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. 1975 Sep;16(3):613–620. doi: 10.1128/jvi.16.3.613-620.1975

Sindbis virus glycoproteins: effect of the host cell on the oligosaccharides.

K Keegstra, B Sefton, D Burke
PMCID: PMC354709  PMID: 1171992

Abstract

Sindbis virus was grown in four different host cells and the carbohydrate portions of the glycoproteins were analyzed. Sindbis virus grown in BHK-21 cells has more sialic acid and galactose than Sindbis virus grown in chicken embryo cells. In other respects the carbohydrates from virus grown in these two hosts are very similar. Sindbis virus grown either in chick cells transformed by Rous sarcoma virus or in BHK cells transformed by polyoma virus was also examined. In comparisons of virus from normal and transformed cells, differences in the amount of sialic acid were observed; but otherwise the carbohydrate structures appeared basically similar. The growth conditions used for the host cell also affected the degree of completion of the carbohydrate chains of the viral glycoproteins.

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Selected References

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

  1. Buck C. A., Glick M. C., Warren L. A comparative study of glycoproteins from the surface of control and Rous sarcoma virus transformed hamster cells. Biochemistry. 1970 Nov 10;9(23):4567–4576. doi: 10.1021/bi00825a016. [DOI] [PubMed] [Google Scholar]
  2. Buck C. A., Glick M. C., Warren L. Effect of growth on the glycoproteins from the surface of control and Rous sarcoma virus transformed hamster cells. Biochemistry. 1971 May 25;10(11):2176–2180. doi: 10.1021/bi00787a034. [DOI] [PubMed] [Google Scholar]
  3. Burge B. W., Huang A. S. Comparison of membrane protein glycopeptides of Sindbis virus and vesicular stomatitis virus. J Virol. 1970 Aug;6(2):176–182. doi: 10.1128/jvi.6.2.176-182.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burge B. W., Strauss J. H., Jr Glycopeptides of the membrane glycoprotein of Sindbis virus. J Mol Biol. 1970 Feb 14;47(3):449–466. doi: 10.1016/0022-2836(70)90314-1. [DOI] [PubMed] [Google Scholar]
  5. Compans R. W. Location of the glycoprotein in the membrane of Sindbis virus. Nat New Biol. 1971 Jan 27;229(4):114–116. doi: 10.1038/newbio229114a0. [DOI] [PubMed] [Google Scholar]
  6. David A. E. Lipid composition of Sindbis virus. Virology. 1971 Dec;46(3):711–720. doi: 10.1016/0042-6822(71)90073-0. [DOI] [PubMed] [Google Scholar]
  7. Etchison J. R., Holland J. J. Carbohydrate composition of the membrane glycoprotein of vesicular stomatitis virus grown in four mammalian cell lines. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4011–4014. doi: 10.1073/pnas.71.10.4011. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Grimes W. J., Burge B. W. Modification of Sindbis virus glycoprotein by host-specified glycosyl transferases. J Virol. 1971 Mar;7(3):309–313. doi: 10.1128/jvi.7.3.309-313.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Grimes W. J. Glycosyltransferase and sialic acid levels of normal and transformed cells. Biochemistry. 1973 Feb 27;12(5):990–996. doi: 10.1021/bi00729a031. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Lai M. M., Duesberg P. H. Differences between the envelope glycoproteins and glycopeptides of avian tumor viruses released from transformed and from nontransformed cells. Virology. 1972 Nov;50(2):359–372. doi: 10.1016/0042-6822(72)90387-x. [DOI] [PubMed] [Google Scholar]
  13. Moyer S. A., Summers D. F. Vesicular stomatitis virus envelope glycoprotein alterations induced by host cell transformation. Cell. 1974 May;2(1):63–70. doi: 10.1016/0092-8674(74)90009-9. [DOI] [PubMed] [Google Scholar]
  14. SPIRO R. G. THE CARBOHYDRATE UNITS OF THYROGLOBULIN. J Biol Chem. 1965 Apr;240:1603–1610. [PubMed] [Google Scholar]
  15. Schlesinger M. J., Schlesinger S., Burge B. W. Identification of a second glycoprotein in Sindbis virus. Virology. 1972 Feb;47(2):539–541. doi: 10.1016/0042-6822(72)90298-x. [DOI] [PubMed] [Google Scholar]
  16. Schloemer R. H., Wagner R. R. Mosquito cells infected with vesicular stomatitis virus yield unsialylated virions of low infectivity. J Virol. 1975 Apr;15(4):1029–1032. doi: 10.1128/jvi.15.4.1029-1032.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Strauss J. H., Jr, Burge B. W., Darnell J. E. Carbohydrate content of the membrane protein of Sindbis virus. J Mol Biol. 1970 Feb 14;47(3):437–448. doi: 10.1016/0022-2836(70)90313-x. [DOI] [PubMed] [Google Scholar]
  19. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]
  20. Warren L., Fuhrer J. P., Buck C. A. Surface glycoproteins of cells before and after transformation by oncogenic viruses. Fed Proc. 1973 Jan;32(1):80–85. [PubMed] [Google Scholar]
  21. Warren L., Fuhrer J. P., Buck C. A. Surface glycoproteins of normal and transformed cells: a difference determined by sialic acid and a growth-dependent sialyl transferase. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1838–1842. doi: 10.1073/pnas.69.7.1838. [DOI] [PMC free article] [PubMed] [Google Scholar]

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