Herpes simplex virus type 1 tegument protein VP22 is capable of modulating the transcription of viral TK and gC genes via interaction with viral ICP0

Biochimie

Volumn 92, Issue 8, 2010, Pages 1024-1030

  Yu, Xian ^a,b   Liu, Longding ^a   Wu, Lianqiu ^a   Wang, Lichun ^a   Dong, Chenghong ^a   Li, Weizhong ^a   Li, Qihan ^a  

^a INSTITUTE OF MEDICAL BIOLOGY   (China)

^b AFFILIATED HOSPITAL OF NORTH SICHUAN MEDICAL COLLEGE   (China)

Author keywords

HSV 1; ICP0; Viral transcription; VP22

Indexed keywords

CHLORAMPHENICOL ACETYLTRANSFERASE; INFECTED CELL POLYPEPTIDE 0; POLYPEPTIDE; PROTEIN VP22; UNCLASSIFIED DRUG;

ARTICLE; CELL NUCLEUS; CONTROLLED STUDY; GC GENE; HERPES SIMPLEX; HERPES SIMPLEX VIRUS 1; LATENT VIRUS INFECTION; NONHUMAN; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; TK GENE; TRANSCRIPTION REGULATION; VIRUS GENE; VIRUS TRANSCRIPTION;

ANIMALS; BASE SEQUENCE; CERCOPITHECUS AETHIOPS; CHLORAMPHENICOL O-ACETYLTRANSFERASE; DNA PRIMERS; GENES, VIRAL; IMMEDIATE-EARLY PROTEINS; MICROSCOPY, FLUORESCENCE; POLYMERASE CHAIN REACTION; THYMIDINE KINASE; TRANSCRIPTION, GENETIC; TWO-HYBRID SYSTEM TECHNIQUES; UBIQUITIN-PROTEIN LIGASES; VERO CELLS; VIRAL STRUCTURAL PROTEINS;

HUMAN HERPESVIRUS 1;

EID: 77954661207     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.04.025     Document Type: Article

References (28)

1. Kristie T.M., Sharp P.A. Interactions of the Oct-1 POU subdomains with specific DNA sequences and with the HSV alpha-trans-activator protein. Genes Dev. 1990, 4:2383-2396.
2. Baines J.D., Roizman B. The UL11 gene of herpes simplex virus 1 encodes a function that facilitates nucleocapsid envelopment and egress from cells. J. Virol. 1992, 66:5168-5174.
3. Sciortino M.T., Taddeo B., Poon A.P., Mastino A., Roizman B. Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection. Proc. Natl. Acad. Sci. U S A 2002, 99:8318-8323.
4. Elliott G., Hafezi W., Whiteley A., Bernard E. Deletion of the herpes simplex virus VP22-encoding gene (UL49) alters the expression, localization, and virion incorporation of ICP0. J. Virol. 2005, 79:9735-9745.
5. Ren X., Harms J.S., Splitter G.A. Bovine herpesvirus 1 tegument protein VP22 interacts with histones, and the carboxyl terminus of VP22 is required for nuclear localization. J. Virol. 2001, 75:8251-8258.
6. Heine J.W., Honess R.W., Cassai E., Roizman B. Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J. Virol. 1974, 14:640-651.
7. Sciortino M.T., Taddeo B., Giuffre-Cuculletto M., Medici M.A., Mastino A., Roizman B. Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase. J. Virol. 2007, 81:10924-10932.
8. Elliott G., Mouzakitis G., O'Hare P. 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. 1995, 69:7932-7941.
9. Chi J.H., Harley C.A., Mukhopadhyay A., Wilson D.W. The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids. J. Gen. Virol. 2005, 86:253-261.
10. Elliott G., O'Hare P. Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules. J. Virol. 1998, 72:6448-6455.
11. Cilloniz C., Jackson W., Grose C., Czechowski D., Hay J., Ruyechan W.T. The varicella-zoster virus (VZV) ORF9 protein interacts with the IE62 major VZV transactivator. J. Virol. 2007, 81:761-774.
12. Blaho J.A., Mitchell C., Roizman B. 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. 1994, 269:17401-17410.
13. Elliott G., O'Reilly D., O'Hare P. Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. J. Virol. 1999, 73:6203-6206.
14. Elliott G., O'Reilly D., O'Hare P. Phosphorylation of the herpes simplex virus type 1 tegument protein VP22. Virology 1996, 226:140-145.
15. Pomeranz L.E., Blaho J.A. Assembly of infectious Herpes simplex virus type 1 virions in the absence of full-length VP22. J. Virol. 2000, 74:10041-10054.
16. del Rio T., Werner H.C., Enquist L.W. 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. 2002, 76:774-782.
17. Duffy C., Mbong E.F., Baines J.D. VP22 of herpes simplex virus 1 promotes protein synthesis at late times in infection and accumulation of a subset of viral mRNAs at early times in infection. J. Virol. 2009, 83:1009-1017.
18. Leslie J., Rixon F.J., McLauchlan J. Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles. Virology 1996, 220:60-68.
19. Pomeranz L.E., Blaho Modified J.A. VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J. Virol. 1999, 73:6769-6781.
20. Hutchinson I., Whiteley A., Browne H., Elliott G. Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains. J. Virol. 2002, 76:10365-10373.
21. Yu X., Li W., Liu L., Che Y., Cun W., Wu W., He C., Shao C., Li Q. Functional analysis of transcriptional regulation of herpes simplex virus type 1 tegument protein VP22. Sci. China C Life Sci. 2008, 51:966-972.
22. Chen J., Silverstein S. Herpes simplex viruses with mutations in the gene encoding ICP0 are defective in gene expression. J. Virol. 1992, 66:2916-2927.
23. Elliott G., O'Hare P. Live-cell analysis of a green fluorescent protein-tagged herpes simplex virus infection. J. Virol. 1999, 73:4110-4119.
24. Mouzakitis G., McLauchlan J., Barreca C., Kueltzo L., O'Hare P. Characterization of VP22 in herpes simplex virus-infected cells. J. Virol. 2005, 79:12185-12198.
25. Martin A., O'Hare P., McLauchlan J., Elliott G. Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding. J. Virol. 2002, 76:4961-4970.
26. van Leeuwen H., Okuwaki M., Hong R., Chakravarti D., Nagata K., O'Hare P. Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT. J. Gen. Virol. 2003, 84:2501-2510.
27. O'Regan K.J., Bucks M.A., Murphy M.A., Wills J.W., Courtney R.J. A conserved region of the herpes simplex virus type 1 tegument protein VP22 facilitates interaction with the cytoplasmic tail of glycoprotein E (gE). Virology 2007, 358:192-200.
28. Everett R., O'Hare P., O'Rourke D., Barlow P., Orr A. Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures. J. Virol. 1995, 69:7339-7344.