Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1971 Oct;68(10):2579–2583. doi: 10.1073/pnas.68.10.2579

Spin-Label Electron Spin Resonance Study of the Lipid-Containing Membrane of Influenza Virus

Frank R Landsberger *,§, John Lenard *, John Paxton , Richard W Compans
PMCID: PMC389472  PMID: 4332817

Abstract

The organization of the lipid-containing membrane of influenza virus has been studied by the use of three different lipid spin labels, and the results are compared with a parallel study on human erythrocyte ghosts. The lipid phase of the viral membrane is slightly more rigid than that of the erythrocyte ghosts. The data suggest that the viral lipid is arranged in a bilayer. The data suggest that the viral lipid is arranged in a bilayer. The glycoprotein spikes covering the viral membrane were specifically removed by proteases, and no alteration in the environment of any of the three spin labels was detected. This suggests that the spikes are not involved in determining the organization of the lipid bilayer.

Keywords: erythrocyte ghosts, stearate label, androstane label, membrane glycoproteins

Full text

PDF
2579

Images in this article

Selected References

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

  1. Almeida J. D., Waterson A. P. Some observations on the envelope of an influenza virus. J Gen Microbiol. 1967 Jan;46(1):107–110. doi: 10.1099/00221287-46-1-107. [DOI] [PubMed] [Google Scholar]
  2. Archetti I., Jemolo A., Steve-Bocciarelli D., Arangio-Ruiz G., Tangucci F. On the fine structure of influenza viruses. Arch Gesamte Virusforsch. 1967;20(1):133–136. doi: 10.1007/BF01245776. [DOI] [PubMed] [Google Scholar]
  3. Ashe G. B., Steim J. M. Membrane transitions in Gram-positive bacteria. Biochim Biophys Acta. 1971 Jun 1;233(3):810–814. doi: 10.1016/0005-2736(71)90182-9. [DOI] [PubMed] [Google Scholar]
  4. Butler K. W., Smith I. C., Schneider H. Sterol structure and ordering effects in spin-labelled phospholipid multibilayer structures. Biochim Biophys Acta. 1970 Dec 1;219(2):514–517. doi: 10.1016/0005-2736(70)90236-1. [DOI] [PubMed] [Google Scholar]
  5. Bächi T., Gerhard W., Lindenmann J., Mühlethaler K. Morphogenesis of influenza A virus in Ehrlich ascites tumor cells as revealed by thin-sectioning and freeze-etching. J Virol. 1969 Nov;4(5):769–776. doi: 10.1128/jvi.4.5.769-776.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Caliguiri L. A., Klenk H. D., Choppin P. W. The proteins of the parainfluenza virus SV5. 1. Separation of virion polypeptides by polyacrylamide gel electrophoresis. Virology. 1969 Nov;39(3):460–466. doi: 10.1016/0042-6822(69)90094-4. [DOI] [PubMed] [Google Scholar]
  7. Chen C., Compans R. W., Choppin P. W. Parainfluenza virus surface projections: glycoproteins with haemagglutinin and neuraminidase activities. J Gen Virol. 1971 Apr;11(1):53–58. doi: 10.1099/0022-1317-11-1-53. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Compans R. W., Dimmock N. J. An electron microscopic study of single-cycle infection of chick embryo fibroblasts by influenza virus. Virology. 1969 Nov;39(3):499–515. doi: 10.1016/0042-6822(69)90098-1. [DOI] [PubMed] [Google Scholar]
  10. Compans R. W., Holmes K. V., Dales S., Choppin P. W. An electron microscopic study of moderate and virulent virus-cell interactions of the parainfluenza virus SV5. Virology. 1966 Nov;30(3):411–426. doi: 10.1016/0042-6822(66)90119-x. [DOI] [PubMed] [Google Scholar]
  11. Compans R. W., Klenk H. D., Caliguiri L. A., Choppin P. W. Influenza virus proteins. I. Analysis of polypeptides of the virion and identification of spike glycoproteins. Virology. 1970 Dec;42(4):880–889. doi: 10.1016/0042-6822(70)90337-5. [DOI] [PubMed] [Google Scholar]
