Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Aug;78(8):5202–5206. doi: 10.1073/pnas.78.8.5202

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.

L Pereira, D Dondero, B Norrild, B Roizman
PMCID: PMC320373  PMID: 6272294

Abstract

Herpes simplex virus types 1 and 2 (HSV-1 and HSV-2, respectively) specify five major glycoproteins designated as gA, gB, gC, gD, and gE. Previous studies have shown that gA and gB differ in electrophoretic mobility but not in reactivity with antisera prepared to each of these glycoproteins. Moreover, gA and gB of HSV-1 crossreact in serologic tests with the corresponding glycoproteins of HSV-2. In this paper, we report on the reactivities of gA and gB of HSV-1 and HSV-2 with 24 independently derived monoclonal antibodies reactive with these antigens. Our results show the following: (i) Electrophoretic mobilities of HSV-1 and HSV-2 glycoproteins gA and gB made in HEp-2 cells are significantly less than those made in Vero cells. (ii) All monoclonal antibodies precipitated both gA and gB made in infected HEp-2 cells. These include 12 monoclonal antibodies that neutralized virus and 12 that did not. (iii) HSV-2 glycoproteins gA and gB made in HEp-2 cells contain type-specific domains. However, monoclonal antibodies produced by one clone directed to these domains did not react with glycoproteins made in Vero cells. (iv) Lysates of infected Vero cells contain three lower molecular weight polypeptides that also reacted with monoclonal antibodies directed to glycoproteins gA and gB. These polypeptides are virus specific inasmuch as those specified by HSV-1 differ in electrophoretic mobilities from those specified by HSV-2. these polypeptides are absent in lysates of HEp-2 cells.

Full text

PDF
5204

Images in this article

5203Image
on p.5203
5205Image
on p.5205

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. Cohen G. H., Katze M., Hydrean-Stern C., Eisenberg R. J. Type-common CP-1 antigen of herpes simplex virus is associated with a 59,000-molecular-weight envelope glycoprotein. J Virol. 1978 Jul;27(1):172–181. doi: 10.1128/jvi.27.1.172-181.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. 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]
  5. Ejercito P. M., Kieff E. D., Roizman B. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J Gen Virol. 1968 May;2(3):357–364. doi: 10.1099/0022-1317-2-3-357. [DOI] [PubMed] [Google Scholar]
  6. Kieff E. D., Bachenheimer S. L., Roizman B. Size, composition, and structure of the deoxyribonucleic acid of herpes simplex virus subtypes 1 and 2. J Virol. 1971 Aug;8(2):125–132. doi: 10.1128/jvi.8.2.125-132.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Morse L. S., Pereira L., Roizman B., Schaffer P. A. Anatomy of herpes simplex virus (HSV) DNA. X. Mapping of viral genes by analysis of polypeptides and functions specified by HSV-1 X HSV-2 recombinants. J Virol. 1978 May;26(2):389–410. doi: 10.1128/jvi.26.2.389-410.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. 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]
  11. Powell K. L., Buchan A., Sim C., Watson D. H. Type-specific protein in herpes simplex virus envelope reacts with neutralising antibody. Nature. 1974 May 24;249(455):360–361. doi: 10.1038/249360a0. [DOI] [PubMed] [Google Scholar]
  12. Roizman B., Spear P. G. Preparation of herpes simplex virus of high titer. J Virol. 1968 Jan;2(1):83–84. doi: 10.1128/jvi.2.1.83-84.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ruyechan W. T., Morse L. S., Knipe D. M., Roizman B. Molecular genetics of herpes simplex virus. II. Mapping of the major viral glycoproteins and of the genetic loci specifying the social behavior of infected cells. J Virol. 1979 Feb;29(2):677–697. doi: 10.1128/jvi.29.2.677-697.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sim C., Watson D. H. The role of type specific and cross reacting structural antigens in the neutralization of herpes simplex virus types 1 and 2. J Gen Virol. 1973 May;19(2):217–233. doi: 10.1099/0022-1317-19-2-217. [DOI] [PubMed] [Google Scholar]
  15. Spear P. G. Glycoproteins specified by herpes simplex virus type 1: their synthesis, processing and antigenic relatedness to HSV -2 glycoproteins. IARC Sci Publ. 1975;(11 Pt 1):49–61. [PubMed] [Google Scholar]
  16. 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]
  17. Spear P. G., Roizman B. Proteins specified by herpes simplex virus, IV. Site of glycosylation and accumulation of viral membrane proteins. Proc Natl Acad Sci U S A. 1970 Jul;66(3):730–737. doi: 10.1073/pnas.66.3.730. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Vestergaard B. F., Norrild B. Crossed immunoelectrophoresis of a herpes simplex virus type 1-specific antigen: immunological and biochemical characterization. J Infect Dis. 1978 Nov;138(5):639–643. doi: 10.1093/infdis/138.5.639. [DOI] [PubMed] [Google Scholar]
  19. Zweig M., Heilman C. J., Jr, Rabin H., Hampar B. Shared antigenic determinants between two distinct classes of proteins in cells infected with herpes simplex virus. J Virol. 1980 Sep;35(3):644–652. doi: 10.1128/jvi.35.3.644-652.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES