Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1976 May;18(2):644–651. doi: 10.1128/jvi.18.2.644-651.1976

Effects of 2-deoxyglucose, glucosamine, and mannose on cell fusion and the glycoproteins of herpes simplex virus.

R W Knowles, S Person
PMCID: PMC515591  PMID: 178901

Abstract

2-Deoxyglucose and glucosamine were found to inhibit cell fusion caused by a syncytial mutant of herpes simplex virus and to inhibit the glycosylation of viral glycoproteins in the infected cells. The inhibition of fusion and the inhibition of glycosylation caused by 2-deoxyglucose were substantially prevented when mannose was also present during infection. When glycosylation was inhibited, three new bands were found in major glycoprotein region on sodium dodecyl sulfate-polyacrylamide gels. These bands may be precursors to the normal glycoproteins. The correlation between fusion and glycosylation in the presence of 2-deoxyglucose, glucosamine, and mannose suggests that the cells cannot fuse if their glycoproteins have a considerably reduced carbohydrate content.

Full text

PDF
644

Images in this article

646Image
on p.646
648Image
on p.648
650Image
on p.650

Selected References

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

  1. Bratt M. A., Gallaher W. R. Preliminary analysis of the requirements for fusion from within and fusion from without by Newcastle disease virus. Proc Natl Acad Sci U S A. 1969 Oct;64(2):536–543. doi: 10.1073/pnas.64.2.536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bretscher M. S. Major human erythrocyte glycoprotein spans the cell membrane. Nat New Biol. 1971 Jun 23;231(25):229–232. doi: 10.1038/newbio231229a0. [DOI] [PubMed] [Google Scholar]
  3. Courtney R. J., Steiner S. M., Benyesh-Melnick M. Effects of 2-deoxy-D-glucose on herpes simplex virus replication. Virology. 1973 Apr;52(2):447–455. doi: 10.1016/0042-6822(73)90340-1. [DOI] [PubMed] [Google Scholar]
  4. Duda E., Schlesinger M. J. Alterations in Sindbis viral enbelope proteins by treating BHK cells with glucosamine. J Virol. 1975 Feb;15(2):416–419. doi: 10.1128/jvi.15.2.416-419.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gallaher W. R., Levitan D. B., Blough H. A. Effect of 2-deoxy-D-glucose on cell fusion induced by Newcastle disease and herpes simplex viruses. Virology. 1973 Sep;55(1):193–201. doi: 10.1016/s0042-6822(73)81021-9. [DOI] [PubMed] [Google Scholar]
  6. Gandhi S. S., Stanley P., Taylor J. M., White D. O. Inhibition of influenza viral glycoprotein synthesis by sugars. Microbios. 1972 Jan;5(17):41–50. [PubMed] [Google Scholar]
  7. Havell E. A., Vilcek J., Falcoff E., Berman B. Suppression of human interferon production by inhibitors of glycosylation. Virology. 1975 Feb;63(2):475–483. doi: 10.1016/0042-6822(75)90320-7. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Hodes D. S., Schnitzer T. J., Kalica A. R., Camargo E., Chanock R. M. Inhibition of Respiratory syncytial, parainfluenza 3 and measles viruses by 2-deoxy-D-glucose. Virology. 1975 Jan;63(1):201–208. doi: 10.1016/0042-6822(75)90385-2. [DOI] [PubMed] [Google Scholar]
  10. Honess R. W., Roizman B. Proteins specified by herpes simplex virus. XI. Identification and relative molar rates of synthesis of structural and nonstructural herpes virus polypeptides in the infected cell. J Virol. 1973 Dec;12(6):1347–1365. doi: 10.1128/jvi.12.6.1347-1365.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KILBOURNE E. D. Inhibition of influenza virus multiplication with a glucose antimetabolite (2-deoxy-D-glucose). Nature. 1959 Jan 24;183(4656):271–272. doi: 10.1038/183271b0. [DOI] [PubMed] [Google Scholar]
