Abstract
DNA-binding proteins present in varicella-zoster virus-infected cells were identified by DNA-cellulose chromatography of radioactively labeled cell extracts. Seven virus-specific proteins, ranging in molecular weight from approximately 175,000 to 21,000, showed affinity for single- or double-stranded DNA or both. These proteins include the varicella-zoster virus major capsid protein, a phosphorylated tegument protein, and a 125,000-molecular-weight species which may be analogous to the major DNA-binding protein of herpes simplex virus. We also identified a number of DNA-binding phosphoproteins by these procedures. Finally, protein blot studies were carried out to determine whether these proteins bind preferentially to virus rather than to host cell DNA.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bayliss G. J., Marsden H. S., Hay J. Herpes simplex virus proteins: DNA-binding proteins in infected cells and in the virus structure. Virology. 1975 Nov;68(1):124–134. doi: 10.1016/0042-6822(75)90154-3. [DOI] [PubMed] [Google Scholar]
- Ben-Porat T., Veach R. A., Hampl H. Functions of the major nonstructural DNA binding protein of a herpesvirus (pseudorabies). Virology. 1983 Jan 30;124(2):411–424. doi: 10.1016/0042-6822(83)90357-4. [DOI] [PubMed] [Google Scholar]
- Blair E. D., Honess R. W. DNA-binding proteins specified by herpesvirus saimiri. J Gen Virol. 1983 Dec;64(Pt 12):2697–2715. doi: 10.1099/0022-1317-64-12-2697. [DOI] [PubMed] [Google Scholar]
- Bowen B., Steinberg J., Laemmli U. K., Weintraub H. The detection of DNA-binding proteins by protein blotting. Nucleic Acids Res. 1980 Jan 11;8(1):1–20. doi: 10.1093/nar/8.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Braun D. K., Batterson W., Roizman B. Identification and genetic mapping of a herpes simplex virus capsid protein that binds DNA. J Virol. 1984 May;50(2):645–648. doi: 10.1128/jvi.50.2.645-648.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown S. M., Ritchie D. A., Subak-Sharpe J. H. Genetic studies with herpes simplex virus type 1. The isolation of temperature-sensitive mutants, their arrangement into complementation groups and recombination analysis leading to a linkage map. J Gen Virol. 1973 Mar;18(3):329–346. doi: 10.1099/0022-1317-18-3-329. [DOI] [PubMed] [Google Scholar]
- Dalziel R. G., Marsden H. S. Identification of two herpes simplex virus type 1-induced proteins (21K and 22K) which interact specifically with the a sequence of herpes simplex virus DNA. J Gen Virol. 1984 Sep;65(Pt 9):1467–1475. doi: 10.1099/0022-1317-65-9-1467. [DOI] [PubMed] [Google Scholar]
- Gibson W., Roizman B. Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels. J Virol. 1974 Jan;13(1):155–165. doi: 10.1128/jvi.13.1.155-165.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hay R. T., Hay J. Properties of herpesvirus-induced "immediate early" polypeptides. Virology. 1980 Jul 15;104(1):230–234. doi: 10.1016/0042-6822(80)90381-5. [DOI] [PubMed] [Google Scholar]
- 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 Sep;14(3):640–651. doi: 10.1128/jvi.14.3.640-651.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Honess R. W., Roizman B. Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. J Virol. 1974 Jul;14(1):8–19. doi: 10.1128/jvi.14.1.8-19.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Knopf K. W., Kaerner H. C. 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. 1980 Feb;46(2):405–414. doi: 10.1099/0022-1317-46-2-405. [DOI] [PubMed] [Google Scholar]
- Lee C. K., Knipe D. M. Thermolabile in vivo DNA-binding activity associated with a protein encoded by mutants of herpes simplex virus type 1. J Virol. 1983 Jun;46(3):909–919. doi: 10.1128/jvi.46.3.909-919.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Littler E., Purifoy D., Minson A., Powell K. L. Herpes simplex virus non-structural proteins. III. Function of the major DNA-binding protein. J Gen Virol. 1983 May;64(Pt 5):983–995. doi: 10.1099/0022-1317-64-5-983. [DOI] [PubMed] [Google Scholar]
- Littler E., Yeo J., Killington R. A., Purifoy D. J., Powell K. L. Antigenic and structural conservation of herpesvirus DNA-binding proteins. J Gen Virol. 1981 Oct;56(Pt 2):409–419. doi: 10.1099/0022-1317-56-2-409. [DOI] [PubMed] [Google Scholar]
- Marsden H. S., Crombie I. K., Subak-Sharpe J. H. Control of protein synthesis in herpesvirus-infected cells: analysis of the polypeptides induced by wild type and sixteen temperature-sensitive mutants of HSV strain 17. J Gen Virol. 1976 Jun;31(3):347–372. doi: 10.1099/0022-1317-31-3-347. [DOI] [PubMed] [Google Scholar]
- Powell K. L., Littler E., Purifoy D. J. Nonstructural proteins of herpes simplex virus. II. Major virus-specific DNa-binding protein. J Virol. 1981 Sep;39(3):894–902. doi: 10.1128/jvi.39.3.894-902.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Powell K. L., Purifoy D. J. DNA-binding proteins of cells infected by herpes simplex virus type 1 and type 2. Intervirology. 1976;7(4-5):225–239. doi: 10.1159/000149955. [DOI] [PubMed] [Google Scholar]
- Purifoy D. J., Powell K. L. DNA-binding proteins induced by herpes simplex virus type 2 in HEp-2 cells. J Virol. 1976 Aug;19(2):717–731. doi: 10.1128/jvi.19.2.717-731.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
- Ruyechan W. T. The major herpes simplex virus DNA-binding protein holds single-stranded DNA in an extended configuration. J Virol. 1983 May;46(2):661–666. doi: 10.1128/jvi.46.2.661-666.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spear P. G., Roizman B. Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J Virol. 1972 Jan;9(1):143–159. doi: 10.1128/jvi.9.1.143-159.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Straus S. E., Aulakh H. S., Ruyechan W. T., Hay J., Casey T. A., Vande Woude G. F., Owens J., Smith H. A. Structure of varicella-zoster virus DNA. J Virol. 1981 Nov;40(2):516–525. doi: 10.1128/jvi.40.2.516-525.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Timbury M. C. Temperature-sensitive mutants of herpes simplex virus type 2. J Gen Virol. 1971 Nov;13(2):373–376. doi: 10.1099/0022-1317-13-2-373. [DOI] [PubMed] [Google Scholar]
- Weller S. K., Lee K. J., Sabourin D. J., Schaffer P. A. Genetic analysis of temperature-sensitive mutants which define the gene for the major herpes simplex virus type 1 DNA-binding protein. J Virol. 1983 Jan;45(1):354–366. doi: 10.1128/jvi.45.1.354-366.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Yeo J., Killington R. A., Watson D. H., Powell K. L. Studies on cross-reactive antigens in the herpesviruses. Virology. 1981 Jan 30;108(2):256–266. doi: 10.1016/0042-6822(81)90434-7. [DOI] [PubMed] [Google Scholar]