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Separation and sugar component analysis of the oligosaccharides in the surface glycoproteins of Newcastle Disease Virus

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Summary

The precursor glycoproteins HN0 and F0 in the surface spikes of Newcastle Disease Virus strain Ulster as produced by MDBK cells, were found to contain 10.4 and 11.9 weight per cent, respectively, of the sugars typical forN-glycosidically linked glycoprotein glycans. A molar ratio ofD-mannose:D-galactose:L-fucose:N-acetyl-D-glucosamine approaching 1.0:1.1:0.5:1.0 was found for HN0, and of 1.0:0.7:0.3:0.6 for F0.

By a sequence of degradation (with pronase, with endo-β-N-acetylglucosaminidase H [endo H], and by hydrazinolysis) and separation procedures (Concanavalin A-affinity and Biogel P-4 chromatography), the radiolabelled carbohydrate moieties of NDV HN0 and F0 (as oligosaccharitols) were separated into (at least) ten and eight fractions, respectively. Separatein vivo labelling with tritiated derivatives of the four sugars showed that both glycoproteins contain oligosaccharides of the oligomannosidic (“high mannose”), of theN-acetyllactosaminic (“complex”), as well as of the “mixed” type. The majority of the oligosaccharides in F0, but not of those in HN0, was found to be endo H-sensitive.

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References

  1. Carlson, D. M.: Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins. J. Biol. Chem.243, 616–626 (1968).

    Google Scholar 

  2. Choppin, P. W., Scheid, A.: The role of viral glycoproteins in adsorption, penetration, and pathogenicity of viruses. Rev. Infect. Dis.2, 40–61 (1980).

    Google Scholar 

  3. Choppin, P. W., Richardson, C. D., Merz, D. C., Hall, W. W., Scheid, A.: The functions and inhibition of the membrane glycoproteins of Paramyxoviruses and Myxoviruses and the role of the Measles virus M protein in subacute Sclerosing Panencephalitis. J. Infect. Dis.143, 352–363 (1981).

    Google Scholar 

  4. Downs, F., Pigman, W.: Determination of hexosamines and hexosaminitols using the amino acid analyzer. Meth. Carbohydr. Chem.7, 244–248 (1976).

    Google Scholar 

  5. Garten, W., Berk, W., Nagai, Y., Rott, R., Klenk, H.-D.: Mutational changes of the protease susceptibility of glycoprotein F of Newcastle Disease Virus: Effects on pathogenicity. J. gen. Virol.50, 135–147 (1980).

    Google Scholar 

  6. Garten, W., Kohama, T., Klenk, H.-D.: Proteolytic activation of the haemagglutinin-neuraminidase of Newcastle Disease Virus involves loss of a glycopeptide. J. gen. Virol.51, 207–211 (1980).

    Google Scholar 

  7. Geyer, R., Geyer, H., Kühnhardt, S., Mink, W., Stirm, S.: Capillary gas chromatography of methylhexitol acetates obtained upon methylation ofN-glycosidically linked glycoprotein oligosaccharides. Anal. Biochem.121, 263–274 (1982).

    Google Scholar 

  8. Hounsel, E. F., Wood, E., Feizi, T., Fukuda, M., Powell, M. E., Hakomori, S.: Structural analysis of hexa- to octa-saccharide fractions isolated from sheep gastric-glycoproteins having blood-group I and i activities. Carbohydr. Res.90, 283–307 (1981).

    Google Scholar 

  9. Klenk, H.-D., Compans, R. W., Choppin, P. W.: An electron microscopic study of the presence or absence of neuraminic acid in enveloped viruses. Virology42, 1158–1162 (1970).

    Google Scholar 

  10. Klenk, H.-D., Rott, R.: Cotranslational and posttranslational processing of viral glycoproteins. Curr. Top. Microbiol. Immunol.90, 19–48 (1980).

    Google Scholar 

  11. Kobata, A.: Use of endo- and exoglycosidases for structural studies of glycoconjugates. Anal. Biochem.100, 1–14 (1979).

    Google Scholar 

  12. Kohama, T., Shimizu, K., Ishida, N.: Carbohydrate composition of the envelope glycoproteins of Sendai Virus. Virology90, 226–234 (1978).

    Google Scholar 

  13. Kohama, T., Garten, W., Klenk, H.-D.: Changes in conformation and charge paralleling proteolytic activation of Newcastle Disease virus glycoproteins. Virology111, 364–376 (1981).

    Google Scholar 

  14. Krusius, T., Finne, J., Rauvala, H.: The structural basis of the different affinities of two types of acidicN-glycosidic glycopeptides for concanavalin A-Sepharose. FEBS Lett.71, 117–120 (1976).

    Google Scholar 

  15. Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature227, 680–685 (1970).

    Google Scholar 

  16. Lennarz, W. J.: The biochemistry of glycoproteins and proteoglycans, 1st ed. New York-London: Plenum Press 1980.

    Google Scholar 

  17. Matthews, R. E. F.: Classification and nomenclature of viruses. In: Third Report of the International Committee on Taxonomy of Viruses, 216. Basel: S. Karger 1979.

    Google Scholar 

  18. Mizuochi, T., Fujii, J., Kurachi, K., Kobata, A.: Structural studies of the carbohydrate moiety of human antithrombin III. Arch. Biochem. Biophys.203, 458–465 (1980).

    Google Scholar 

  19. Montreuil, J.: Primary structure of glycoprotein glycans. Basis for the molecular biology of glycoproteins. Adv. Carbohydr. Chem. Biochem.37, 157–223 (1980).

    Google Scholar 

  20. Nagai, Y., Klenk, H.-D., Rott, R.: Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle Disease Virus. Virology72, 494–508 (1976).

    Google Scholar 

  21. Nagai, Y., Klenk, H.-D.: Activation of precursors to both glycoproteins of Newcastle Disease Virus by proteolytic cleavage. Virology77, 125–134 (1977).

    Google Scholar 

  22. Portner, A.: The HN glycoprotein of Sendai virus: Analysis of site(s) involved in haemagglutinating and neuraminidase activities. Virology115, 375–384 (1981).

    Google Scholar 

  23. Prehm, P., Scheid, A., Choppin, P. W.: The carbohydrate structure of the glycoproteins of the Paramyxovirus SV 5 grown in bovine kidney cells. J. Biol. Chem.254, 9669–9677 (1979).

    Google Scholar 

  24. Sawardeker, J. S., Slonker, J. H., Jeanes, A.: Quantitative determination of monosaccharides as their alditol acetates by gas liquid chromatography. Anal. Chem.12, 1602–1604 (1965).

    Google Scholar 

  25. Schwarz, R. T., Klenk, H.-D.: Inhibition of glycosylation of the influenza virus hemagglutinin. J. Virol.14, 1023–1034 (1974).

    Google Scholar 

  26. Stellner, K., Saito, H., Hakomori, S.: Determination of aminosugar linkages in glycolipids by methylation. Aminosugar linkages of ceramide pentasaccharides of rabbit erythrocytes and of Forssman antigen. Arch. Biochem. Biophys.155, 464–472 (1973).

    Google Scholar 

  27. Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y., Kobata, A.: Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J. Biol. Chem.250, 8569–8575 (1975).

    Google Scholar 

  28. Trevelyan, W. E., Procter, D. P., Harrison, J. S.: Detection of sugars on paper chromatograms. Nature166, 444–445 (1950).

    Google Scholar 

  29. Yoshima, H., Nakanishi, M., Okada, Y., Kobata, A.: Carbohydrate structures of HVJ (Sendai virus) glycoproteins. J. Biol. Chem.256, 5355–5361 (1981).

    Google Scholar 

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Dedicated to Professor Eckhart Buddecke on the occasion of his 60th birthday.

With 6 Figures

In partial fulfilment of the requirements for the degree of Dr. rer. nat. at Giessen University.

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Diabaté, S., Geyer, R. & Stirm, S. Separation and sugar component analysis of the oligosaccharides in the surface glycoproteins of Newcastle Disease Virus. Archives of Virology 76, 321–334 (1983). https://doi.org/10.1007/BF01311199

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  • DOI: https://doi.org/10.1007/BF01311199

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