1887

Journal of General Virology header logo

Volume 72, Issue 2

The difference in sensitivity to cicloxolone sodium between herpes simplex virus types 1 and 2 maps to the locations of genes UL22 (gH) and UL44 (gC) Free

Abstract

Cicloxolone sodium (CCX) is a broad spectrum anti-viral agent which has a largely non-specific and complex mode of antiviral action. However, the experimental finding that herpes simplex virus type 2 (HSV-2) (strain HG52) is consistently more sensitive to inhibition by CCX than HSV-1 (117 syn) additionally implies the specific involvement of HSV genes. HSV-1/HSV-2 intertypic recombinants have been utilized to investigate this genetic difference by comparing their CCX ED concentrations. No short stretch of HSV-2 DNA was associated with its greater sensitivity to CCX, implying that two or more non-contiguously located HSV genes are involved. Correlating CCX sensitivity with recombinant virus genome structures allowed separate evaluation of the gene regions encoding glycoproteins gB, gC, gD, gE, gG, gH and gI and this suggests that the gene locations encoding gH and gC determine the CCX sensitivity difference. The selective inhibitor of Golgi apparatus glycosylation, monensin, gave results analogous to those obtained with CCX.

  • Received:
  • Accepted:
  • Published Online:
© Journal of General Virology 1991
Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-72-2-377
1991-02-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/jgv/72/2/JV0720020377.html?itemId=/content/journal/jgv/10.1099/0022-1317-72-2-377&mimeType=html&fmt=ahah

