Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1986 May;58(2):689–693. doi: 10.1128/jvi.58.2.689-693.1986

Expression of herpes simplex virus glycoproteins in polarized epithelial cells.

R V Srinivas, N Balachandran, F V Alonso-Caplen, R W Compans
PMCID: PMC252965  PMID: 3009881

Abstract

Members of the herpesvirus family mature at inner nuclear membranes, although a fraction of the viral glycoproteins is expressed on the cell surface. In this study, we investigated the localization of herpes simplex virus type 2 (HSV-2) glycoproteins in virus-infected epithelial cells by using a panel of monoclonal antibodies directed against each of the major viral glycoproteins. All of the HSV-2 glycoproteins were localized exclusively on the basolateral membranes of Vero C1008, Madin-Darby bovine kidney, and mouse mammary epithelial cells. Using a monoclonal antibody to HSV-2 gD which cross-reacts with HSV-1 strains, we could also localize HSV-1 gD on the basolateral membranes of Madin-Darby bovine kidney cells. These results indicate that these molecules contain putative sorting signals that direct them to basolateral membrane domains.

Full text

PDF
689

Images in this article

689Image
on p.689
690Image
on p.690
690Image
on p.690
691Image
on p.691
692Image
on p.692

Selected References

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

  1. Balachandran N., Bacchetti S., Rawls W. E. Protection against lethal challenge of BALB/c mice by passive transfer of monoclonal antibodies to five glycoproteins of herpes simplex virus type 2. Infect Immun. 1982 Sep;37(3):1132–1137. doi: 10.1128/iai.37.3.1132-1137.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balachandran N., Harnish D., Killington R. A., Bacchetti S., Rawls W. E. Monoclonal antibodies to two glycoproteins of herpes simplex virus type 2. J Virol. 1981 Aug;39(2):438–446. doi: 10.1128/jvi.39.2.438-446.1981. [DOI] [PMC free article] [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. Balachandran N., Hutt-Fletcher L. M. Synthesis and processing of glycoprotein gG of herpes simplex virus type 2. J Virol. 1985 Jun;54(3):825–832. doi: 10.1128/jvi.54.3.825-832.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DeLuca N., Bzik D. J., Bond V. C., Person S., Snipes W. Nucleotide sequences of herpes simplex virus type 1 (HSV-1) affecting virus entry, cell fusion, and production of glycoprotein gb (VP7). Virology. 1982 Oct 30;122(2):411–423. doi: 10.1016/0042-6822(82)90240-9. [DOI] [PubMed] [Google Scholar]
  6. Draper K. G., Frink R. J., Devi G. B., Swain M., Galloway D., Wagner E. K. Herpes simplex virus types 1 and 2 homology in the region between 0.58 and 0.68 map units. J Virol. 1984 Nov;52(2):615–623. doi: 10.1128/jvi.52.2.615-623.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Johnson D. C., Smiley J. R. Intracellular transport of herpes simplex virus gD occurs more rapidly in uninfected cells than in infected cells. J Virol. 1985 Jun;54(3):682–689. doi: 10.1128/jvi.54.3.682-689.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Pellett P. E., Kousoulas K. G., Pereira L., Roizman B. Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: primary sequence and predicted protein structure of the wild type and of monoclonal antibody-resistant mutants. J Virol. 1985 Jan;53(1):243–253. doi: 10.1128/jvi.53.1.243-253.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Richardson J. C., Simmons N. L. Demonstration of protein asymmetries in the plasma membrane of cultured renal (MDCK) epithelial cells by lactoperoxidase-mediated iodination. FEBS Lett. 1979 Sep 15;105(2):201–204. doi: 10.1016/0014-5793(79)80611-0. [DOI] [PubMed] [Google Scholar]
  12. Rodriguez Boulan E., Pendergast M. Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells. Cell. 1980 May;20(1):45–54. doi: 10.1016/0092-8674(80)90233-0. [DOI] [PubMed] [Google Scholar]
  13. Rodriguez Boulan E., Sabatini D. D. Asymmetric budding of viruses in epithelial monlayers: a model system for study of epithelial polarity. Proc Natl Acad Sci U S A. 1978 Oct;75(10):5071–5075. doi: 10.1073/pnas.75.10.5071. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Roth M. G., Compans R. W., Giusti L., Davis A. R., Nayak D. P., Gething M. J., Sambrook J. Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA. Cell. 1983 Jun;33(2):435–443. doi: 10.1016/0092-8674(83)90425-7. [DOI] [PubMed] [Google Scholar]
  15. Roth M. G., Srinivas R. V., Compans R. W. Basolateral maturation of retroviruses in polarized epithelial cells. J Virol. 1983 Mar;45(3):1065–1073. doi: 10.1128/jvi.45.3.1065-1073.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Swain M. A., Peet R. W., Galloway D. A. Characterization of the gene encoding herpes simplex virus type 2 glycoprotein C and comparison with the type 1 counterpart. J Virol. 1985 Feb;53(2):561–569. doi: 10.1128/jvi.53.2.561-569.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Watson R. J., Weis J. H., Salstrom J. S., Enquist L. W. Herpes simplex virus type-1 glycoprotein D gene: nucleotide sequence and expression in Escherichia coli. Science. 1982 Oct 22;218(4570):381–384. doi: 10.1126/science.6289440. [DOI] [PubMed] [Google Scholar]

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

RESOURCES