. Wang, and D. M. Meredith. 1998. Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. J. Virol. 72:7108-7114.
32. Newcomb, W. W., F. L. Homa, D. R. Thomsen, Z. Ye, and J. C. Brown. 1994. Cell-free assembly of the herpes simplex virus capsid. J. Virol. 68:6059-6063.
33. Pomeranz, L. E., and J. A. Blaho. 1999. Unpublished data.
34. Pomeranz, L. E., and J. A. Blaho. 9 February 1999, posting date. Electronic data. [Online.] http://www.mssm.edu/micro/blaho/lpdns/html. [19 May 1999, last date accessed.]
35. 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.
36. Roizman, B., and A. E. Sears. 1996. Herpes simplex viruses and their replication, p. 2231-2295. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
37. Spear, P. G., and B. Roizman. 1970. Proteins specified by herpes simplex virus. IV. Site of glycosylation and accumulation of viral membrane proteins. Proc. Natl. Acad. Sci. USA 66:730-737.
38. Spear, P. G., and B. Roizman. 1972. Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J. Virol. 9:143-159.
39. Trus, B. L., F. L. Homa, F. P. Booy, W. W. Newcomb, D. R. Thorasen, N. Cheng, J. C. Brown, and A. C. Steven. 1995. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26. J. Virol. 69:7362-7366.
40. Uprichard, S. L., and D. M. Knipe. 1997. Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites. Virology 229:113-125.
41. Ward, P. L., E. Avitabile, G. Campadelli-Fiume, and B. Roizman. 1998. Conservation of the architecture of the Golgi apparatus related to a differential organization of microtubules in polykaryocytes induced by syn-mutants of herpes simplex virus 1. Virology 241:189-199.
42. 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.
43. Zhong, L., and G. S. Hayward. 1997. Assembly of complete, functionally active herpes simplex virus DNA replication compartments and recruitment of associated viral and cellular proteins in transient cotransfection assays. J. Virol. 71:3146-3160.