1887

Abstract

SUMMARY

Lipid-free influenza virus cores have been obtained by a three step procedure consisting of () treatment with proteolytic enzyme, () fixation with formaldehyde and () delipidization with saponin or deoxycholate.

Several reagents proved efficient in removing the virus lipids as judged by morphological features and increased buoyant density, but only cores prepared by means of sodium deoxycholate have been characterized closely. Ultrathin sections revealed round bodies (about 65 nm in diam.) delineated by a single dense track and with an internal structure very similar to that of the complete virus particles. They contained both the nucleoprotein and the M-protein and no lipids.

It is proposed to call the limiting structure which appears (3 to 4 nm thick in ultrathin sections) the core shell.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-31-2-211
1976-05-01
2024-04-24
Loading full text...

Full text loading...

/deliver/fulltext/jgv/31/2/JV0310020211.html?itemId=/content/journal/jgv/10.1099/0022-1317-31-2-211&mimeType=html&fmt=ahah

References

  1. COMP ANS R. W., DIMMOCK N. J. 1969; An electron microscopic study of single-cycle infection of chick embryo fibroblast by influenza virus. Virology 39:499–515
    [Google Scholar]
  2. COMPANS R. W., LANSBERGER F. R., LENARD J., CHOPPIN P. W. 1972 Structure of the membrane of influenza virus. Orthomyxoviruses and Paramyxoviruses: Session 13, Proceedings of the Second International Congress for Virology130–132 Edited by Melnick J. L. Basel: Karger;
    [Google Scholar]
  3. DOURMASHKIN R. R., TYRRELL D. A. J. 1974; Electron microscopic observations on the entry of influenza virus into susceptible cells. Journal of General Virology 24:129–141
    [Google Scholar]
  4. DULBECCO R., VOGT M. 1954; Plaque formation and isolation of pure line with poliomyelitis viruses. Journal of Experimental Medicine 99:167–182
    [Google Scholar]
  5. GIGG R., PAYNE S. N. 1969; The reaction of glutaraldehyde with tissue lipids. Chemistry and Physics of Lipids 3:292–296
    [Google Scholar]
  6. KENDAL A. P., APOSTOLOV K., BELYAVIN G. 1969; The effect of protease treatment on the morphology of influenza A, B and C viruses. Journal of General Virology 5:141–143
    [Google Scholar]
  7. KILBOURNE E. D., CHOPPIN P. W., SCHULZE I. T., BUCHER D. L. 1972; Influenza virus polypeptides and antigens. Summary of Influenza Workshop I. Journal of Infectious Diseases 125:447–455
    [Google Scholar]
  8. LAVER W. G. 1973 The polypeptides of influenza viruses. Advances in Virus Research 1857–104 Edited by Lauffer M. A., Bang F. B., Maramorosch K., Smith K. M. New York and London: Academic Press;
    [Google Scholar]
  9. LENARD J., WONG C. Y., COMPANS R. W. 1974; Association of internal membrane protein with the lipid bilayer in influenza virus. Biochimica et Biophysica Acta 332:341–349
    [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. 1951; Protein measurements with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  11. NERMUT M. V. 1972; Further investigation on the fine structure of influenza virus. Journal of General Virology 17:317–331
    [Google Scholar]
  12. NIR I., HALL M. O. 1974; Ultrastructure of lipid-depleted rod photoreceptor membrane. Journal of Cell Biology 63:587–598
    [Google Scholar]
  13. OXFORD J. S., SCHILD G. 1975 Immunological studies with influenza virus matrix protein. Negative Strand Viruses 1611–620 Edited by Mahy B. W. J., Barry R. D. London: Academic Press;
    [Google Scholar]
  14. PAYNE S. N. 1964; The quantitative separation and estimation by thin-layer chromatography of lipids in nervous tissue. Journal of Chromatography 15:173–179
    [Google Scholar]
  15. REGINSTER M. 1965; Modification of influenza virus morphology by caseinase C from Streptomyces albus G. Acta Virologica 9:462–463
    [Google Scholar]
  16. REGINSTER M. 1966; Release of influenza neuraminidase by caseinase C of Streptomyces albus G. Journal of General Microbiology 42:323–331
    [Google Scholar]
  17. REYNOLDS E. S. J. 1963; The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. Journal of Cell Biology 17:208–212
    [Google Scholar]
  18. SCHILD G. C., HENRY-AYMARD M., PEREIRA H. G. 1972; A quantitative single radial diffusion test for immunological studies with influenza virus. Journal of General Virology 16:231–236
    [Google Scholar]
  19. SCHULZE I. T. 1970; The structure of influenza virus. I. The polypeptides of the virion. Virology 42:890–904
    [Google Scholar]
  20. SCHULZE I. T. 1972; The structure of influenza virus. II. A model based on the morphology and composition of subviral particles. Virology 47:181–196
    [Google Scholar]
  21. SCHULZE I. T. 1973 Structure of influenza virion. Advances in Virus Research 181–56 Edited by Lauffer M. A., Bang F. B., Maramorosh K., Smith K. M. New York & London: Academic Press;
    [Google Scholar]
  22. SKEHEL J. 1971; The characterization of subviral particles derived from influenza virus. Virology 44:409–417
    [Google Scholar]
  23. SKEHEL J., SCHILD G. C. 1971; The polypeptide composition of influenza A virus. Virology 44:396–408
    [Google Scholar]
  24. SOHIER R., PEILLARD M. M., GINESTE J., FREYDIER J. 1956; Micromethode en tubes pour la reaction de fixation du complement appliquée au diagnostic des infections a virus. Annales de Biologie Clinique 14:1–10
    [Google Scholar]
  25. SPURR A. R. 1969; A low viscosity epoxy resin embedding medium for electron microscopy. Journal of Ultrastructure Research 26:31–43
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-31-2-211
Loading
/content/journal/jgv/10.1099/0022-1317-31-2-211
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error