Skip to main content
Journal of Virology logoLink to Journal of Virology
. 1987 Jan;61(1):104–112. doi: 10.1128/jvi.61.1.104-112.1987

Kinetics of expression of herpes simplex virus type 1-specific glycoprotein species on the surfaces of infected murine, simian, and human cells: flow cytometric analysis.

S R Jennings, P A Lippe, K J Pauza, P G Spear, L Pereira, S S Tevethia
PMCID: PMC255213  PMID: 3023688

Abstract

The kinetics of expression of the herpes simplex virus type 1-encoded major glycoprotein species gB, gC, gD, and gE on the surfaces of cells of murine, simian, and human origins were studied. Viable cells were stained with monoclonal antibodies specific for each species, and the levels expressed were determined by fluorescence flow cytometry. Differences were observed in both the kinetics and the levels of expression of individual glycoprotein species, depending upon the origin of the host cells. Glycoprotein gC was expressed early and at high levels in cells of murine and human origins, but late and at relatively low levels in simian cells. In contrast, gE was expressed at high levels in simian cells, but was not detectable until late in the infectious cycle in murine and human cells. The kinetics and levels of expression of gB were similar for all cells investigated, whereas gD, with high levels of expression in all cells late in infection, appeared on the surfaces of murine cells very early postinfection. This approach has allowed a simple quantitative method for comparing levels of glycoprotein expression.

Full text

PDF
104

Selected References

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

  1. Ackermann M., Chou J., Sarmiento M., Lerner R. A., Roizman B. Identification by antibody to a synthetic peptide of a protein specified by a diploid gene located in the terminal repeats of the L component of herpes simplex virus genome. J Virol. 1986 Jun;58(3):843–850. doi: 10.1128/jvi.58.3.843-850.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ackermann M., Longnecker R., Roizman B., Pereira L. Identification, properties, and gene location of a novel glycoprotein specified by herpes simplex virus 1. Virology. 1986 Apr 15;150(1):207–220. doi: 10.1016/0042-6822(86)90280-1. [DOI] [PubMed] [Google Scholar]
  3. Balachandran N., Harnish D., Rawls W. E., Bacchetti S. Glycoproteins of herpes simplex virus type 2 as defined by monoclonal antibodies. J Virol. 1982 Oct;44(1):344–355. doi: 10.1128/jvi.44.1.344-355.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. Buckmaster E. A., Gompels U., Minson A. Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10(3) molecular weight. Virology. 1984 Dec;139(2):408–413. doi: 10.1016/0042-6822(84)90387-8. [DOI] [PubMed] [Google Scholar]
  6. Carter V. C., Schaffer P. A., Tevethia S. S. The involvement of herpes simplex virus type 1 glycoproteins in cell-mediated immunity. J Immunol. 1981 May;126(5):1655–1660. [PubMed] [Google Scholar]
  7. 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]
  8. Eberle R., Russell R. G., Rouse B. T. Cell-mediated immunity to herpes simplex virus: recognition of type-specific and type-common surface antigens by cytotoxic T cell populations. Infect Immun. 1981 Dec;34(3):795–803. doi: 10.1128/iai.34.3.795-803.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Friedman H. M., Cohen G. H., Eisenberg R. J., Seidel C. A., Cines D. B. Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells. Nature. 1984 Jun 14;309(5969):633–635. doi: 10.1038/309633a0. [DOI] [PubMed] [Google Scholar]
  10. Glorioso J. C., Smith J. W. Immune interactions with cells infected with herpes simplex virus: antibodies to radioiodinated surface antigens. J Immunol. 1977 Jan;118(1):114–121. [PubMed] [Google Scholar]
  11. Glorioso J. C., Wilson L. A., Fenger T. W., Smith J. W. Complement-mediated cytolysis of HSV-1 and HSV-2 infected cells: plasma membrane antigens reactive with type-specific and cross-reactive antibody. J Gen Virol. 1978 Aug;40(2):443–454. doi: 10.1099/0022-1317-40-2-443. [DOI] [PubMed] [Google Scholar]
  12. Glorioso J., Kees U., Kümel G., Kirchner H., Krammer P. H. Identification of herpes simplex virus type 1 (HSV-1) glycoprotein gC as the immunodominant antigen for HSV-1-specific memory cytotoxic T lymphocytes. J Immunol. 1985 Jul;135(1):575–582. [PubMed] [Google Scholar]
  13. Glorioso J., Szczesiul M. S., Marlin S. D., Levine M. Inhibition of glycosylation of herpes simplex virus glycoproteins: identification of antigenic and immunogenic partially glycosylated glycopeptides on the cell surface membrane. Virology. 1983 Apr 15;126(1):1–18. doi: 10.1016/0042-6822(83)90458-0. [DOI] [PubMed] [Google Scholar]
  14. 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]
  15. Heine J. W., Spear P. G., Roizman B. Proteins specified by herpes simplex virus. VI. Viral proteins in the plasma membrane. J Virol. 1972 Mar;9(3):431–439. doi: 10.1128/jvi.9.3.431-439.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. Honess R. W., Roizman B. Regulation of herpesvirus macromolecular synthesis: sequential transition of polypeptide synthesis requires functional viral polypeptides. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1276–1280. doi: 10.1073/pnas.72.4.1276. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Johnson D. C., Spear P. G. Evidence for translational regulation of herpes simplex virus type 1 gD expression. J Virol. 1984 Aug;51(2):389–394. doi: 10.1128/jvi.51.2.389-394.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. 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]
  21. Lawman M. J., Courtney R. J., Eberle R., Schaffer P. A., O'Hara M. K., Rouse B. T. Cell-mediated immunity to herpes simplex virus: specificity of cytotoxic T cells. Infect Immun. 1980 Nov;30(2):451–461. doi: 10.1128/iai.30.2.451-461.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Little S. P., Jofre J. T., Courtney R. J., Schaffer P. A. A virion-associated glycoprotein essential for infectivity of herpes simplex virus type 1. Virology. 1981 Nov;115(1):149–160. doi: 10.1016/0042-6822(81)90097-0. [DOI] [PubMed] [Google Scholar]
  23. Machtiger N. A., Pancake B. A., Eberle R., Courtney R. J., Tevethia S. S., Schaffer P. A. Herpes simplex virus glycoproteins: isolation of mutants resistant to immune cytolysis. J Virol. 1980 May;34(2):336–346. doi: 10.1128/jvi.34.2.336-346.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Manservigi R., Spear P. G., Buchan A. Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3913–3917. doi: 10.1073/pnas.74.9.3913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Marsden H. S., Buckmaster A., Palfreyman J. W., Hope R. G., Minson A. C. Characterization of the 92,000-dalton glycoprotein induced by herpes simplex virus type 2. J Virol. 1984 May;50(2):547–554. doi: 10.1128/jvi.50.2.547-554.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Noble A. G., Lee G. T., Sprague R., Parish M. L., Spear P. G. Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type 1. Virology. 1983 Aug;129(1):218–224. doi: 10.1016/0042-6822(83)90409-9. [DOI] [PubMed] [Google Scholar]
  28. Norrild B., Bjerrum O. J., Ludwig H., Vestergaard B. F. Analysis of herpes simplex virus type 1 antigens exposed on the surface of infected tissue culture cells. Virology. 1978 Jun 15;87(2):307–316. doi: 10.1016/0042-6822(78)90136-8. [DOI] [PubMed] [Google Scholar]
  29. Norrild B. Immunochemistry of herpes simplex virus glycoproteins. Curr Top Microbiol Immunol. 1980;90:67–106. doi: 10.1007/978-3-642-67717-5_4. [DOI] [PubMed] [Google Scholar]
  30. Norrild B., Shore S. L., Nahmias A. J. Herpes simplex virus glycoproteins: participation of individual herpes simplex virus type 1 glycoprotein antigens in immunocytolysis and their correlation with previously identified glycopolypeptides. J Virol. 1979 Dec;32(3):741–748. doi: 10.1128/jvi.32.3.741-748.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Para M. F., Baucke R. B., Spear P. G. Glycoprotein gE of herpes simplex virus type 1: effects of anti-gE on virion infectivity and on virus-induced fc-binding receptors. J Virol. 1982 Jan;41(1):129–136. doi: 10.1128/jvi.41.1.129-136.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Pereira L., Dondero D., Norrild B., Roizman B. Differential immunologic reactivity and processing of glycoproteins gA and gB of herpes simplex virus types 1 and 2 made in Vero and HEp-2 cells. Proc Natl Acad Sci U S A. 1981 Aug;78(8):5202–5206. doi: 10.1073/pnas.78.8.5202. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Pereira L., Dondero D., Roizman B. Herpes simplex virus glycoprotein gA/B: evidence that the infected Vero cell products comap and arise by proteolysis. J Virol. 1982 Oct;44(1):88–97. doi: 10.1128/jvi.44.1.88-97.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Pereira L., Klassen T., Baringer J. R. Type-common and type-specific monoclonal antibody to herpes simplex virus type 1. Infect Immun. 1980 Aug;29(2):724–732. doi: 10.1128/iai.29.2.724-732.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Pereira L. Use of monoclonal antibodies to HSV-1 and HSV-2 for serological analysis of the viral glycoproteins. Dev Biol Stand. 1982;52:115–131. [PubMed] [Google Scholar]
  36. Pretell J., Greenfield R. S., Tevethia S. S. Biology of simian virus 40 (SV40) transplantation antigen (TrAg). V In vitro demonstration of SV40 TrAg in SV40 infected nonpermissive mouse cells by the lymphocyte mediated cytotoxicity assay. Virology. 1979 Aug;97(1):32–41. doi: 10.1016/0042-6822(79)90370-2. [DOI] [PubMed] [Google Scholar]
  37. Richman D. D., Buckmaster A., Bell S., Hodgman C., Minson A. C. Identification of a new glycoprotein of herpes simplex virus type 1 and genetic mapping of the gene that codes for it. J Virol. 1986 Feb;57(2):647–655. doi: 10.1128/jvi.57.2.647-655.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Roizman B., Norrild B., Chan C., Pereira L. Identification and preliminary mapping with monoclonal antibodies of a herpes simplex virus 2 glycoprotein lacking a known type 1 counterpart. Virology. 1984 Feb;133(1):242–247. doi: 10.1016/0042-6822(84)90447-1. [DOI] [PubMed] [Google Scholar]
  39. Sarmiento M., Haffey M., Spear P. G. Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7(B2) in virion infectivity. J Virol. 1979 Mar;29(3):1149–1158. doi: 10.1128/jvi.29.3.1149-1158.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Showalter S. D., Zweig M., Hampar B. Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4. Infect Immun. 1981 Dec;34(3):684–692. doi: 10.1128/iai.34.3.684-692.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. 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]
  42. Vahlne A., Blomberg J., Olofsson S., Lycke E. Subtyping of herpes simplex virus. Acta Pathol Microbiol Scand B. 1975 Oct;83(5):506–512. doi: 10.1111/j.1699-0463.1975.tb00131.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES