1887

Abstract

SUMMARY

Glucosamine inhibited the formation of infectious fowl plague, Sindbis, and Semliki Forest virus but had little or no effect on the multiplication of vesicular stomatitis, Newcastle disease, and polio virus. 2-deoxy--glucose had a somewhat stronger effect than glucosamine. Only the production of virus glycoproteins seemed to be affected. Almost normal amounts of virus RNA and RNA polymerase were synthesized, and RNP-antigen activities reached control levels. After infection with fowl plague virus the nuclei and cytoplasm of cells incubated with glucosamine showed brilliant staining with fluorescent antibodies against RNP-antigen, whereas haemagglutinin-specific fluorescence was visible weakly in the cytoplasm. The virus-induced alterations of the cell surface, as measured by the agglutinability with Concanavalin A, were abolished by glucosamine.

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1972-03-01
2024-12-07
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References

  1. Becht H. 1968; Properties of erythrocytes stabilized with sulfosalicylic acid and their use in an indirect haemagglutination test with influenza virus RNP-antigen. Journal of Immunology 101:18
    [Google Scholar]
  2. Becht H., Rott R., Klenk H.D. 1972; Effect of Concanavalin A on cells infected with enveloped RNA viruses. Journal of General Virology 14:1
    [Google Scholar]
  3. Bekesi J. G., Winzler R. J. 1969; The effect of d-glucosamine on the adenine and uridine nucleotides of sarcoma 180 ascites tumor cells. Journal of Biological Chemistry 244:5663
    [Google Scholar]
  4. Breitenfeld P. M., Schäfer W. 1957; The formation of fowl plague virus antigens in infected cells, as studied with fluorescent antibodies. Virology 4:328
    [Google Scholar]
  5. Burge B. W., Huang A. S. 1970; Comparison of membrane protein glycopeptides of Sindbis virus and vesicular stomatitis virus. Journal of Virology 6:176
    [Google Scholar]
  6. Burge B. W., Strauss J. H. Jr 1970; Glycopeptides of the membrane glycoprotein of Sindbis virus. Journal of Molecular Biology 47:449
    [Google Scholar]
  7. Compans R. W., Klenk H.-D., Caliguiri L. A., Chopin P. W. 1970; Influenza virus proteins. I. Analysis of polypeptides of the virion and identification of spike glycoproteins. Virology 42:880
    [Google Scholar]
  8. Davenport F. M., Rott R., Schäfer W. 1960; Physical and biological properties of influenza virus components obtained after ether treatment. Journal of Experimental Medicine 112:765
    [Google Scholar]
  9. Drzeniek R. 1967; Differences in splitting capacity of virus and V. cholerae neuraminidase on sialic acid substrates. Biochemical and Biophysical Research Communications 26:631
    [Google Scholar]
  10. Eagle H., Habel K. 1956; The nutritional requirements for the propagation of poliomyelitis virus by the HeLa cell. Journal of Experimental Medicine 104:271
    [Google Scholar]
  11. Grimes W. J., Burge B. W. 1971; Modification of Sindbis virus glycoprotein by host-specified glycosyl transferases. Journal of Virology 7:309
    [Google Scholar]
  12. Keppler D. O. R., Rudigier J. F. M., Bischoff E., Decker K. F. A. 1970; The trapping of uridine phosphates by d-galactosamine, d-glucosamine, and 2-deoxy-d-galactose. A study on the mechanism of galactosamine hepatitis. European Journal of Biochemistry 17:246
    [Google Scholar]
  13. Klenk H.-D., Caliguiri L. A., Choppin P. W. 1970; The proteins of the parainfluenza virus SV5. II. The carbohydrate content and glycoproteins of the virion. Virology 42:473
    [Google Scholar]
  14. Klenk H.-D., Choppin P. W. 1970; Glycosphingolipids of plasma membranes of cultured cells and an enveloped virus (SV5) grown in these cells. Proceedings of the National Academy of Sciences of the United States of America 66:57
    [Google Scholar]
  15. Mcsharry J. J., Wagner R. R. 1971; Carbohydrate composition of vesicular stomatitis virus. Journal of Virology 7:412
    [Google Scholar]
  16. Molnar J., Robinson G. B., Winzler R. J. 1964; The biosynthesis of glycoproteins. III. Glucosamine intermediates in plasma glycoprotein synthesis in livers of puromycin-treated rats. Journal of Biological Chemistry 239:3157
    [Google Scholar]
  17. Rott R., Scholtissek C. 1968; Biochemical studies on influenza virus multiplication at reduced temperatures. Journal of General Virology 3:239
    [Google Scholar]
  18. Scholtissek C. 1971; Detection of an unstable RNA in chick fibroblasts after reduction of the UTP-pool by glucosamine. European Journal of Biochemistry (in the Press)
    [Google Scholar]
  19. Scholtissek C., Rott R. 1969; Ribonucleic acid nucleotidyl transferase induced in chick fibroblasts after infection with an influenza virus. Journal of General Virology 4:125
    [Google Scholar]
  20. Schultze I. T. 1970; The structure of the influenza virus. I. The polypeptides of the virion. Virology 42:890
    [Google Scholar]
  21. Strauss J. H. JR., Burge B. W., Darnell J. E. 1970; Carbohydrate content of the membrane protein of Sindbis virus. Journal of Molecular Biology 47:437
    [Google Scholar]
  22. Zimmermann T., Schäfer W. 1960; Effect of p-fluorophenyl-alanine on Fowl plague virus multiplication. Virology 11:676
    [Google Scholar]
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