  12. DODGE J. T., MITCHELL C., HANAHAN D. J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys. 1963 Jan;100:119–130. doi: 10.1016/0003-9861(63)90042-0. [DOI] [PubMed] [Google Scholar]
  13. FROMMHAGEN L. H., KNIGHT C. A., FREEMAN N. K. The ribonucleic acid, lipid, and polysaccharide constituents of influenza virus preparations. Virology. 1959 Jun;8(2):176–197. doi: 10.1016/0042-6822(59)90003-0. [DOI] [PubMed] [Google Scholar]
  14. Holland J. J., Kiehn E. D. Influenza virus effects on cell membrane proteins. Science. 1970 Jan 9;167(3915):202–205. doi: 10.1126/science.167.3915.202. [DOI] [PubMed] [Google Scholar]
  15. Hsia J. C., Schneider H., Smith I. C. A spin label study of the effects of cholesterol in liposomes. Chem Phys Lipids. 1970 Apr;4(2):238–242. doi: 10.1016/0009-3084(70)90055-1. [DOI] [PubMed] [Google Scholar]
  16. Hubbell W. L., McConnell H. M. Molecular motion in spin-labeled phospholipids and membranes. J Am Chem Soc. 1971 Jan 27;93(2):314–326. doi: 10.1021/ja00731a005. [DOI] [PubMed] [Google Scholar]
  17. Hubbell W. L., McConnell H. M. Orientation and motion of amphiphilic spin labels in membranes. Proc Natl Acad Sci U S A. 1969 Sep;64(1):20–27. doi: 10.1073/pnas.64.1.20. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Klenk H. D., Caliguiri L. A., Choppin P. W. The proteins of the parainfluenza virus SV5. II. The carbohydrate content and glycoproteins of the virion. Virology. 1970 Oct;42(2):473–481. doi: 10.1016/0042-6822(70)90290-4. [DOI] [PubMed] [Google Scholar]
  19. Klenk H. D., Choppin P. W. Glycosphingolipids of plasma membranes of cultured cells and an enveloped virus (SV5) grown in these cells. Proc Natl Acad Sci U S A. 1970 May;66(1):57–64. doi: 10.1073/pnas.66.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Klenk H. D., Choppin P. W. Lipids of plasma membranes of monkey and hamster kidney cells and of parainfluenza virions grown in these cells. Virology. 1969 Jun;38(2):255–268. doi: 10.1016/0042-6822(69)90367-5. [DOI] [PubMed] [Google Scholar]
  21. Klenk H. D., Choppin P. W. Plasma membrane lipids and parainfluenza virus assembly. Virology. 1970 Apr;40(4):939–947. doi: 10.1016/0042-6822(70)90140-6. [DOI] [PubMed] [Google Scholar]
  22. Laver W. G., Valentine R. C. Morphology of the isolated hemagglutinin and neuraminidase subunits of influenza virus. Virology. 1969 May;38(1):105–119. doi: 10.1016/0042-6822(69)90132-9. [DOI] [PubMed] [Google Scholar]
  23. Libertini L. J., Waggoner A. S., Jost P. C., Griffith O. H. Orientation of lipid spin labels in lecithin multilayers. Proc Natl Acad Sci U S A. 1969 Sep;64(1):13–19. doi: 10.1073/pnas.64.1.13. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. McSharry J. J., Wagner R. R. Lipid composition of purified vesicular stomatitis viruses. J Virol. 1971 Jan;7(1):59–70. doi: 10.1128/jvi.7.1.59-70.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Phillips M. C., Kamat V. B., Chapman D. The interaction of cholesterol with the sterol free lipids of plasma membranes. Chem Phys Lipids. 1970 Aug;4(3):409–417. doi: 10.1016/0009-3084(70)90039-3. [DOI] [PubMed] [Google Scholar]
  26. Rottem S., Hubbell W. L., Hayflick L., McConnell H. M. Motion of fatty acid spin labels in the plasma membrane of mycoplasma. Biochim Biophys Acta. 1970;219(1):104–113. doi: 10.1016/0005-2736(70)90065-9. [DOI] [PubMed] [Google Scholar]
  27. Wilkins M. H., Blaurock A. E., Engelman D. M. Bilayer structure in membranes. Nat New Biol. 1971 Mar 17;230(11):72–76. doi: 10.1038/newbio230072a0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES