Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1984 Feb;49(2):594–597. doi: 10.1128/jvi.49.2.594-597.1984

Virus-specific glycoproteins associated with the nuclear fraction of herpes simplex virus type 1-infected cells.

T Compton, R J Courtney
PMCID: PMC255504  PMID: 6319761

Abstract

Monospecific antisera to herpes simplex virus type 1 (HSV-1) glycoproteins gB, gC, and gD were used to identify the HSV-1-specific glycoproteins associated with the nuclear fraction as compared with those associated with cytoplasmic fraction, whole-cell lysates, and purified virions. The results indicate that a predominance of HSV glycoprotein precursors pgC(105), pgB(110), and pgD(52) is associated with the nuclear fraction. Treatment of the nuclear fraction with the enzyme endo-beta-N-acetylglucosaminidase H indicated that the lower-molecular-weight glycoproteins are sensitive to this endoglycosidase. These results suggest that in the nuclear fraction of HSV-1-infected cells virus-specific glycoproteins gB, gC, and gD are predominately in the high-mannose precursor form; however, detectable amounts of the fully glycosylated forms of gC and gD were also found.

Full text

PDF
595

Images in this article

595Image
on p.595
596Image
on p.596
596Image
on p.596

Selected References

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

  1. Baucke R. B., Spear P. G. Membrane proteins specified by herpes simplex viruses. V. Identification of an Fc-binding glycoprotein. J Virol. 1979 Dec;32(3):779–789. doi: 10.1128/jvi.32.3.779-789.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Campadelli-Fiume G., Poletti L., Dall'Olio F., Serafini-Cessi F. Infectivity and glycoprotein processing of herpes simplex virus type 1 grown in a ricin-resistant cell line deficient in N-acetylglucosaminyl transferase I. J Virol. 1982 Sep;43(3):1061–1071. doi: 10.1128/jvi.43.3.1061-1071.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cohen G. H., Long D., Eisenberg R. J. Synthesis and processing of glycoproteins gD and gC of herpes simplex virus type 1. J Virol. 1980 Nov;36(2):429–439. doi: 10.1128/jvi.36.2.429-439.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Courtney R. J. Herpes simplex virus protein synthesis in the presence of 2-deoxy-D-glucose. Virology. 1976 Aug;73(1):286–294. doi: 10.1016/0042-6822(76)90081-7. [DOI] [PubMed] [Google Scholar]
  5. Darlington R. W., Moss L. H., 3rd Herpesvirus envelopment. J Virol. 1968 Jan;2(1):48–55. doi: 10.1128/jvi.2.1.48-55.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Eberle R., Courtney R. J. Preparation and characterization of specific antisera to individual glycoprotein antigens comprising the major glycoprotein region of herpes simplex virus type 1. J Virol. 1980 Sep;35(3):902–917. doi: 10.1128/jvi.35.3.902-917.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eberle R., Courtney R. J. gA and gB glycoproteins of herpes simplex virus type 1: two forms of a single polypeptide. J Virol. 1980 Dec;36(3):665–675. doi: 10.1128/jvi.36.3.665-675.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Eisenberg R. J., Hydrean-Stern C., Cohen G. H. Structural analysis of precursor and product forms of type-common envelope glycoprotein D (CP-1 antigen) of herpes simplex virus type 1. J Virol. 1979 Sep;31(3):608–620. doi: 10.1128/jvi.31.3.608-620.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Frink R. J., Eisenberg R., Cohen G., Wagner E. K. Detailed analysis of the portion of the herpes simplex virus type 1 genome encoding glycoprotein C. J Virol. 1983 Feb;45(2):634–647. doi: 10.1128/jvi.45.2.634-647.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Haffey M. L., Spear P. G. Alterations in glycoprotein gB specified by mutants and their partial revertants in herpes simplex virus type 1 and relationship to other mutant phenotypes. J Virol. 1980 Jul;35(1):114–128. doi: 10.1128/jvi.35.1.114-128.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Harris J. R. The biochemistry and ultrastructure of the nuclear envelope. Biochim Biophys Acta. 1978 Apr 10;515(1):55–104. doi: 10.1016/0304-4157(78)90008-4. [DOI] [PubMed] [Google Scholar]
  12. Honess R. W., Roizman B. Proteins specified by herpes simplex virus. XIII. Glycosylation of viral polypeptides. J Virol. 1975 Nov;16(5):1308–1326. doi: 10.1128/jvi.16.5.1308-1326.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Johnson D. C., Spear P. G. Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells. J Virol. 1982 Sep;43(3):1102–1112. doi: 10.1128/jvi.43.3.1102-1112.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Johnson D. C., Spear P. G. O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Cell. 1983 Mar;32(3):987–997. doi: 10.1016/0092-8674(83)90083-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kawasaki T., Yamashina I. Isolation and characterization of glycopeptides from rat liver nuclear membrane. J Biochem. 1972 Dec;72(6):1517–1525. doi: 10.1093/oxfordjournals.jbchem.a130043. [DOI] [PubMed] [Google Scholar]
