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. 1979 Mar;29(3):997–1005. doi: 10.1128/jvi.29.3.997-1005.1979

Carbohydrate Components of Influenza C Virions

Kiyoto Nakamura 1, George Herrler 2, Thomas Petri 2, Herbert Meier-Ewert 2, Richard W Compans 1
PMCID: PMC353260  PMID: 448803

Abstract

The carbohydrate components of influenza C virions grown in chicken kidney (CK) cells were analyzed by gel filtration following exhaustive digestion with Pronase. The [3H]glucosamine-labeled glycopeptides were larger and more heterogeneous than those of influenza A/WSN virions; three major size classes (G1, G2, and G3) were resolved. Treatment with Vibrio cholerae neuraminidase caused a decrease in size of G1 and G2, along with release of about 16% of the 3H label. The released sugar components were identified as N-acetylneuraminic acid by thin-layer chromatography. Peak G3 was highly labeled with [3H]mannose, whereas G1 and G2 contained lower levels of mannose. The three major viral glycoproteins gp88, gp65, and gp30 were isolated from sodium dodecyl sulfate-polyacrylamide gels, and their glycopeptide components were analyzed after Pronase digestion. The three size classes of glycopeptides were obtained from any of the three glycoproteins; however, the relative amounts of the three components varied among the glycoproteins. Host cell-derived components, which appear to be mucopolysaccharides and glycoproteins, were found associated with influenza C virions grown in CK cells. These components contained glycopeptides that were mainly of sizes similar to peak G2 from influenza C virions. Previous studies have shown that influenza A/WSN virus grown in several cell types contained only two size classes of glycopeptides. Two size classes comparable to peaks G2 and G3 from influenza C virions were also observed in influenza A/WSN grown in CK cells. Thus the large G1 glycopeptides appear to be characteristic of influenza C virions.

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Selected References

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  1. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  2. Burke D. J., Keegstra K. Purification and composition of the proteins from Sindbis virus grown in chick and BHK cells. J Virol. 1976 Dec;20(3):676–686. doi: 10.1128/jvi.20.3.676-686.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Choppin P. W. Replication of influenza virus in a continuous cell line: high yield of infective virus from cells inoculated at high multiplicity. Virology. 1969 Sep;39(1):130–134. doi: 10.1016/0042-6822(69)90354-7. [DOI] [PubMed] [Google Scholar]
  4. Collins J. K., Knight C. A. Purification of the influenza hemagglutinin glycoprotein and characterization of its carbohydrate components. J Virol. 1978 May;26(2):457–467. doi: 10.1128/jvi.26.2.457-467.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Compans R. W., Bishop D. H., Meier-Ewert H. Structural components of influenza C virions. J Virol. 1977 Feb;21(2):658–665. doi: 10.1128/jvi.21.2.658-665.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Compans R. W. Hemagglutination-inhibition: rapid assay for neuraminic acid-containing viruses. J Virol. 1974 Nov;14(5):1307–1309. doi: 10.1128/jvi.14.5.1307-1309.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Compans R. W., Pinter A. Incorporation of sulfate into influenza virus glycoproteins. Virology. 1975 Jul;66(1):151–160. doi: 10.1016/0042-6822(75)90186-5. [DOI] [PubMed] [Google Scholar]
  8. Cox N. J., Kendal A. P. Presence of a segmented single-stranded RNA genome in influenza C virus. Virology. 1976 Oct 1;74(1):239–241. doi: 10.1016/0042-6822(76)90147-1. [DOI] [PubMed] [Google Scholar]
  9. Etchison J. R., Robertson J. S., Summers D. F. Partial structural analysis of the oligosaccharide moieties of the vesicular stomatitis virus glycoprotein by sequential chemical and enzymatic degradation. Virology. 1977 May 15;78(2):375–392. doi: 10.1016/0042-6822(77)90115-5. [DOI] [PubMed] [Google Scholar]
  10. HIRST G. K. The relationship of the receptors of a new strain of virus to those of the mumps-NDV-influenza group. J Exp Med. 1950 Feb;91(2):177–184. doi: 10.1084/jem.91.2.177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Johnson I., Clamp J. R. The oligosaccharide units of a human type L immunoglobulin M (Macroglobulin). Biochem J. 1971 Aug;123(5):739–745. doi: 10.1042/bj1230739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kendal A. P. A comparison of "influenza C" with prototype myxoviruses: receptor-destroycing activity (neuraminidase) and structural polypeptides. Virology. 1975 May;65(1):87–99. doi: 10.1016/0042-6822(75)90009-4. [DOI] [PubMed] [Google Scholar]
  13. Kornfeld R., Kornfeld S. Comparative aspects of glycoprotein structure. Annu Rev Biochem. 1976;45:217–237. doi: 10.1146/annurev.bi.45.070176.001245. [DOI] [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Mattila K., Luukkonen A., Renkonen O. Protein-bound oligosaccharides of Semliki Forest virus. Biochim Biophys Acta. 1976 Feb 6;419(3):435–444. doi: 10.1016/0005-2736(76)90257-1. [DOI] [PubMed] [Google Scholar]
  16. Nakamura K., Compans R. W. Glycopeptide components of influenza viral glycoproteins. Virology. 1978 May 15;86(2):432–442. doi: 10.1016/0042-6822(78)90083-1. [DOI] [PubMed] [Google Scholar]
  17. Nakamura K., Compans R. W. The cellular site of sulfation of influenza viral glycoproteins. Virology. 1977 Jun 15;79(2):381–392. doi: 10.1016/0042-6822(77)90365-8. [DOI] [PubMed] [Google Scholar]
  18. Nerome K., Ishida M., Nakayama M. Absence of neuraminidase from influenza C virus. Arch Virol. 1976;50(3):241–244. doi: 10.1007/BF01320578. [DOI] [PubMed] [Google Scholar]
  19. O'Callaghan R. J., Loughlin M., Labat D. D., Howe C. Properties of influenza C virus grown in cell culture. J Virol. 1977 Dec;24(3):875–882. doi: 10.1128/jvi.24.3.875-882.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ritchey M. B., Palese P., Kilbourne E. D. RNAs of influenza A, B, and C viruses. J Virol. 1976 May;18(2):738–744. doi: 10.1128/jvi.18.2.738-744.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Schwarz R. T., Schmidt M. F., Anwer U., Klenk H. D. Carbohydrates of influenza virus. I. Glycopeptides derived from viral glycoproteins after labeling with radioactive sugars. J Virol. 1977 Aug;23(2):217–226. doi: 10.1128/jvi.23.2.217-226.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sefton B. M., Keegstra K. Glycoproteins of Sindbis virus: priliminary characterization of the oligosaccharides. J Virol. 1974 Sep;14(3):522–530. doi: 10.1128/jvi.14.3.522-530.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]

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