Characterization of regulatory functions of the HSV-1 immediate-early protein ICP22

Virology

Volumn 226, Issue 2, 1996, Pages 393-402

  Prod'Hon, Catherine ^a   Machuca, Irma ^a,b   Berthomme, Herve ^a   Epstein, Alberto ^a   Jacquemont, Bernard ^a  

^a UNIVERSITÉ LYON 1   (France)

^b UNIVERSITÉ DE LYON   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

ARTICLE; GENE EXPRESSION; HERPES SIMPLEX VIRUS 1; IMMUNOBLOTTING; IMMUNOPRECIPITATION; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SYNTHESIS;

EID: 0030589686     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0667     Document Type: Article

References (50)

1. Ackerman, M., Sarmiento, M., and Roizman, B. (1985). Application of antibody to synthetic peptides for characterisation of the intact and truncated α22 protein specified by Herpes simplex virus 1 and the R325 α22-deletion mutant. J. Virol. 56, 207-215.
2. Allende, J. E., and Allende, C. C. (1995). Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation. FASEB J. 9, 313-323.
3. Baron, M., Reynes, J. P., Stassi, D., and Tiraby, G. (1992). A selectable bifunctional β-galactosidase phleomycin-resistance fusion protein as a potential marker for eukaryotic cells. Gene 114, 239-243.
4. Blaho, J. A., Mitchell, C., and Roizman, B. (1993). Guanylation and adenylylation of the α regulatory proteins of Herpes simplex virus require a viral β or γ function. J. Virol. 67, 3891-3900.
5. Cai, W., Astor, T. L., Liptak, L. M., Cho, C., Coen, D. M., and Schaffer, P. A. (1993). The herpes simplex virus type1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency. J. Virol. 67, 7501-7512.
6. Carter, K. L., and Roizman, B. (1996). The promoter and transcriptional unit of a novel herpes simplex virus 1 α gene are contained in, and encode a protein in frame with, the open reading frame of the α22 gene. J. Virol. 70, 172-178.
7. Coulter, L. J., Moss, H. W. M., Lang, J., and McGeoch, D. J. (1993). A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted. J. Gen. Virol. 74, 387-395.
8. Cunningham, C., Davidson, A. J., Dolan, A., Frame, M. C., McGeoch, D. J., Meredith, D. M., Moss, H. W., and Orr, A. C. (1992). The UL13 virion protein of herpes simplex virus type1 is phosphorylated by a novel virus-induced protein kinase J. Gen. Virol. 73, 303-311.
9. Debrus, S., Sadzot-Delvaux, C., Nikkels, A. F., Piette, J., and Rentier, B. (1995). Varicella-Zoster virus gene 63 encodes an immediate-early protein that is abundantly expressed during latency. J. Virol. 69, 3240-3245.
10. Deluca, N. A., McCarthy, A. M., and Schaffer, P. A. (1985). Isolation and characterization of deletion mutants of Herpes simplex virus type1 in the gene encoding immediate-early regulatory protein ICP4. J. Virol. 56, 558-570.
11. Eustice, D. C., Feldman, P. A., Colberg-Poley, A. M., Buckery, R. M., and Neubauer, R. H. (1991). A sensitive method for the detection of β-galactosidase in transfected mammalian cells. Biotechniques. 11, 739-742.
12. Foecking, M. K., and Hofstetter, H. (1986). Powerful and versatile enhancer-promoter unit for mammalian expression vectors. Gene 45, 101-105.
13. Garcin, D., Masse, T., Madjar, J. J., and Jacquemont, B. (1990). Herpes simplex type-1 immediate-early expression and shu-off of host protein synthesis are inhibited in neomycin pre-treated HEp-2 cells. Eur. J. Biochem. 194, 279-286.
14. Gamier, J., Osguthorpe, D. J., and Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
15. Gelman, I. H., and Silverstein, S. (1987). Herpes simplex virus immediate-early promoters are responsive to virus and cell trans-acting factors. J. Virol. 61, 2286-2296.
16. German, C. M., Moffat, L. F., and Howard, B. H. (1982). Recombinants genomes which express chloramphenicol acetyl-transferase in mammalin cells. Mol. Cell. Biol. 2, 1044-1051.
17. Graham, F. L., and Van Der Eb, A. J. (1973). A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52, 456-467.
18. Greco, A., Simonin, D., Diaz, J. J., Barjhoux, L., Kindbeiter, K., Madjar, J. J., and Masse, T. (1994). The DNA sequence coding for the 5′ untranslated region of herpes simplex virus type 1 ICP22 mRNA mediates a high level of gene expression. J. Gen. Virol. 75, 1693-1702.
19. Heine, M. D., Honess, R. W., Cassai, E., and Roizman, B. (1974). Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J. Virol. 14, 640-651.
20. Heineman, T. C., and Cohen, J. I. (1995). The varicella-Zoster virus (VZV) open reading frame 47 (ORF47) protein kinase is dispensable for viral replication and is not required for phosphorylation of ORF 63 protein, the VZV homolog of Herpes Simplex virus ICP22. J. Virol. 69, 7367-7370.
21. Holden, V. R., Yalamanchili, R. R., Harty, R. N., and O'Callaghan, D. J. (1992). ICP22 homolog of equine herpesvirus 1: Expression from early and late promoters. J. Virol. 66, 664-673.
22. Holden, V. G., Thompson, Y., Caughman, G. B., Smith, R. H., and O'Callaghan, D. J. (1995). Characterization of the regulatory function of the ICP22 protein of equine herpesvirus type1. Virology 210, 273-282.
23. Jackers, P., Defechereux, P., Baudoux, L., Lambert, C., Massaer, M., Merville-Louis, M. P., Rentier, B., and Piette, J. (1992). Characterization of regulatory functions of the Varicella-Zoster virus gene 63 encoded protein. J. Virol. 66, 3899-3903.
24. Jesse Chan, K. F., Hurst, M. O., and Graves, D. J. (1982). Phosphorylase kinase specificity. A comparative study with cAMP-dependent protein kinase on synthetic peptides and peptide analogs of glycogen synthetase and phosphatase. J. Biol. Chem. 257, 3655-3659.
25. Kost, R. G., Kupinsky, H., and Straus, S. E. (1995). Varicella-Zoster virus gene 63: transcript mapping and regulatory activity. Virology 209, 218-224.
26. Lemaster, S., and Roizman, B. (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.
27. Mackem, S., and Roizman, (1982). Structural features of the Herpes simplex virus α gene 4, 0, and 27 promoter-regulatory sequences which confer α regulation on chimeric thymidine kinase genes. J. Virol. 44, 939-949.
28. Meisner, H., and Czech, M. P. (1991). Phosphorylation of transcriptional factors and cell-cycle-dependent proteins by casein kinase II. Curr. Opin. Cell Biol. 3, 474-483.
29. Miller, J., and Germain, R. N. (1986). Efficient cell surface expression of class II MHC molecules in the absence of associated invariant chain. J. Exp. Med. 164, 1478-1489.
30. Mitchell, C., Blaho, J. A., and Roizman, B. (1994). Casein kinase II specifically nucleotidylylates in vitro the amino acid sequence of the protein encoded by the α22 gene of herpes simplex virus 1. Proc. Natl. Acad. Sci. USA 91, 11864-11868.
31. Ng, T. I., Keenan, L., Kinchington, P. R., and Grose, C. (1994). Phosphorylation of varicella-Zoster virus open reading frame (ORF) 62 regulatory product by viral ORF47-associated protein kinase. J. Virol. 68, 1350-1359.
32. O'Hare, P., and Hayward, G. S. (1985). Evidence for a direct role for both the 175,000 and 110,000 molecular weight immediate early proteins of herpes simplex virus in the transcription of delayed-early promoters. J. Virol. 53, 751-760.
33. Overton, H. A., McMillan, D. J., Klavinskis, L. S., Hpe, L., Ritche, A. J., and Wong-Kai-In, P., (1992). Herpes simplex virus type1 gene UL13 encodes a phosphoprotein that is a component of the virion. Virology 190, 184-192.
34. Perry, L. J., and McGeoch, D. J. (1988). The DNA sequences of the long repeat region and adjoining parts of the long unique region in the genome of herpes simplex virus type 1. J. Gen. Virol. 69, 2831-2846.
35. Piette, J., Kryszke, M., and Yaniv, M. (1985). Specific interaction of cellular factors with the B enhancer of polyoma virus. EMBO J. 4, 2675-2685.
36. Pinna, L. A. (1990). Casein kinase 2: An eminence grise in cellular regulation. Biochem. Biophys. Acta 1054, 267-284.
37. Poffenberger, K. L., Raichlen, P. E., and Herman, R. C. (1993). In vitro characterization of a herpes simplex virus type 1 ICP22 deletion mutant. Virus Gene 7, 171-186.
38. Purves, F. C., and Roizman, B. (1992). The UL13 gene of herpes simplex virus 1 encodes the functions for posttranslational processing associated with phosphorylation of the regulatory protein α22. Proc. Natl. Acad. Sci. USA 89, 7310-7314.
39. Purves, F. C., Ogle, W. O., and Roizman, B. (1993). Processing of the herpes simplex virus regulatory protein α22 mediated by the UL13 protein kinase determines the accumulation of a subset of α and γ mRNAs and proteins in infected cells. Proc. Natl. Acad. Sci. USA 90, 6701-6705.
40. Rice, S. A., Long, M. C., Lam, V., and Spencer, C. A. (1994). RNA polymerase II is aberrantly phosphorylated and located to viral replication compartments following herpes simplex virus infection. J. Virol. 68, 988-1001.
41. Rice, S. A., Long, M. C., Lam, V., Schaffer, P. A., and Spencer, C. A. (1995). Herpes simplex virus immediate-early protein ICP22 is required for viral modification of host RNA polymerase II and establishment of the normal viral transcription program. J. Virol. 69, 5550-5559.
42. Roizman, B., and Sears, A. E. (1991). Herpes simplex viruses and their replication. In "Virology" (B. N. Fields and D. M. Knipe, Eds.), pp. 1795-1842. Raven Press, New York.
43. Schwyzer, M., Wirth, U. V., Vogt, B., and Fraefel, C. (1994). BICP22 of bovine herpesvirus 1 is encoded by a spliced 1.7kb RNA which exhibits immediate early and late transcription kinetics. J. Gen. Virol. 75, 1703-1711.
44. Sears, A. E., Halliburton, I. W., Meignier, B., Silver, S., and Roizman, B. (1985). Herpes simplex virus1 mutant deleted in the α22 gene: Growth and expression in permissive and restrictive cells and establishment of latency in mice. J. Virol. 55, 338-346.
45. Sekulovich, R. E., Leary, K., and Sandri-Goldin, R. M. (1988). The herpes simplex type 1 α protein ICP27 can act as a trans-repressor or a trans-activator in combination with ICP4 and ICPO. J. Virol. 62, 4510-4522.
46. Stevenson, D., Xue, M., Hay, J., and Ruyechan, W. T. (1996). Phosphorylation and nuclear localization of the varicella-zoster virus gene 63 protein. J. Virol. 70, 658-662.
47. Walboomers, J. M., and Ter Scheggett, J. (1976). A new method for the isolation of herpes simplex virus type 2 DNA. Virology 74, 256-258.
48. Watson, R. J., and Clements, J. B. (1980). A herpes simplex virus type1 function continuously required for early and late virus RNA synthesis. Nature 285, 329-331.
49. Wilcox, K. W., Kohn, A., Sklyanskaya, E., and Roizman, B. (1980). Herpes simplex virus phosphoproteins. I Phosphate cycles on and off some viral polypeptides and can alter their affinity for DNA. J. Virol. 33, 167-182.
50. Zhang, G., and Leader, D. P. (1990). The structure of the pseudorabies virus genome at the end of the inverted repeat sequences proximal to the junction with the short unique region. J. Gen. Virol. 71, 2433-2441.