Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1997 Dec;71(12):9828–9832. doi: 10.1128/jvi.71.12.9828-9832.1997

Tyrosine phosphorylation of the herpes simplex virus type 1 regulatory protein ICP22 and a cellular protein which shares antigenic determinants with ICP22.

J A Blaho 1, C S Zong 1, K A Mortimer 1
PMCID: PMC230299  PMID: 9371655

Abstract

At least eight herpes simplex virus type 1 (HSV-1) and five HSV-2 proteins were tyrosine phosphorylated in infected cells. The first viral tyrosine phosphoprotein identified was the HSV-1 regulatory protein ICP22. Also, two novel phosphotyrosine proteins were bound by anti-ICP22 antibodies. H(R22) is a cellular protein, while the F(R10) protein is observed only in HSV-1-infected cells.

Full Text

The Full Text of this article is available as a PDF (860.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ackermann M., Sarmiento M., Roizman B. Application of antibody to synthetic peptides for characterization of the intact and truncated alpha 22 protein specified by herpes simplex virus 1 and the R325 alpha 22- deletion mutant. J Virol. 1985 Oct;56(1):207–215. doi: 10.1128/jvi.56.1.207-215.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blaho J. A., Mitchell C., Roizman B. Guanylylation and adenylylation of the alpha regulatory proteins of herpes simplex virus require a viral beta or gamma function. J Virol. 1993 Jul;67(7):3891–3900. doi: 10.1128/jvi.67.7.3891-3900.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Carter K. L., Roizman B. The promoter and transcriptional unit of a novel herpes simplex virus 1 alpha gene are contained in, and encode a protein in frame with, the open reading frame of the alpha 22 gene. J Virol. 1996 Jan;70(1):172–178. doi: 10.1128/jvi.70.1.172-178.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ejercito P. M., Kieff E. D., Roizman B. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J Gen Virol. 1968 May;2(3):357–364. doi: 10.1099/0022-1317-2-3-357. [DOI] [PubMed] [Google Scholar]
  5. Erpel T., Courtneidge S. A. Src family protein tyrosine kinases and cellular signal transduction pathways. Curr Opin Cell Biol. 1995 Apr;7(2):176–182. doi: 10.1016/0955-0674(95)80025-5. [DOI] [PubMed] [Google Scholar]
  6. Leopardi R., Ward P. L., Ogle W. O., Roizman B. Association of herpes simplex virus regulatory protein ICP22 with transcriptional complexes containing EAP, ICP4, RNA polymerase II, and viral DNA requires posttranslational modification by the U(L)13 proteinkinase. J Virol. 1997 Feb;71(2):1133–1139. doi: 10.1128/jvi.71.2.1133-1139.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. McGeoch D. J., Dalrymple M. A., Davison A. J., Dolan A., Frame M. C., McNab D., Perry L. J., Scott J. E., Taylor P. The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69(Pt 7):1531–1574. doi: 10.1099/0022-1317-69-7-1531. [DOI] [PubMed] [Google Scholar]
  8. McGeoch D. J., Dolan A., Donald S., Rixon F. J. Sequence determination and genetic content of the short unique region in the genome of herpes simplex virus type 1. J Mol Biol. 1985 Jan 5;181(1):1–13. doi: 10.1016/0022-2836(85)90320-1. [DOI] [PubMed] [Google Scholar]
  9. Mitchell C., Blaho J. A., Roizman B. Casein kinase II specifically nucleotidylylates in vitro the amino acid sequence of the protein encoded by the alpha 22 gene of herpes simplex virus 1. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11864–11868. doi: 10.1073/pnas.91.25.11864. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Poffenberger K. L., Idowu A. D., Fraser-Smith E. B., Raichlen P. E., Herman R. C. A herpes simplex virus type 1 ICP22 deletion mutant is altered for virulence and latency in vivo. Arch Virol. 1994;139(1-2):111–119. doi: 10.1007/BF01309458. [DOI] [PubMed] [Google Scholar]
  11. Poffenberger K. L., Raichlen P. E., Herman R. C. In vitro characterization of a herpes simplex virus type 1 ICP22 deletion mutant. Virus Genes. 1993 Jun;7(2):171–186. doi: 10.1007/BF01702397. [DOI] [PubMed] [Google Scholar]
  12. Post L. E., Roizman B. A generalized technique for deletion of specific genes in large genomes: alpha gene 22 of herpes simplex virus 1 is not essential for growth. Cell. 1981 Jul;25(1):227–232. doi: 10.1016/0092-8674(81)90247-6. [DOI] [PubMed] [Google Scholar]
  13. Prod'hon C., Machuca I., Berthomme H., Epstein A., Jacquemont B. Characterization of regulatory functions of the HSV-1 immediate-early protein ICP22. Virology. 1996 Dec 15;226(2):393–402. doi: 10.1006/viro.1996.0667. [DOI] [PubMed] [Google Scholar]
  14. Purves F. C., Roizman B. The UL13 gene of herpes simplex virus 1 encodes the functions for posttranslational processing associated with phosphorylation of the regulatory protein alpha 22. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7310–7314. doi: 10.1073/pnas.89.16.7310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rice S. A., Long M. C., Lam V., Spencer C. A. RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection. J Virol. 1994 Feb;68(2):988–1001. doi: 10.1128/jvi.68.2.988-1001.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sears A. E., Halliburton I. W., Meignier B., Silver S., Roizman B. Herpes simplex virus 1 mutant deleted in the alpha 22 gene: growth and gene expression in permissive and restrictive cells and establishment of latency in mice. J Virol. 1985 Aug;55(2):338–346. doi: 10.1128/jvi.55.2.338-346.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol. 1986 May 5;189(1):113–130. doi: 10.1016/0022-2836(86)90385-2. [DOI] [PubMed] [Google Scholar]
  18. Wilcox K. W., Kohn A., Sklyanskaya E., Roizman B. Herpes simplex virus phosphoproteins. I. Phosphate cycles on and off some viral polypeptides and can alter their affinity for DNA. J Virol. 1980 Jan;33(1):167–182. doi: 10.1128/jvi.33.1.167-182.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES