Phosphorylation of the herpes simplex virus tegument protein VP22 has no effect on incorporation of VP22 into the virus but is involved in optimal expression and virion packaging of ICP0

Journal of Virology

Volumn 79, Issue 22, 2005, Pages 14057-14068

  Potel, Corinne ^a   Elliott, Gillian ^a  

^a MARIE CURIE RESEARCH INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; GREEN FLUORESCENT PROTEIN; INFECTED CELL PROTEIN 0; PROTEIN VP16; PROTEIN VP22; SERINE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS PROTEIN ICP0;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; EPITHELIUM CELL; HERPES SIMPLEX VIRUS 1; IMMUNOFLUORESCENCE; MICROTUBULE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; VIRION; VIRUS INFECTION; VIRUS PARTICLE; VIRUS RECOMBINANT; VIRUS REPLICATION; WESTERN BLOTTING;

ANIMALS; CERCOPITHECUS AETHIOPS; CRICETINAE; GENE DELETION; GENE EXPRESSION REGULATION, VIRAL; IMMEDIATE-EARLY PROTEINS; PHOSPHORYLATION; SIMPLEXVIRUS; UBIQUITIN-PROTEIN LIGASES; VARIATION (GENETICS); VERO CELLS; VIRAL STRUCTURAL PROTEINS; VIRUS REPLICATION;

ANIMALIA; HUMAN HERPESVIRUS 1; SIMPLEXVIRUS;

EID: 27644540535     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.22.14057-14068.2005     Document Type: Article

References (36)

1. Banham, A. H., and G. L. Smith. 1992. Vaccinia virus gene B1R encodes a 34-kDa serine/threonine protein kinase that localizes in cytoplasmic factories and is packaged into virions. Virology 191:803-812.
2. Cambiazo, V., E. Logarinho, H. Pottstock, and C. E. Sunkel. 2000. Microtubule binding of the drosophila DMAP-85 protein is regulated by phosphorylation in vitro. FEBS Lett. 483:37-42.
3. Chi, J. H., C. A. Harley, A. Mukhopadhyay, and D. W. Wilson. 2005. The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids. J. Gen. Virol. 86:253-261.
4. 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.
5. 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.
6. Dargin, D. 1986. The structure and assembly of herpes viruses, p. 359-437. In J. R. Harris and R. W. Horne (ed.), Electron microscopy of proteins, vol. 5. Viral structure. Academic Press, London, United Kingdom.
7. Ebneth, A., G. Drewes, E. M. Mandelkow, and E. Mandelkow. 1999. Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells. Cell Motil. Cytoskeleton 44:209-224.
8. Elliott, G., W. Hafezi, A. Whiteley, and E. Bernard. 2005. Deletion of the herpes simplex virus VP22-encoding gene (UL49) alters the expression, localization, and virion incorporation of ICP0. J. Virol. 79:9735-9745.
9. 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.
10. Elliott, G., and P. O'Hare. 2000. Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division. J. Virol. 74:2131-2141.
11. 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.
12. Elliott, G., and P. O'Hare. 1997. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88:223-233.
13. 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.
14. 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.
15. 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.
16. 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.
17. Geiss, B. J., G. L. Cano, J. E. Tavis, and L. A. Morrison. 2004. Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization. Virology 330:74-81.
18. 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.
19. Granzow, H., B. G. Klupp, and T. C. Mettenleiter. 2004. The pseudorabies virus US3 protein is a component of primary and of mature virions. J. Virol. 78:1314-1323.
20. Hui, E. K. 2002. Virion-associated protein kinases. Cell Mol. Life Sci. 59:920-931.
21. 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.
22. Jacque, J. M., A. Mann, H. Enslen, N. Sharova, B. Brichacek, R. J. Davis, and M. Stevenson. 1998. Modulation of HIV-1 infectivity by MAPK, a virion-associated kinase. EMBO J. 17:2607-2618.
23. Johnson, G. V., and W. H. Stoothoff. 2004. Tau phosphorylation in neuronal cell function and dysfunction. J. Cell Sci. 117:5721-5729.
24. Kawaguchi, Y., and K. Kato. 2003. Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2. Rev. Med. Virol. 13:331-340.
25. Knopf, K. W., and H. C. Kaerner. 1980. Virus-specific basic phosphoproteins associated with herpes simplex virus type a (HSV-1) particles and the chromatin of HSV-1-infected cells. J. Gen. Virol. 46:405-414.
26. Leader, D. P. 1993. Viral protein kinases and protein phosphatases. Pharmacol. Ther. 59:343-389.
27. Leader, D. P., and M. Katan. 1988. Viral aspects of protein phosphorylation. J. Gen. Virol. 69:1441-1464.
28. Lemaster, S., and B. Roizman. 1980. Herpes simplex virus phosphoproteins. II. Characterization of the virion protein kinase and of the polypeptides phosphorylated in the virion. J. Virol. 35:798-811.
29. Lenard, J. 1999. Host cell protein kinases in nonsegmented negative-strand virus (mononegavirales) infection. Pharmacol. Ther. 83:39-48.
30. Mettenleiter, T. C. 2002. Herpesvirus assembly and egress. J. Virol. 76:1537-1547.
31. Michel, D., and T. Mertens. 2004. The UL97 protein kinase of human cytomegalovirus and homologues in other herpesviruses: impact on virus and host. Biochim. Biophys. Acta 1697:169-180.
32. 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.
33. 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.
34. Ren, X., J. S. Harms, and G. A. Splitter. 2001. Tyrosine phosphorylation of bovine herpesvirus 1 tegument protein VP22 correlates with the incorporation of VP22 into virions. J. Virol. 75:9010-9017.
35. Roizman, B., and D. Furlong. 1974. The replication of herpesviruses, p. 229-403. In H. Fraenkel-Conrat and R. R. Wagner (ed.), Comprehensive virology, vol. 3. Plenum Press, New York, N. Y.
36. Zhang, G., R. Stevens, and D. P. Leader. 1990. The protein kinase encoded in the short unique region of pseudorabies virus: description of the gene and identification of its product in virions and in infected cells. J. Gen. Virol. 71:1757-1765.