References

  1. Boss W. F., Morre D. J., Mollenhauer H. H. 1984; Monensin-induced swelling of Golgi apparatus cistemae mediated by a proton gradient. European Journal of Cell Biology 34:1–8
     [Google Scholar]
  2. Brown S. M., Ritchie D. A., Subak-Sharpe J. H. 1973; Genetic studies with herpes simplex virus type 1. The isolation of temperature-sensitive mutants, their arrangement into complementation groups and recombination analysis leading to a linkage map. Journal of General Virology 18:329–346
     [Google Scholar]
  3. Brown S. M., Harland J., Subak-Sharpe J. H. 1984; Isolation of restriction endonuclease site deletion mutants of herpes simplex virus. Journal of General Virology 65:1053–1068
     [Google Scholar]
  4. Buckmaster E. A., Gompels U., Minson A. 1984; Characterization and physical mapping of an HSV-1 glycoprotein of approximately 115 × 103 molecular weight. Virology 139:408–413
     [Google Scholar]
  5. Chartrand P., Stow N. D., Timbury M. C., Wilkie N. M. 1979; Physical mapping of paar mutations of herpes simplex virus type 1 and type 2 by intertypic marker rescue. Journal of Virology 31:265–276
     [Google Scholar]
  6. Chartrand P., Wilkie N. M., Timbury M. C. 1981; Physical mapping of temperature-sensitive mutations of herpes simplex virus type 2 by marker rescue. Journal of General Virology 52:121–133
     [Google Scholar]
  7. Dargan D. J., Subak-Sharpe J. H. 1985; The effect of triterpenoid compounds on uninfected and herpes simplex virus-infected cells in culture. I. Effect on cell growth, virus particles and virus replication. Journal of General Virology 66:1771–1784
     [Google Scholar]
  8. Dargan D. J., Subak-Sharpe J. H. 1986a; The effect of triterpenoid compounds on uninfected and herpes simplex virus-infected cells in culture. II. DNA and protein synthesis, polypeptide processing and transport. Journal of General Virology 67:1831–1850
     [Google Scholar]
  9. Dargan D. J., Subak-Sharpe J. H. 1986b; The antiherpes activity of the triterpenoid compounds carbenoxolone sodium and cicloxolone sodium. Journal of Antimicrobial Chemotherapy 18: supplement W 185–200
     [Google Scholar]
  10. Dargan D. J., Aitken J. D., Subak-Sharpe J. H. 1988; The effect of triterpenoid compounds on uninfected and herpes simplex virus-infected cells in culture. III. Ultrastructural study of virion maturation. Journal of General Virology 69:439–444
     [Google Scholar]
  11. DeLuca N., Bzik D. J., Bond V. C., Person S., Snipes W. 1982; Nucleotide sequences of herpes simplex virus type 1 (HSV-1) affecting virus entry, cell fusion and production of glycoprotein gB (VP7). Virology 122:411–423
     [Google Scholar]
  12. Desai P. J., Schaffer P. A., Minson A. C. 1988; Excretion of non-infectious virus particles lacking glycoprotein H by a temperature-senstitive mutant of herpes simplex virus type 1: evidence that gH is essential for virion infectivity. Journal of General Virology 69:1147–1156
     [Google Scholar]
  13. Epstein A. L., Jacquemont B., Machuca I. 1984; Infection of a restrictive cell line (XC cells) by intratypic recombinants of HSV-1: relationship between penetration of the virus and relative amounts of glycoprotein C. Virology 132:315–324
     [Google Scholar]
  14. Fuller O. A., Santos R. E., Spear P. G. 1989; Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration. Journal of Virology 63:3435–3443
     [Google Scholar]
  15. Galt C., Dargan D. J., Subak-Sharpe J. H. 1990; In vitro studies of the antiviral range of cicloxolone sodium and identification of cell lines tolerant to the drug. Antiviral Chemistry and Chemotherapy 1:115–123
     [Google Scholar]
  16. Ghosh-Choudhury N., Graham A., Ghosh H. P. 1987; Herpes simplex virus type 2 glycoprotein biogenesis: effect of monensin on glycoprotein maturation, intracellular transport and virus infectivity. Journal of General Virology 68:1939–1949
     [Google Scholar]
  17. Gompels U., Minson A. 1986; The properties and sequence of glycoprotein H of herpes simplex virus type 1. Virology 153:230–247
     [Google Scholar]
  18. Gompels U. A., Minson A. C. 1989; Antigenic properties and cellular localization of herpes simplex virus glycoprotein H synthesized in a mammalian cell expression system. Journal of Virology 63:4744–4755
     [Google Scholar]
  19. Griffiths G., Quin P., Warren G. 1983; Dissection of the Golgi complex. I. Monsensin inhibits the transport of viral membrane proteins from medial to trans Golgi cisternae in baby hamster kidney cells infected with Semliki Forest virus. Journal of Cell Biology 96:835–850
     [Google Scholar]
  20. Holland T. C., Homa F. L., Marlin S. D., Levine M., Glorioso J. 1984; Herpes simplex virus type 1 glycoprotein C negative mutants exhibit multiple phenotypes, including secretion of truncated glycoproteins. Journal of Virology 52:566–574
     [Google Scholar]
  21. Homa F. L., Purifoy D. J. M., Glorioso J. C., Levine M. 1986; Molecular basis of the glycoprotein C negative phenotypes of herpes simplex virus type 1 mutants selected with a virus-neutralizing monoclonal antibody. Journal of Virology 58:281–289
     [Google Scholar]
  22. Johnson D. C., Spear P. G. 1982; Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface and the egress of virions from infected cells. Journal of Virology 43:1102–1112
     [Google Scholar]
  23. Johnson D. C., Spear P. G. 1983; O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Cell 32:987–997
     [Google Scholar]
  24. Kousoulas K., Bzik D. J., Person S. 1983; Effect of the ionophore monensin on herpes simplex virus type 1-induced cell fusion, glycoprotein synthesis, and virion infectivity. Intervirology 20:56–60
     [Google Scholar]
  25. Langeland N., Øyan A. M., Marsden H. S., Cross A., Glorioso J. C., Moore L. J., Haarr L. 1990; Localization on the herpes simplex virus type 1 genome of a region encoding proteins involved in adsorption to the cellular receptor. Journal of Virology 64:1271–1277
     [Google Scholar]
  26. McGeoch D. J., Dalrymple M. A., Davison A. J., Dolan A., Frame M. C., McNab D., Perry L. L., Scott J. E., Taylor P. 1988; The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. Journal of General Virology 69:1531–1574
     [Google Scholar]
  27. McNearney T. A., Odell C., Holers V. M., Spear P. G., Atkinson J. P. 1987; Herpes simplex virus glycoproteins gC-1 and gC-2 bind to the third component of complement and provide protection against complement-mediated neutralization of viral infectivity. Journal of Experimental Medicine 166:1525–1535
     [Google Scholar]
  28. Marsden H. S., Stow N. D., Preston V. G., Timbury M. C., Wilkie N. M. 1978; Physical mapping of herpes simplex virusinduced polypeptides. Journal of Virology 28:624–642
     [Google Scholar]
  29. Preston V. G., Davison A. J., Marsden H. S., Timbury M. C., Subak-Sharpe J. H., Wilkie N. M. 1978; Recombinants between herpes simplex virus types 1 and 2: analysis of genome structures and expression of immediate early polypeptides. Journal of Virology 28:499–517
     [Google Scholar]
  30. Seidel-Dugan C., Ponce de Leon M., Freidman H. M., Eisenberg R. J., Cohen G. H. 1990; Identification of C3b-binding regions of herpes simplex virus type 2 glycoprotein C. Journal of Virology 64:1897–1906
     [Google Scholar]
  31. Stow N. D., Wilkie N. M. 1978; Physical mapping of temperature-sensitive mutations of herpes simplex virus type 1 by intertypic marker rescue. Virology 90:1–11
     [Google Scholar]
  32. Timbury M. C. 1971; Temperature-sensitive mutants of herpes simplex virus type 2. Journal of General Virology 13:373–376
     [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-72-2-377
Loading
The difference in sensitivity to cicloxolone sodium between herpes simplex virus types 1 and 2 maps to the locations of genes UL22 (gH) and UL44 (gC)
J. Gen. Virol. 72, 377 (1991); https://doi.org/10.1099/0022-1317-72-2-377
/content/journal/jgv/10.1099/0022-1317-72-2-377
/content/journal/jgv/10.1099/0022-1317-72-2-377
Loading

Data & Media loading...

Most cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error