1887

Abstract

SUMMARY

Isolates of tick-borne encephalitis (TBE) virus from Finland, Germany, Czechoslovakia, Switzerland and Austria were compared with strains of the Far Eastern subtype isolated in Russia as well as Louping ill virus and other flaviviruses belonging to a different serocomplex: West Nile, Murray Valley encephalitis and Rocio viruses. Analysis of the structural polypeptides by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) revealed identical mol. wt. of the glycoprotein E (mol. wt. 55000) and the core protein C (mol. wt. 15000) for all the TBE virus strains analysed. However, the small envelope protein M from viruses isolated in Germany, Switzerland and Austria migrated slightly slower (apparent mol. wt. 7500) compared to M from viruses isolated in Finland, Czechoslovakia or the Far Eastern subtype strains (apparent mol. wt. 6500 to 7000). The structural glycoproteins were isolated from purified [S]methionine-labelled virions and subjected to peptide mapping by limited proteolysis with α-chymotrypsin or V8 protease followed by SDS-PAGE of the resulting cleavage products. With both proteases a remarkably homogeneous pattern was obtained for all the European isolates with only very minor deviations from the common pattern in single cases. Similar but distinguishable patterns were obtained for the Far Eastern subtype strains and also Louping ill virus, which, in addition, differed in the mol. wt. of its core protein C (mol. wt. 16000) and the small membrane protein M (mol. wt. 9000). These almost identical peptide maps observed with the TBE virus strains were in sharp contrast to the unrelated patterns obtained with the glycoproteins from West Nile, Murray Valley encephalitis and Rocio viruses. Although these viruses are serologically closely related and members of the same serocomplex of flaviviruses their glycoprotein peptide maps were completely different from one another. In a competitive radioimmunoassay all European TBE virus isolates showed identical immunological reactivity which further points to the great stability of this type of virus.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-57-2-263
1981-12-01
2021-10-27
Loading full text...

Full text loading...

/deliver/fulltext/jgv/57/2/JV0570020263.html?itemId=/content/journal/jgv/10.1099/0022-1317-57-2-263&mimeType=html&fmt=ahah

References

  1. Atassi M. Z. 1980; Precise determination of protein antigenic structures has unravelled the molecular immune recognition of proteins and provided a prototype for synthetic mimicking of other protein binding sites. Molecular and Cellular Biochemistry 32:21–43
    [Google Scholar]
  2. Brummer-Korvenkontio M., Saikku P., Korhonen P., Oker-Blom N. 1973; Arboviruses in Finland. I. Isolation of tick-borne encephalitis (TBE) virus from arthropods, vertebrates, and patients. American Journal of Tropical Medicine and Hygiene 22:382–389
    [Google Scholar]
  3. Clarke D. H. 1962; Antigenic relationship among viruses of the tick-borne encephalitis complex as studied by antibody absorption and agar gel precipitin techniques. In Symposium on the Biology of Viruses of the Tick-Borne Encephalitis Complex pp. 67–75 Edited by Libikova H. New York: Academic Press;
    [Google Scholar]
  4. Clarke D. H. 1964; Further studies on antigenic relationship among the viruses of the group B tick-borne complex. Bulletin of the World Health Organization 31:45–56
    [Google Scholar]
  5. Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. 1977; Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. Journal of Biological Chemistry 252:1102–1106
    [Google Scholar]
  6. Crumpton M. J. 1974; Protein antigens: the molecular basis of antigenicity and immunogenicity. In The Antigens vol 2 pp. 1–78 Edited by Sela M. New York and London: Academic Press;
    [Google Scholar]
  7. De Jong W. W., Zweers A., Cohen L. M. 1978; Influence of single amino acid substitutions on electrophoretic mobility of sodium-dodecylsulphate-protein complexes. Biochemical and Biophysical Research Communications 82:532–539
    [Google Scholar]
  8. De Madrid A. T., Porterfield J. S. 1974; The flaviviruses (group B arboviruses): a cross-neutralization study. Journal of General Virology 23:91–96
    [Google Scholar]
  9. France J. K., Wyrick B. C., Trent D. W. 1979; Biochemical and antigenic comparisons of the envelope glycoproteins of Venezuelan equine encephalomyelitis virus strains. Journal of General Virology 44:725–740
    [Google Scholar]
  10. Hall W. W., Lamb R. A., Choppin P. W. 1980; The polypeptides of canine distemper virus: synthesis in infected cells and relatedness to the polypeptides of other morbilliviruses. Virology 100:433–449
    [Google Scholar]
  11. Heinz F. X., Kunz Ch. 1980; Formation of polymeric glycoprotein complexes from a flavivirus: tick-borne encephalitis virus. Journal of General Virology 49:125–132
    [Google Scholar]
  12. Heinz F. X., Kunz C. H., Fauma H. 1980; Preparation of a highly purified vaccine against tick-borne encephalitis by continuous flow zonal ultracentrifugation. Journal of Medical Virology 6:213–222
    [Google Scholar]
  13. Heinz F. X., Tuma W., Kunz C. H. 1981; Antigenic and immunogenic properties of defined physical forms of tick-borne encephalitis virus structural proteins. Infection and Immunity 33:250–257
    [Google Scholar]
  14. Karabatsos N. (editor) 1978; The Subcommittee on Information Exchange of the American Committee on Arthropod-Borne Viruses. International catalogue of arboviruses including certain other viruses of vertebrates. American Journal of Tropical Medicine and Hygiene (Supplement) 27:418–419
    [Google Scholar]
  15. Kunz Ch., Heinz F. X., Hofmann H. 1980a; The efficacy of vaccination against tick-borne encephalitis. Wiener Klinische Wochenschrift 92:809–813
    [Google Scholar]
  16. Kunz Ch., Heinz F. X., Hofmann H. 1980b; Immunogenicity and reactogenicity of a highly purified vaccine against tick-borne encephalitis. Journal of Medical Virology 6:103–109
    [Google Scholar]
  17. Laemmli U. K., Favre M. 1973; Maturation of the head of bacteriophage T4. I. DNA packaging events. Journal of Molecular Biology 80:575–599
    [Google Scholar]
  18. Nagai Y., Hamaguchi M., Maeno K., Inuma M., Matsumoto T. 1980; Proteins of Newcastle disease virus. A comparison by partial protease digestion among the strains of different pathogenicity. Virology 102:463–467
    [Google Scholar]
  19. Okuno T., Okada T., Kondo A., Suzuki M., Kabayashi M., Oya A. 1968; Immunotyping of different strains of Japanese encephalitis virus by antibody absorption and complement-fixation tests. Bulletin of the World Health Organization 38:547–563
    [Google Scholar]
  20. Porterfield J. S. 1980; Antigenic characteristics and classification of togaviridae. In The Togaviruses: Biology, Structure, Replication pp. 13–46 Edited by Schlesinger R. W. New York and London: Academic Press;
    [Google Scholar]
  21. Russell P. K., Brandt W. E., Dalrymple I. M. 1980; Chemical and antigenic structure of flaviviruses. In The Togaviruses: Biology, Structure, Replication pp. 503–529 Edited by Schlesinger R. W. New York and London: Academic Press;
    [Google Scholar]
  22. Schaffner G., Weissmann C. 1973; A rapid, sensitive, and specific method for the determination of protein in dilute solution. Analytical Biochemistry 56:502–514
    [Google Scholar]
  23. Shapiro D., Trent D., Brandt W. E., Russell P. K. 1972; Comparison of the virion polypeptides of group B arboviruses. Infection and Immunity 6:206–209
    [Google Scholar]
  24. Swank R. T., Munkres K. P. 1975; Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Analytical Biochemistry 39:462
    [Google Scholar]
  25. Trent D. W. 1977; Antigenic characterization of flavivirus structural proteins separated by isoelectric focusing. Journal of Virology 22:608–618
    [Google Scholar]
  26. Trent D. W., Grant J. A., Monath T. P. 1979; Genetic heterogeneity among Saint Louis encephalitis virus isolates of different geographic origin. In Vector-Borne Diseases Division 1979 Report Part I: Arbovirus Reference & Research pp. 165–184 U.S. Department of Health and Human Services Public Health Service Center for Disease Control;
    [Google Scholar]
  27. Vezza A. C., Rosen L., Repik P., Dalrymple J., Bishop D. H. L. 1980; Characterization of the viral RNA species of prototype dengue viruses. American Journal of Tropical Medicine and Hygiene 29:643–652
    [Google Scholar]
  28. Webster R. G., Laver W. G. 1975; Antigenic variation of influenza viruses. In The Influenza Viruses and Influenza pp. 270–310 Edited by Kilbourne E. D. New York and London: Academic Press;
    [Google Scholar]
  29. Wengler G., Beato M., Wengler G. 1979; In vitro translation of 42S virus-specific RNA from cells infected with the flavivirus West Nile virus. Virology 96:516–529
    [Google Scholar]
  30. Westaway E. G., McKimm J. L., McLeod L. G. 1977; Heterogeneity among flavivirus proteins separated in slab gels. Archives of Virology 53:305–312
    [Google Scholar]
  31. Westaway E. G., Schlesinger R. W., Dalrymple J. M., Trent D. W. 1980; Nomenclature of flavivirus-specified proteins. Intervirology 14:114–117
    [Google Scholar]
  32. Wyler R., Schmidtke W., Kunz Ch., Radda A., Henn V., Meyer R. 1973; Zeckenenzephalitis in der Region Schaffhausen. Isolierung des Virus aus Zecken und serologische Untersuchungen. Schweizerische Medizinische Wochenschrift 103:1487–1492
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-57-2-263
Loading
/content/journal/jgv/10.1099/0022-1317-57-2-263
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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