Nature Publishing Group, publisher of Nature, and other science journals and reference works
Nature
my account e-alerts subscribe register
   
Saturday 28 November 2009
Journal Home
Current Issue
AOP
Archive
Download PDF
References
Export citation
Export references
Send to a friend
More articles like this

Letters to Nature
Nature 274, 487 - 490 (03 August 1978); doi:10.1038/274487a0

Glycosylation is not necessary for membrane insertion and cleavage of Semliki Forest virus membrane proteins

HENRIK GAROFF* & RALPH T. SCHWARZ

*European Molecular Biology Laboratory, Postfach 10 2209, D6900, Heidelberg, FRG
Institut für Virologie, Justus Liebig University, D6300 Giessen, FRG

RECENT translation studies in vitro 1,2,33 have shown that the synthesis of membrane ectoproteins, like the glycoproteins of vesicular stomatitis virus (VSV) and Semliki Forest virus (SFV), (budding, enveloped viruses), occurs simultaneously with their insertion into membranes, their glycosylation and their proteolytic processing. We have studied the synthesis of SFV membrane proteins in infected cells treated with tunicamycin, which prevents glycosylation of proteins by inhibiting the formation of the lipid bound sugar intermediates needed for protein glycosylation3−5. We have found that glycosylation is not a prerequisite for correct insertion and cleavage of such membrane ectoproteins.

------------------

References
1. Katz, F. N., Rothman, J. E., Lingappa, V. R., Blobel, G. & Lodish, H. F. Proc. natn. Acad. Sci. U.S.A. 74, 3278–3282 (1977).
2. Rothman, E. J. & Lodish, H. F. Nature 269, 775–780 (1977).
3. Takatsuki, A., Kohno, K. & Tamura, G. Agric. biol. Chem. 39, 2089–2091 (1975).
4. Tkacz, J. S. & Lampen, J. O. Biochem. biophys. Res. Commun. 65, 248–257 (1975).
5. Lehle, L. & Tanner, W. B. FEBS Lett. 71, 167–170 (1976).
6. Lachmi, E. & Kääriäinen, L. Proc. natn. Acad. Sci. U.S.A. 73, 1936–1940 (1976).
7. Glanville, N., Ranki, M., Morser, J., Kääriäinen, L. & Smith, A. E. Proc. natn. Acad. Sci. U.S.A. 73, 3059–3963 (1976).
8. Clegg, J. C. S. Nature 254, 454–455 (1975).
9. Clegg, J. C. S. & Kennedy, S. I. T. J. molec. Biol. 97, 401–411 (1975).
10. Simons, K. & Kääriäinen, L. Biochem. biophys. Res. Commun. 38, 981–988 (1970).
11. Garoff, H., Simons, K. & Renkonen, O. Virology 61, 493–504 (1974).
12. Simons, K., Keränen, S. & Kääriäinen, L. FEBS Lett. 29, 87–91 (1973).
13. Sefton, B. M. Cell 10, 659–668 (1977).
14. Mattila, K., Luukkonen, A. & Renkonen, O. Biochim. biophys. Acta 419, 435–444 (1976).
15. Caliguiri, L. A. & Mosser, A. G. Virology 46, 375–386 (1971).
16. Schwarz, R. T., Rohrschneider, J. M. & Schmidt, M. F. G. J. Virol. 19, 782–791 (1976).
17. Leavitt, R., Schlesinger, S. & Kornfeld, S. J. Virol. 21, 375–385 (1977).
18. Kaluza, G. J. Virol. 16, 602–612 (1975).
19. Schmidt, M. F. G., Schwarz, R. T. & Ludwig, H. J. Virol. 18, 819–823 (1976).
20. Wirth, D. F., Katz, F., Small, B. & Lodish, H. F. Cell 10, 253–263 (1977).
21. Richardson, C. D. & Vance, D. E. J. biol. Chem. 251, 5544–5550 (1976).
22. Acheson, N. H. & Tamm, I. Virology 32, 128–143 (1967).
23. Garoff, H. & Simons, K. Proc. natn. Acad. Sci. U.S.A. 71, 3988–3992 (1974).
24. Hickman, S., Kulczycki, A., Jr, Lynch, R. G. & Kornfeld, S. J. biol. Chem. 252, 4402–4408 (1977).
25. Leavitt, R., Schlesinger, S. & Kornfeld, S. J. biol. Chem. 252, 9018–9023 (1977).
26. Tabas, I., Schlesinger, S. & Kornfeld, S. J. biol. Chem. 253, 716–722 (1978).
27. Gibson, R., Leavitt, R., Kornfeld, S. & Schlesinger, S. Cell 13, 671–679 (1978).
28. Kääriäinen, L., Simons, K. & von Bonsdorff, C. H. Ann. med. exp. Biol. Fenn. 47, 235–248 (1969).
29. Blobel, G. & Dobberstein, B. J. Cell Biol. 67, 835–862 (1975).
30. Bonner, W. M. & Laskey, R. A. Eur. J. Biochem. 46, 83–88 (1974).
31. Neville, D. M., Jr J. biol. Chem. 246, 6328–6334 (1971).
32. Sabatini, D. D. & Blobel, G. J. Cell Biol. 45, 146–157 (1970).
33. Garoff, H., Simons, K. & Dobberstein, B. J. molec. Biol. (in the press).
34. Garoff, H. & So macrderlund, H. J. molec. Biol. (in the press).



© 1978 Nature Publishing Group
Privacy Policy