  16. Lee G. T., Pogue-Geile K. L., Pereira L., Spear P. G. Expression of herpes simplex virus glycoprotein C from a DNA fragment inserted into the thymidine kinase gene of this virus. Proc Natl Acad Sci U S A. 1982 Nov;79(21):6612–6616. doi: 10.1073/pnas.79.21.6612. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. MORGAN C., ELLISON S. A., ROSE H. M., MOORE D. H. Structure and development of viruses as observed in the electron microscope. I. Herpes simplex virus. J Exp Med. 1954 Aug 1;100(2):195–202. doi: 10.1084/jem.100.2.195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. MORGAN C., ROSE H. M., HOLDEN M., JONES E. P. Electron microscopic observations on the development of herpes simplex virus. J Exp Med. 1959 Oct 1;110:643–656. doi: 10.1084/jem.110.4.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Nii S., Morgan C., Rose H. M. Electron microscopy of herpes simplex virus. II. Sequence of development. J Virol. 1968 May;2(5):517–536. doi: 10.1128/jvi.2.5.517-536.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Olofsson S., Blomberg J., Lycke E. O-glycosidic carbohydrate-peptide linkages of Herpes simplex virus glycoproteins. Arch Virol. 1981;70(4):321–329. doi: 10.1007/BF01320247. [DOI] [PubMed] [Google Scholar]
  21. Olofsson S., Jeansson S., Lycke E. Unusual lectin-binding properties of a herpes simplex virus type 1-specific glycoprotein. J Virol. 1981 May;38(2):564–570. doi: 10.1128/jvi.38.2.564-570.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Penman S. RNA metabolism in the HeLa cell nucleus. J Mol Biol. 1966 May;17(1):117–130. doi: 10.1016/s0022-2836(66)80098-0. [DOI] [PubMed] [Google Scholar]
  23. Pizer L. I., Cohen G. H., Eisenberg R. J. Effect of tunicamycin on herpes simplex virus glycoproteins and infectious virus production. J Virol. 1980 Apr;34(1):142–153. doi: 10.1128/jvi.34.1.142-153.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Powell K. L., Courtney R. J. Polypeptide synthesized in herpes simplex virus type 2-infected HEp-2 cells. Virology. 1975 Jul;66(1):217–228. doi: 10.1016/0042-6822(75)90192-0. [DOI] [PubMed] [Google Scholar]
  25. Serafini-Cessi F., Campadelli-Fiume G. Studies on benzhydrazone, a specific inhibitor of herpesvirus glycoprotein synthesis. Size distribution of glycopeptides and endo-beta-N-acetylglucosaminidase-H treatment. Arch Virol. 1981;70(4):331–343. doi: 10.1007/BF01320248. [DOI] [PubMed] [Google Scholar]
  26. Spear P. G. Membrane proteins specified by herpes simplex viruses. I. Identification of four glycoprotein precursors and their products in type 1-infected cells. J Virol. 1976 Mar;17(3):991–1008. doi: 10.1128/jvi.17.3.991-1008.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Spear P. G., Roizman B. The proteins specified by herpes simplex virus. I. Time of synthesis, transfer into nuclei, and properties of proteins made in productively infected cells. Virology. 1968 Dec;36(4):545–555. doi: 10.1016/0042-6822(68)90186-4. [DOI] [PubMed] [Google Scholar]
  28. Stackpole C. W. Herpes-type virus of the frog renal adenocarcinoma. I. Virus development in tumor transplants maintained at low temperature. J Virol. 1969 Jul;4(1):75–93. doi: 10.1128/jvi.4.1.75-93.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Tabas I., Schlesinger S., Kornfeld S. Processing of high mannose oligosaccharides to form complex type oligosaccharides on the newly synthesized polypeptides of the vesicular stomatitis virus G protein and the IgG heavy chain. J Biol Chem. 1978 Feb 10;253(3):716–722. [PubMed] [Google Scholar]
  30. Takatsuki A., Tamura G. Effect of tunicamycin on the synthesis of macromolecules in cultures of chick embryo fibroblasts infected with Newcastle disease virus. J Antibiot (Tokyo) 1971 Nov;24(11):785–794. doi: 10.7164/antibiotics.24.785. [DOI] [PubMed] [Google Scholar]
  31. Tarentino A. L., Maley F. Purification and properties of an endo-beta-N-acetylglucosaminidase from Streptomyces griseus. J Biol Chem. 1974 Feb 10;249(3):811–817. [PubMed] [Google Scholar]
  32. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. WARNER J. R., KNOPF P. M., RICH A. A multiple ribosomal structure in protein synthesis. Proc Natl Acad Sci U S A. 1963 Jan 15;49:122–129. doi: 10.1073/pnas.49.1.122. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Wenske E. A., Bratton M. W., Courtney R. J. Endo-beta-N-acetylglucosaminidase H sensitivity of precursors to herpes simplex virus type 1 glycoproteins gB and gC. J Virol. 1982 Oct;44(1):241–248. doi: 10.1128/jvi.44.1.241-248.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Wenske E. A., Courtney R. J. Glycosylation of herpes simplex virus type 1 gC in the presence of tunicamycin. J Virol. 1983 Apr;46(1):297–301. doi: 10.1128/jvi.46.1.297-301.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES