1887

Abstract

The post-translational events leading from the precursor to the processed forms of a glycoprotein with an of 28K to 32K (gp28/32) of Marek’s disease virus (MDV) serotype 2 were examined with pulse-chase experiments and treatment with tunicamycin and monensin. Cell-free translation of infected cell mRNA followed by immunoprecipitation analysis suggested that a polypeptide with a size of 22K is the initial precursor. Experiments with endo---acetylglucosa- minidase H and endo---acetylglucosaminidase F indicated that gp28/32 contains mostly -linked oligosaccharides of the complex type. These studies showed that 22K, the initial product, is then processed through intermediates to the 28K to 32K form.

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1990-08-01
2024-12-14
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References

  1. Binns M. M., Ross N. L. J. 1989; Nucleotide sequence of the Marek’s disease virus (MDV) RB-1B A antigen gene and the identification of the MDV A antigen as the herpes simplex virus-1 glycoprotein C homologue. Virus Research 12:371–382
    [Google Scholar]
  2. Carter V. C., Schaffer P. A., Tevethia S. S. 1981; The involvement of herpes simplex type 1 glycoproteins in cell-mediated immunity. Journal of Immunology 126:1655–1660
    [Google Scholar]
  3. Chirgwin J. M., Przybyla A. E., Macdonald R. J., Rutter W. J. 1979; Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294–5299
    [Google Scholar]
  4. Eberle R., Courtney R. J. 1980; Preparation and characterization of specific antisera to individual glycoprotein antigens comprising the major glycoprotein region of herpes simplex virus type 1. Journal of Virology 35:902–917
    [Google Scholar]
  5. Frame M. C., Marsden H. S., McGeoch D. J. 1986; Novel herpes simplex virus type 1 glycoproteins identified by antiserum against a synthetic oligopeptide from the predicted product of gene US4. Journal of General Virology 67:745–751
    [Google Scholar]
  6. Heifetz A., Keenan R. W., Elbein A. D. 1979; Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate GlcNAc-1- phosphate transferase. Biochemistry 18:2186–2192
    [Google Scholar]
  7. Hirai K., Nakajima K., Ikuta K., Kirisawa R., Kawakami Y., Mikami T., Kato S. 1986; Similarities and dissimilarities in the structure and expression of viral genomes of various virus strains immunologically related to Marek’s disease virus. Archives of Virology 89:113–130
    [Google Scholar]
  8. Ituka K., Ueda S., Kato S., Hirai K. 1983; Monoclonal antibodies reactive with the surface and secreted glycoproteins of Marek’s disease virus and herpesvirus of turkeys. Journal of General Virology 64:2597–2610
    [Google Scholar]
  9. Ikuta K., Nakajima K., Ueda S., Kato S., Hirai K. 1985; Differences in the processing of secreted glycoprotein A induced by Marek’s disease virus and herpesvirus of turkeys. Journal of General Virology 66:1131–1137
    [Google Scholar]
  10. Kato A., Sato I., Ihara T., Ueda S., Ishihama A., Hirai K. 1989; Homology and collinear arrangement of two open reading frames including a secreted glycoprotein A gene between herpesvirus of turkeys and Marek’s disease virus type 1. Gene 84:399–405
    [Google Scholar]
  11. Kato S., Hirai K. 1985; Marek’s disease virus. Advances in Virus Research 30:225–227
    [Google Scholar]
  12. Loh L. C. 1989; Synthesis and processing of a 22-26K murine cytomegalovirus glycoprotein recognized by a neutralizing monoclonal antibody. Virology 169:474–478
    [Google Scholar]
  13. Long P. A., Clark J. L., Velicer L. F. 1975; Marek’s disease herpesviruses. II. Purification and further characterization of Marek’s disease herpesvirus A antigen. Journal of Virology 15:1192–1201
    [Google Scholar]
  14. Nakajima K., Ikuta K., Ueda S., Kato S., Hirai K. 1986; Identification with monoclonal antibodies of virus-specific DNA-binding proteins in the nuclei of cells infected with three serotypes of Marek’s disease virus-related viruses. Journal of Virology 59:154–158
    [Google Scholar]
  15. Nakajima K., Shibayama T., Yokota M., Ikuta K., Kato S., Hirai K. 1989; Identification of virus-specific polypeptides by monoclonal antibodies against serotype 2 Marek’s disease virus. Journal of General Virology 70:2563–2571
    [Google Scholar]
  16. Ross L. J. N., Sanderson M., Scott S. D., Binns M. M., Doel T., Milne B. 1989; Nucleotide sequence and characterization of the Marek’s disease virus homologue of glycoprotein B of herpes simplex virus. Journal of General Virology 70:1789–1804
    [Google Scholar]
  17. Rothman J. E., Katz F. N., Lodish H. F. 1978; Glycosylation of a membrane protein is restricted to the growing polypeptide chain but is not necessary for insertion as a transmembrane protein. Cell 15:1447–1454
    [Google Scholar]
  18. Sithole I., Lee L. F., Velicer L. F. 1988; Synthesis and processing of the Marek’s disease herpesvirus B antigen glycoprotein complex. Journal of Virology 62:4270–4279
    [Google Scholar]
  19. Snowden B. W., Kinchington P. R., Powell K. L., Halliburton I. W. 1985; Antigenic and biochemical analysis of gB of herpes simplex virus type 1 and type 2 and of cross-reacting glycoproteins induced by bovine mammillitis virus and equine herpesvirus type 1. Journal of General Virology 66:231–247
    [Google Scholar]
  20. Velicer L. F., Yager D. R., Clark J. L. 1978; Marek’s disease herpesviruses. III. Purification and characterization of Marek’s disease herpesvirus B antigen. Journal of Virology 27:205–217
    [Google Scholar]
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