Characterization of VP22 in herpes simplex virus-infected cells

Journal of Virology

Volumn 79, Issue 19, 2005, Pages 12185-12198

  Mouzakitis, G ^a,c   McLauchlan, John ^b   Barreca, Cristina ^a   Kueltzo, Lisa ^a,d   O'Hare, P ^a  

^a MARIE CURIE RESEARCH INSTITUTE   (United Kingdom)

^b INSTITUTE OF VIROLOGY   (United Kingdom)

^c UNIVERSITY COLLEGE CORK   (Ireland)

^d UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GLYCEROL; PHOSPHOTRANSFERASE; PROTEIN VP16; PROTEIN VP22; TETRAMER; UNCLASSIFIED DRUG; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHROMATOGRAPHY; CONTROLLED STUDY; CROSS LINKING; DNA REPLICATION; ENZYME ACTIVITY; GEL FILTRATION; GENE DELETION; HERPES SIMPLEX VIRUS; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VITRO STUDY; ISOTOPE LABELING; MOLECULAR SIZE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SEDIMENTATION; VIRUS CELL INTERACTION; VIRUS PARTICLE;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; DIMERIZATION; DNA REPLICATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; EPITHELIAL CELLS; HELA CELLS; HERPES SIMPLEX VIRUS PROTEIN VMW65; HERPESVIRUS 1, HUMAN; HUMANS; IMMUNOPRECIPITATION; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN KINASES; VIRAL STRUCTURAL PROTEINS;

SIMPLEXVIRUS;

EID: 25144508144     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.19.12185-12198.2005     Document Type: Article

References (36)

1. 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.
2. Blouin, A., and J. A. Blaho. 2001. Assessment of the subcellular localization of the herpes simplex virus structural protein VP22 in the absence of other viral gene products. Virus Res. 81:57-68.
3. Brignati, M. J., J. S. Loomis, J. W. Wills, and R. J. Courtney. 2003. Membrane association of VP22, a herpes simplex virus type 1 tegument protein. J. Virol. 77:4888-4898.
4. Chi, J. H., C. A. Harley, A. Mukhopadhyay, and D. W. Wilson. 2005. The cytoplasmic tail of herpes simplex virus envelope gD binds to the tegument protein VP22 and to capsids. J. Gen. Virol. 86:253-261.
5. Coulter, L. J., H. W. Moss, J. Lang, and D. J. McGeoch. 1993. A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted. J. Gen. Virol. 74:387-395.
6. Cunningham, C., A. J. Davison, A. Dolan, M. C. Frame, D. J. McGeoch, D. M. Meredith, H. W. Moss, and A. C. Orr. 1992. The UL13 virion protein of herpes simplex virus type 1 is phosphorylated by a novel virus-induced protein kinase. J. Gen. Virol. 73:303-311.
7. Dargan, D. 1986. The structure and assembly of herpesviruses, p. 359-437. In J. R. Harris and W, Horne (ed.), Electron microscopy of proteins, vol. 5:VIral structure. Academic Press, New York, N.Y.
8. del Rio, T., H. C. Werner, and L. W. Enquist. 2002. The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents. J. Virol. 76:774-782.
9. del Rio, T., H. C. Werner, and L. W. Enquist. 2002. The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents. J. Virol. 76:774-782.
10. Dorange, F., B. K. Tischer, J. F. Vautherot, and N. Osterrieder. 2002. Characterization of Marek's disease virus serotype 1 (MDV-1) deletion mutants that lack UL46 to UL49 genes: MDV-1 UL49, encoding VP22, is indispensable for virus growth. J. Virol. 76:1959-1970.
11. Elliott, G., W. Hafezi, A. Whitely, and E. Bernard. 2005. Deletion of the herpes simplex virus VP22-endocing gene (UL49) alters the expression, localization, and virion incorporation of ICP0. J. Virol. 79:9735-9745.
12. 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.
13. Elliott, G., and P. O'Hare. 2000. Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division. J. Virol. 74:2131-2141.
14. 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.
15. Elliott, G., and P. O'Hare. 1999. Live-cell analysis of a green fluorescent protein-tagged herpes simplex virus infection. J. Virol. 73:4110-4119.
16. Elliott, G., D. O'Reilly, and P. O'Hare. 1999. Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. J. Virol. 73:6203-6206.
17. 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.
18. 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.
19. Fuchs, W., B. G. Klupp, H. Granzow, C. Hengartner, A. Brack, A. Mundt, L. W. Enquist, and T. C. Mettenleiter. 2002. Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49. J. Virol. 76:8208-8217.
20. Geiss, B. J., J. E. Tavis, L. M. Metzger, D. A. Leib, and L. A. Morrison. 2001. Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation. J. Virol, 75:10721-10729.
21. Heine, J. W., R. W. Honess, E. Cassai, and B. Roizman. 1974. Proteins specified by herpes simplex virus XII. The virion polypeptides of Type 1 strains. J. Virol. 14:640-651.
22. Hutchinson, I., A. Whiteley, H. Browne, and G. Elliott. 2002. Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains. J. Virol. 76:10365-10373.
23. Kotsakis, A., L. E. Pomeranz, A. Blouin, and J. A. Blaho. 2001. Microtubule reorganization during herpes simplex virus type 1 infection facilitates the nuclear localization of VP22, a major virion tegument protein. J. Virol. 75:8697-8711.
24. Leslie, J., F. J. Rixon. and J. McLauchlan. 1996. Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles. Virology 220:60-68.
25. Liand, X., B. Chow, Y. Li, C. Raggo, D. Yoo, S. Attah-Poku, and L. Babiuk. 1995. Characterization of bovine herpesvirus 1 UL49 homolog gene and product: bovine herpesvirus 1 UL9 homolog is dispensable for virus growth. J. Virol. 69:3863-3867.
26. Martin, A., P. O'Hare, J. McLauchlan, and G. Elliott. 2002. Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding. J. Virol. 76: 4961-4970.
27. Mettenleiter, T. 2002. Herpesvirus assembly and egress. J. Virol. 76:1537-1547.
28. Miranda-Saksena, M., R. A. Boadle, P. Armati, and A. L. Cunningham. 2002. In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell body. J. Virol. 76:9934-9951.
29. 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.
30. 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.
31. Normand, N., H. van Leeuwen, and P. O'Hare. 2001. Particle formation by a conserved domain of the herpes simplex virus protein VP22 facilitating protein and nucleic acid delivery. J. Biol. Chem. 276:15042-15050.
32. Overton, H. A, D. J. McMillan, L. S. Klavinskis, L. Hope, A. J. Ritchie, and P. Wong-kai-in. 1992. Herpes simplex virus type 1 gene UL13 encodes a phosphoprotein that is a component of the virion. Virology 190:184-192.
33. Pomeranz, L. E., and J. A. Blaho. 2000. Assembly of infectious herpes simplex virus type 1 virions in the absence of full-length VP22. J. Virol. 74:10041-10054.
34. Pomeranz, L. E., and J. A. Blaho. 1999. Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J. Virol. 73:6769-6781.
35. van Leeuwen, H., G. Elliott, and P. O'Hare. 2002. Evidence of a role for nonmuscle myosin II in herpes simplex virus type 1 egress. J. Virol. 76:3471-3481.
36. Wu, C. 1984. Two protein-binding sites in chromatin implicated in the activation of heat-shock genes. Nature (London) 309:229-234.