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. 1992 Mar;66(3):1402–1408. doi: 10.1128/jvi.66.3.1402-1408.1992

Recombinant fowlpox viruses expressing the glycoprotein B homolog and the pp38 gene of Marek's disease virus.

N Yanagida 1, R Ogawa 1, Y Li 1, L F Lee 1, K Nazerian 1
PMCID: PMC240863  PMID: 1310754

Abstract

Two Marek's disease virus (MDV) genes, one homologous to the glycoprotein B gene of herpes simplex virus and encoding the B antigen complex and the other encoding a 38-kDa phosphorylated protein (pp38), were inserted into the fowlpox virus (FPV) genome under the control of poxvirus promoters. Randomly selected nonessential regions of FPV were used for insertion, and the vaccinia virus 7.5 kDa polypeptide gene promoter or a poxvirus synthetic promoter was used for expression of MDV genes. Gene expression in cells infected with these recombinants was highly influenced by the promoter (the synthetic promoter being more effective) but was only slightly influenced by the insertion site and by the transcription direction of the insert relative to the direction of the flanking FPV sequences. Cells infected with an FPV recombinant expressing the MDV gB gene reacted positively with a monoclonal antibody specific to this glycoprotein in an immunofluorescence assay. Immunoprecipitation of infected cell lysates showed three glycoproteins identical to those associated with the B antigen complex of MDV (100, 60, and 49 kDa). Cells infected with a recombinant expressing the pp38 gene reacted positively with an anti-pp38 monoclonal antibody in an immunofluorescence assay. The generated protein was phosphorylated and had a molecular weight similar to that of the native pp38 protein. Sera from chickens immunized with an FPV recombinant expressing the MDV glycoprotein B gene reacted with MDV-infected cells.

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Selected References

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

  1. Binns M. M., Boursnell M. E., Tomley F. M., Campbell J. Analysis of the fowlpoxvirus gene encoding the 4b core polypeptide and demonstration that it possesses efficient promoter sequences. Virology. 1989 May;170(1):288–291. doi: 10.1016/0042-6822(89)90380-2. [DOI] [PubMed] [Google Scholar]
  2. Boyle D. B., Coupar B. E. Construction of recombinant fowlpox viruses as vectors for poultry vaccines. Virus Res. 1988 Jun;10(4):343–356. doi: 10.1016/0168-1702(88)90075-5. [DOI] [PubMed] [Google Scholar]
  3. Cebrian J., Kaschka-Dierich C., Berthelot N., Sheldrick P. Inverted repeat nucleotide sequences in the genomes of Marek disease virus and the herpesvirus of the turkey. Proc Natl Acad Sci U S A. 1982 Jan;79(2):555–558. doi: 10.1073/pnas.79.2.555. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Churchill A. E., Chubb R. C., Baxendale W. The attenuation, with loss of oncogenicity, of the herpes-type virus of Marek's disease (strain HPRS-16) on passage in cell culture. J Gen Virol. 1969 Jun;4(4):557–564. doi: 10.1099/0022-1317-4-4-557. [DOI] [PubMed] [Google Scholar]
  5. Coussens P. M., Velicer L. F. Structure and complete nucleotide sequence of the Marek's disease herpesvirus gp57-65 gene. J Virol. 1988 Jul;62(7):2373–2379. doi: 10.1128/jvi.62.7.2373-2379.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cui Z. Z., Lee L. F., Liu J. L., Kung H. J. Structural analysis and transcriptional mapping of the Marek's disease virus gene encoding pp38, an antigen associated with transformed cells. J Virol. 1991 Dec;65(12):6509–6515. doi: 10.1128/jvi.65.12.6509-6515.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cui Z. Z., Yan D., Lee L. F. Marek's disease virus gene clones encoding virus-specific phosphorylated polypeptides and serological characterization of fusion proteins. Virus Genes. 1990 Apr;3(4):309–322. doi: 10.1007/BF00569038. [DOI] [PubMed] [Google Scholar]
  8. Davison A. J., Moss B. Structure of vaccinia virus early promoters. J Mol Biol. 1989 Dec 20;210(4):749–769. doi: 10.1016/0022-2836(89)90107-1. [DOI] [PubMed] [Google Scholar]
  9. Davison A. J., Moss B. Structure of vaccinia virus late promoters. J Mol Biol. 1989 Dec 20;210(4):771–784. doi: 10.1016/0022-2836(89)90108-3. [DOI] [PubMed] [Google Scholar]
  10. Fukuchi K., Sudo M., Lee Y. S., Tanaka A., Nonoyama M. Structure of Marek's disease virus DNA: detailed restriction enzyme map. J Virol. 1984 Jul;51(1):102–109. doi: 10.1128/jvi.51.1.102-109.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ikuta K., Ueda S., Kato S., Hirai K. Processing of glycoprotein gB related to neutralization of Marek's disease virus and herpesvirus of turkeys. Microbiol Immunol. 1984;28(8):923–933. doi: 10.1111/j.1348-0421.1984.tb00748.x. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Nakajima K., Ikuta K., Naito M., Ueda S., Kato S., Hirai K. Analysis of Marek's disease virus serotype 1-specific phosphorylated polypeptides in virus-infected cells and Marek's disease lymphoblastoid cells. J Gen Virol. 1987 May;68(Pt 5):1379–1389. doi: 10.1099/0022-1317-68-5-1379. [DOI] [PubMed] [Google Scholar]
  14. Nazerian K., Dhawale S., Payne W. S. Structural proteins of two different plaque-size phenotypes of fowlpox virus. Avian Dis. 1989 Jul-Sep;33(3):458–465. [PubMed] [Google Scholar]
  15. Nazerian K., Lee L. F., Yanagida N., Ogawa R. Protection against Marek's disease by a fowlpox virus recombinant expressing the glycoprotein B of Marek's disease virus. J Virol. 1992 Mar;66(3):1409–1413. doi: 10.1128/jvi.66.3.1409-1413.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ogawa R., Yanagida N., Saeki S., Saito S., Ohkawa S., Gotoh H., Kodama K., Kamogawa K., Sawaguchi K., Iritani Y. Recombinant fowlpox viruses inducing protective immunity against Newcastle disease and fowlpox viruses. Vaccine. 1990 Oct;8(5):486–490. doi: 10.1016/0264-410x(90)90251-g. [DOI] [PubMed] [Google Scholar]
  17. Ono K., Takashima M., Ishikawa T., Hayashi M., Yoshida I., Konobe T., Ikuta K., Nakajima K., Ueda S., Kato S. Partial protection against Marek's disease in chickens immunized with glycoproteins gB purified from turkey-herpesvirus-infected cells by affinity chromatography coupled with monoclonal antibodies. Avian Dis. 1985 Apr-Jun;29(2):533–539. [PubMed] [Google Scholar]
  18. Prideaux C. T., Kumar S., Boyle D. B. Comparative analysis of vaccinia virus promoter activity in fowlpox and vaccinia virus recombinants. Virus Res. 1990 Apr;16(1):43–57. doi: 10.1016/0168-1702(90)90042-a. [DOI] [PubMed] [Google Scholar]
  19. Ross L. J., Binns M. M. Properties and evolutionary relationships of the Marek's disease virus homologues of protein kinase, glycoprotein D and glycoprotein I of herpes simplex virus. J Gen Virol. 1991 Apr;72(Pt 4):939–947. doi: 10.1099/0022-1317-72-4-939. [DOI] [PubMed] [Google Scholar]
  20. Ross L. J., Sanderson M., Scott S. D., Binns M. M., Doel T., Milne B. Nucleotide sequence and characterization of the Marek's disease virus homologue of glycoprotein B of herpes simplex virus. J Gen Virol. 1989 Jul;70(Pt 7):1789–1804. doi: 10.1099/0022-1317-70-7-1789. [DOI] [PubMed] [Google Scholar]
  21. Saiki R. K., Scharf S., Faloona F., Mullis K. B., Horn G. T., Erlich H. A., Arnheim N. Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science. 1985 Dec 20;230(4732):1350–1354. doi: 10.1126/science.2999980. [DOI] [PubMed] [Google Scholar]
  22. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Shirakawa M., Tsurimoto T., Matsubara K. Plasmid vectors designed for high-efficiency expression controlled by the portable recA promoter-operator of Escherichia coli. Gene. 1984 Apr;28(1):127–132. doi: 10.1016/0378-1119(84)90096-9. [DOI] [PubMed] [Google Scholar]
  24. Silva R. F., Lee L. F. Monoclonal antibody-mediated immunoprecipitation of proteins from cells infected with Marek's disease virus or turkey herpesvirus. Virology. 1984 Jul 30;136(2):307–320. doi: 10.1016/0042-6822(84)90167-3. [DOI] [PubMed] [Google Scholar]
  25. Sithole I., Lee L. F., Velicer L. F. Synthesis and processing of the Marek's disease herpesvirus B antigen glycoprotein complex. J Virol. 1988 Nov;62(11):4270–4279. doi: 10.1128/jvi.62.11.4270-4279.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tsurushita N., Maki H., Korn L. J. Site-directed mutagenesis with Escherichia coli DNA polymerase III holoenzyme. Gene. 1988;62(1):135–139. doi: 10.1016/0378-1119(88)90587-2. [DOI] [PubMed] [Google Scholar]
  27. Venkatesan S., Baroudy B. M., Moss B. Distinctive nucleotide sequences adjacent to multiple initiation and termination sites of an early vaccinia virus gene. Cell. 1981 Sep;25(3):805–813. doi: 10.1016/0092-8674(81)90188-4. [DOI] [PubMed] [Google Scholar]
  28. Yuen L., Moss B. Oligonucleotide sequence signaling transcriptional termination of vaccinia virus early genes. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6417–6421. doi: 10.1073/pnas.84.18.6417. [DOI] [PMC free article] [PubMed] [Google Scholar]

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