  12. Kaluza G. Effect of impaired glycosylation on the biosynthesis of Semliki forest virus glycoproteins. J Virol. 1975 Sep;16(3):602–612. doi: 10.1128/jvi.16.3.602-612.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kaluza G., Schmidt M. F., Scholtissek C. Effect of 2-deoxy-D-glucose on the multiplication of Semliki Forest virus and the reversal of the block by mannose. Virology. 1973 Jul;54(1):179–189. doi: 10.1016/0042-6822(73)90127-x. [DOI] [PubMed] [Google Scholar]
  14. Kaluza G., Scholtissek C., Rott R. Inhibition of the multiplication of enveloped RNA-viruses by glucosamine and 2-deoxy-D-glucose. J Gen Virol. 1972 Mar;14(3):251–259. doi: 10.1099/0022-1317-14-3-251. [DOI] [PubMed] [Google Scholar]
  15. Keller J. M., Spear P. G., Roizman B. Proteins specified by herpes simplex virus. 3. Viruses differing in their effects on the social behavior of infected cells specify different membrane glycoproteins. Proc Natl Acad Sci U S A. 1970 Apr;65(4):865–871. doi: 10.1073/pnas.65.4.865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Klenk H. D., Scholtissek C., Rott R. Inhibition of glycoprotein biosynthesis of influenza virus by D-glucosamine and 2-deoxy-D-glucose. Virology. 1972 Sep;49(3):723–734. doi: 10.1016/0042-6822(72)90529-6. [DOI] [PubMed] [Google Scholar]
  17. Ludwig H., Becht H., Rott R. Inhibition of herpes virus-induced cell fusion by concanavalin A, antisera, and 2-deoxy-D-glucose. J Virol. 1974 Aug;14(2):307–314. doi: 10.1128/jvi.14.2.307-314.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Person S., Knowles R. W., Read G. S., Warner S. C., Bond V. C. Kinetics of cell fusion induced by a syncytia-producing mutant of herpes simplex virus type I. J Virol. 1975 Jan;17(1):183–190. doi: 10.1128/jvi.17.1.183-190.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Poste G., Allison A. C. Membrane fusion. Biochim Biophys Acta. 1973 Dec 28;300(4):421–465. doi: 10.1016/0304-4157(73)90015-4. [DOI] [PubMed] [Google Scholar]
  20. Russ G., Poláková K. The molecular weight determination of proteins and glycoproteins of RNA enveloped viruses by polyacrylamide gel electrophoresis in SDS. Biochem Biophys Res Commun. 1973 Dec 10;55(3):666–672. doi: 10.1016/0006-291x(73)91196-0. [DOI] [PubMed] [Google Scholar]
  21. Schnitzer T. J., Hodes D. S., Gerin J., Camargo E., Chanock R. M. Effect of 2-deoxy-D-glucose and glucosamine on the growth and functions of respiratory syncytial and parainfluenza 3 viruses. Virology. 1975 Sep;67(1):306–309. doi: 10.1016/0042-6822(75)90431-6. [DOI] [PubMed] [Google Scholar]
  22. Scholtissek C., Rott R., Hau G., Kaluza G. Inhibition of the multiplication of vesicular stomatitis and Newcastle disease virus by 2-deoxy-d-glucose. J Virol. 1974 Jun;13(6):1186–1193. doi: 10.1128/jvi.13.6.1186-1193.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Schwarz R. T., Klenk H. D. Inhibition of glycosylation of the influenza virus hemagglutinin. J Virol. 1974 Nov;14(5):1023–1034. doi: 10.1128/jvi.14.5.1023-1034.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Segrest J. P., Jackson R. L., Andrews E. P., Marchesi V. T. Human erythrocyte membrane glycoprotein: a re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis. Biochem Biophys Res Commun. 1971 Jul 16;44(2):390–395. doi: 10.1016/0006-291x(71)90612-7. [DOI] [PubMed] [Google Scholar]
  25. Studier F. W. Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J Mol Biol. 1973 Sep 15;79(2):237–248. doi: 10.1016/0022-2836(73)90003-x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES