1887

Abstract

Human fibroblast cells infected with varicella-zoster virus (VZV) showed a slight increase in lipoprotein synthesis, with the production of two major viral lipoproteins, as detected by radioimmunoprecipitation (RIP). Three bands of 73000, 90000 and 97000 were identified as forms of the VZV gpl glycoprotein. All three incorporated both palmitic and myristic acid, and were shown by thin-layer chromatography to contain myristic, palmitic and stearic acids. A very strong band corresponding to 7000 , which may represent the product of VZV gene 49, was detected after RIP and in VZV-infected cells, and was shown to contain almost entirely myristic acid. Several minor bands were also detected. The possible functions of the lipoproteins are discussed.

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1990-02-01
2024-04-19
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References

  1. Abodeely R. A., Palmer E., Lawson L. A., Randall C. 1971; The proteins of enveloped and de-enveloped equine abortion (herpes) virus and the separated envelope. Virology 44:146–152
    [Google Scholar]
  2. Ben-Porat T., Kaplan A. S. 1971; Phospholipid metabolism of herpesvirus-infected and uninfected rabbit kidney cells. Virology 45:252–264
    [Google Scholar]
  3. Bonner W. M., Laskey R. A. 1974; A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels. European Journal of Biochemistry 46:83–88
    [Google Scholar]
  4. Buss J. E., Sefton B. M. 1985; Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog. Journal of Virology 53:7–12
    [Google Scholar]
  5. Buss J. E., Kamps M. K., Sefton B. M. 1985; Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein. Molecular and Cellular Biology 4:2697–2704
    [Google Scholar]
  6. Carr S. A., Biemann M., Shoji S., Parmalee D. C., Titani K. 1982; N-tetradecanoyl is the NH2-terminal blocking group of cyclic AMP-dependent protein kinase from bovine cardiac muscle. Proceedings of the National Academy of Sciences, U.S.A 79:6128–6131
    [Google Scholar]
  7. Chambers P., Samson A. C. R. 1982; Non-structural proteins in Newcastle disease virus-infected cells. Journal of General Virology 58:1–12
    [Google Scholar]
  8. Chow M., Newman J. F. E., Filman D., Hogle J. M., Rowlands D. J., Brown F. 1987; Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature; London: 327482–486
    [Google Scholar]
  9. Compton T., Courtney R. J. 1985; Effects of herpes simplex virus type 1 on cellular pools of oligosaccharide-lipid. Virology 147:1–8
    [Google Scholar]
  10. Cross F. R., Garber E. A., Pellman D., Hanafusa H. 1984; A short sequence in the p60src N terminus is required for p60srcmyristylation and membrane association and for cell transformation. Molecular and Cellular Biology 4:1834–1842
    [Google Scholar]
  11. Davison A. J., Scott J. E. 1986; The complete DNA sequence of varicella-zoster virus. Journal of General Virology 67:1759–1816
    [Google Scholar]
  12. Dunphy W. G., Fries E., Urbani L. J., Rothman J. E. 1981; Early and late functions associated with the Golgi apparatus reside in distinct compartments. Proceedings of the National Academy of Sciences, U.S.A 78:7453–7457
    [Google Scholar]
  13. Heath R. B. 1987; Varicella-zoster. In Principles and Practice of Clinical Virology pp. 51–73 Zuckerman A. J., Banatvala J. E., Pattison J. R. Edited by Chichester: John Wiley;
    [Google Scholar]
  14. Hedo J. A., Collier E., Watkinson A. 1987; Myristyl and palmityl acylation of the insulin receptor. Journal of Biological Chemistry 262:954–957
    [Google Scholar]
  15. Jerkofsky M., De Siervo A. J. 1986; Differentiation of strains of varicella-zoster virus by changes in neutral lipid metabolism in infected cells. Journal of Virology 57:809–815
    [Google Scholar]
  16. Johnson D. C., Spear P. G. 1983; O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Cell 32:987–997
    [Google Scholar]
  17. Kamps M. K., Buss J. E., Sefton B. M. 1985; Mutation of the NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proceedings of the National Academy of Sciences, U.S.A 82:4626–4628
    [Google Scholar]
  18. Kaufman J. F., Krangel M. S., Strominger J. C. 1984; Cysteines in the transmembrane region of major histocompatibility complex antigens are fatty acylated via thioester bonds. Journal of Biological Chemistry 259:7230–7238
    [Google Scholar]
  19. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
  20. Mcgeoch D. J., Dalrymple M. A., Davison A. J., Dolan A., Frame M. C., Mcnab D., Perry L. J., Scott J. E., Taylor P. 1988; The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. Journal of General Virology 69:1531–1574
    [Google Scholar]
  21. Maclean C. A., Clark B., Mcgeoch D. J. 1989; Gene UL11 of herpes simplex virus type 1 encodes a virion protein which is myristylated. Journal of General Virology 70:3147–3157
    [Google Scholar]
  22. Magee A. I., Courtneidge S. A. 1985; Two classes of fatty acylated proteins exist in eukaryotic cells. EMBO Journal 4:1137–1144
    [Google Scholar]
  23. Magee A. I., Koyama A. H., Malfer C., Wen D., Schlesinger M. J. 1984; Release of fatty acids from virus glycoproteins by hydroxylamine. Biochimica et biophysica acta 798:156–166
    [Google Scholar]
  24. Marinetti G. V., Cattieu K. 1982; Tightly (covalently) bound fatty acids in cell membrane proteins. Biochimica et biophysica acta 685:109–116
    [Google Scholar]
  25. Montalvo E. A., Parmley R. T., Grose C. 1985; Structural analysis of the varicella-zoster virus gp98-gp62 complex: posttranslational addition of AMinked and O-linked oligosaccharide moieties. Journal of Virology 53:761–770
    [Google Scholar]
  26. Okuno T., Yamanishi K., Shiraki K., Takahashi M. 1983; Synthesis and processing of glycoproteins of varicella-zoster virus (VZV) as studied with monoclonal antibodies to VZV antigens. Virology 129:357–368
    [Google Scholar]
  27. Olson E. N., Spizz G. 1986; Fatty acylation of cellular proteins. Journal of Biological Chemistry 261:2458–2466
    [Google Scholar]
  28. Olson E. N., Towler D. A., Glaser L. 1985; Specificity of fatty acid acylation of cellular proteins. Journal of Biological Chemistry 260:3784–3790
    [Google Scholar]
  29. Paul A. V., Schultz A., Pincus S. E., Oroszlan S., Wimmer E. 1987; Capsid protein VP4 of poliovirus is N-myristoylated. Proceedings of the National Academy of Sciences, U.S.A 84:7827–7832
    [Google Scholar]
  30. Pellman D., Garber E. A., Cross F. R., Hanafusa H. 1985; An N-terminal peptide from p60src can direct myristylation and plasma membrane localization when fused to heterologous proteins. Nature; London: 314374–377
    [Google Scholar]
  31. Perdue M. L., Kemp M. C., Randall C. C., O’Callaghan D. J. 1974; Studies of the molecular anatomy of the L-M cell strain of equine herpes virus type 1: proteins of the nucleocapsid and intact virion. Virology 59:201–216
    [Google Scholar]
  32. Rugolo M., Baldassari B., Landini M. P. 1986; Changes in membrane permeability in cells infected by human cytomegalovirus. Archives of Virology 89:203–212
    [Google Scholar]
  33. Schmidt M., Muller H., Schmidt M. F. G., Rott R. 1989; Myristoylation of budgerigar fledgling disease virus capsid protein VP2. Journal of Virology 63:429–431
    [Google Scholar]
  34. Schmidt M. F. G. 1983; Fatty acid binding: a new kind of posttranslational modification of membrane proteins. Current Topics of Microbiology and Immunology 102:101–124
    [Google Scholar]
  35. Schmidt M. F. G. 1984; The transfer of myristic and other fatty acids on lipid and other viral protein acceptors in cultured cells infected with Semliki Forest and influenza viruses. EMBO Journal 3:2295–2300
    [Google Scholar]
  36. Schmidt M. F. G., Schlesinger M. J. 1980; Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins. Journal of Biological Chemistry 255:3334–3339
    [Google Scholar]
  37. Schmidt M. F. G., Bracha M., Schlesinger M. J. 1979; Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins. Proceedings of the National Academy of Sciences, U.S.A 76:1687–1691
    [Google Scholar]
  38. Schultz A., Oroszlan S. 1984; Myristylation of gag-onc fusion proteins in mammalian transforming retroviruses. Virology 133:431–437
    [Google Scholar]
  39. Sefton B. M., Trowbridge I. S., Cooper J. A. 1982; The transforming proteins of Rous sarcoma virus, Harvey sarcoma virus and Abelson virus contain tightly bound lipid. Cell 31:465–474
    [Google Scholar]
  40. Towler D. A., Eubanks S. R., Towery D. S., Adams S. P., Glaser L. 1987; Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. Journal of Biological Chemistry 262:1030–1036
    [Google Scholar]
  41. Van Der Valk J., Verlaan I., De Laat S. W., Moolenaar W. H. 1987; Expression of pp60v-src alters the ionic permeability of the plasma membrane in rat cells. Journal of Biological Chemistry 262:2431–2434
    [Google Scholar]
  42. Veit M., Schmidt M. F. G., Rott R. 1989; Different palmitoylation of paramyxovirus glycoproteins. Virology 168:173–176
    [Google Scholar]
  43. Wold F. 1986; Fatty acylation of proteins (keep fit with fat?). Trends in Biochemical Sciences 11:58–59
    [Google Scholar]
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