Changes in Morphology, Infectivity and Haemagglutinating Activity of Semliki Forest Virus Produced by the Treatment with Caseinase C from G. Free

Abstract

SUMMARY

Electron micrographs of negatively stained Semliki Forest virus were made before and after treatment of the virus with caseinase C from G. The virus appeared as roughly spherical (diameter 550–590 Å), covered with projections and sometimes bearing an appendix, which seemed to be a fold of the envelope. Treated with caseinase C in tris buffered saline, the virus lost its projections and its haemagglutinating activity but remained infectious. The site of haemagglutination, then, is probably located on the projections. Treated with caseinase C in phosphate buffer, the virus lost its infectivity as well as its haemagglutinating activity; the number of the remaining viral particles was not significantly modified. These structures had no projections; their envelope was degraded and sometimes completely destroyed. In this case, they had a smaller diameter (385–390 Å) than the projectionless particles obtained by treatment in tris buffered saline (410–460 Å). As the virus particles with degraded envelope still contained as much infectious RNA as the controls, it was thought that some degree of integrity of the envelope was necessary for the particle infectivity. Thus the site for infectivity appeared to be different from that for haemagglutination.

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1966-04-01
2024-03-29
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References

  1. Anderson S. G., Ada G. L. 1961; The action of phospholipase A and lipid solvents on Murray Valley encephalitis virus. J. gen. Microbiol 25:451
    [Google Scholar]
  2. Andrewes C. H., Horstman D. H. 1949; The susceptibility of viruses to ethyl ether. J. gen. Microbiol 3:290
    [Google Scholar]
  3. Borecky L., Lackovic V., Mrena E. 1964; The effect of trypsin on influenza virus. Acta Virol 8:555
    [Google Scholar]
  4. Brenner S., Horne R. W. 1959; A negative staining method for high resolution electron microscopy of viruses. Biochim. biophys. Acta 34:103
    [Google Scholar]
  5. Cheng P. Y. 1958; The inactivation of group B arthropod borne viruses by proteases. Virology 6:129
    [Google Scholar]
  6. Cheng P. Y. 1961; Purification, size and morphology of a mosquito borne animal virus, Semliki Forest virus. Virology 14:124
    [Google Scholar]
  7. Clarke D., Casals J. 1958; Techniques for haemagglutination and haemagglutination inhibition with arthropod borne viruses. Am. J. trop. Med. Hyg 7:561
    [Google Scholar]
  8. Cohen A. 1963 Mechanism of cell infection. 1. Virus attachment and penetration. Mechanism of virus infection153 ed. by Smith Wilson. London, New York: Academic Press;
    [Google Scholar]
  9. Franklin R. M. 1962; The significance of lipids in animal viruses. Progress Med. Virol 4:1
    [Google Scholar]
  10. Ghuysen J. M., Leyh-Bouille M., Dierickx L. 1962; Structure de la paroi de Bacillus megaterium kmI. Isolement de l’amidase et d’un enzyme nouveau sécrété par le Streptomyces albus g et actif sur la parois de Bacillus megaterium et de Micrococcus lysodeikticus. Biochim. biophys. Acta 63:286
    [Google Scholar]
  11. Horne R. W. 1961 The examination of small particles. Techniques for electron microscopy Ed. by Kay D.150 Oxford: Blackwell Scientific Publications;
    [Google Scholar]
  12. Horne R. W., Wildy P. 1963; Virus structure revealed by negative staining. Advanc. Virus Res 10:101
    [Google Scholar]
  13. Klimenko S. M., Yershov F. I., Gofman Y. P., Nabatnikov A. P., Zhdanov V. M. 1965; Architecture of Venezuelan Equine encephalitis virus. Virology 27:125
    [Google Scholar]
  14. Knight C. A. 1963 Chemistry of viruses. Protoplasmologia : Handbuch der Protoplasmaforschung Vienna: Springer Verlag;
    [Google Scholar]
  15. Miller G. L., Ziegler R. W. 1964; Virus particle count with the negative staining spray droplet technique. Proc. Soc. exp. Biol. Med 115:289
    [Google Scholar]
  16. Morgan C, Howe C., Ross H. N. 1961; Structure of viruses as observed in the electron microscope. V. Western equine encephalitis virus. J. exp. Med 113:219
    [Google Scholar]
  17. Mussgay M. 1964; Growth cycle of Arboviruses in vertebrates and arthropod cells. Progress Med. Virol 6:193
    [Google Scholar]
  18. Mussgay M., Rott R. 1964; Studies on the structure of an haemagglutinating component of a group A arbovirus (Sindbis). Virology 23:573
    [Google Scholar]
  19. Mussgay M., Weibel J. 1962; Electron microscopic and biological studies on the growth of Venezuelan equine encephalitis virus in KB cells. Virology 16:52
    [Google Scholar]
  20. Osterrieth P. M. 1964; RNA-like infectious principle liberated from Semliki Forest virus by sodium deoxycholate. Acta Virol 7:477
    [Google Scholar]
  21. Osterrieth P. M. 1965a; Comparison of the effect of caseinase C and Pronase on the haemagglutinating activity and on the infectivity of Semliki Forest virus. Acta Virol 9:471
    [Google Scholar]
  22. Osterrieth P. M. 1965b; Semliki Forest virus inactivation. Selective destruction of the haemagglutinating activity by caseinase C and of infectivity by sodium deoxycholate. Life Sci 4:1227
    [Google Scholar]
  23. Osterrieth P. M., Dierickx L. 1965; Antiviral activity of an enzyme complex from Streptomyces albus G culture filtrate. Acta Virol 9:248
    [Google Scholar]
  24. Philippson L., Choppin P. W. 1961; On the role of virus sulfhydryl groups in the attachment of enteroviruses to erythrocytes. J. exp. Med 112:455
    [Google Scholar]
  25. Porterfield J. S. 1960; A simple plaque inhibition test for the study of arthropod borne viruses. Bull. Wld Hlth Org 22:373
    [Google Scholar]
  26. Reginster M. 1965a; Inactivation of influenza virus by caseinase C from Streptomyces albus g culture filtrate. J. gen. Microbiol 40:157
    [Google Scholar]
  27. Reginster M. 1965b; Modification of influenza virus by Streptomyces albus g caseinase C. Acta Virol 9:462
    [Google Scholar]
  28. Reginster M. 1966; Release of influenza virus neuraminidase by caseinase C of Streptomyces albus g. J. gen. Microbiol 42:323
    [Google Scholar]
  29. Richter A., Wecker E. 1963; The reaction of Eastern equine encephalitis virus preparation with sodium deoxycholate. Virology 20:263
    [Google Scholar]
  30. Smith K. O. 1964; Relationship between the envelope and infectivity of Herpes virus. Proc. Soc. exp. Biol. Med 115:814
    [Google Scholar]
  31. Takehara M., Hotta S. 1961; Effect of enzymes on a partially purified Japanese B encephalitis virus and on related arboviruses. Science 134:1878
    [Google Scholar]
  32. Theiler M. 1957; Action of Na desoxycholate on arboviruses. Proc. Soc. exp. Biol. Med 96:380
    [Google Scholar]
  33. Watson D. H., Wildy P., Russell W. C. 1964; Quantitative electron microscope studies on the growth of Herpes virus using the techniques of negative staining and ultramicrotomy. Virology 24:523
    [Google Scholar]
  34. Wecker E., Richter A. 1962; Conditions for the replication of infectious viral RNA. Cold Spr. Harb. Symp. quant. Biol 27:137
    [Google Scholar]
  35. Wecker E., Schonne E. 1961; Inhibition of viral RNA synthesis by parafluoro-phenylalanine. Proc. natn. Acad. Sci. U.S.A 47:278
    [Google Scholar]
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