1887

Abstract

SUMMARY

The structural polypeptides of egg grown mumps virus were analysed by SDS-polyacrylamide-slab-gel electrophoresis. Mumps virions contained eight major polypeptides with mol. wt. of 75, 73, 71, 61, 47, 44, 42 and 40 × 10. The 75 K and 61 K polypeptides were glycosylated. In virions treated with pronase and trypsin, the 75 K glycoprotein was removed more readily from the virus than the 61 K glycoprotein. The gradual removal of the 75 K glycoprotein was paralleled by a decrease of haemagglutinating activity. The large glycoprotein was cleaved into a 40 K glycoprotein by trypsin treatment. Pronase and trypsin treatment also removed the smallest 40 K non-glycosylated polypeptide. Thus this polypeptide appears to be located on the outside of the virion and probably represents a cleavage product of the large glycoprotein.

Treatment of virions with 2% Triton-X 100 under alkaline conditions in the absence or presence of 2 -KCl solubilized the two glycoproteins and a fraction of the 71 and 44 K polypeptides, but not the 73 and 47 K polypeptides. The two smallest polypeptides were solubilized by treatment with 2% Triton X-100 in the presence of 2 -KCl. Since the 40 K polypeptide was interpreted to represent a cleavage product of the large surface glycoprotein the 42 K polypeptide was proposed to represent the membrane protein of mumps virus. The 44 K polypeptide co-migrated with Vero cell actin. The nature of the 47 K polypeptide could not be determined, but it is probably located in the central part of the virus. The 73 K polypeptide and in some experiments also the 71 K polypeptide were found in purified nucleocapsid preparations.

It is concluded that mumps virus has a general polypeptide composition similar to other paramyxoviruses. However, the molecular weights of the different polypeptides of mumps virus differ markedly from the corresponding polypeptides in Newcastle disease virus and Sendai virus.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-41-3-527
1978-12-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/jgv/41/3/JV0410030527.html?itemId=/content/journal/jgv/10.1099/0022-1317-41-3-527&mimeType=html&fmt=ahah

References

  1. Bernard J. P., Northrop R. L. 1974; RNA polymerase in mumps virion. Journal of Virology 14:183–186
    [Google Scholar]
  2. 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]
  3. East J. L., Kinosbury D. W. 1971; Mumps virus replication in chick embryo lung cells: properties of ribonucleic acids in virions and infected cells. Journal of Virology 8:161–173
    [Google Scholar]
  4. Homma M., Ohuchi M. 1973; Trypsin action on the growth of Sendai virus in tissue culture cells. III. Structural difference of Sendai virus grown in eggs and tissue culture cells. Journal of Virology 12:1457–1465
    [Google Scholar]
  5. Huppertz H. I., Hall W. W., Ter Meulen V. 1977; Polypeptide composition of mumps virus. Medical Microbiology and Immunology 163:251–259
    [Google Scholar]
  6. Jensik S. C., Silver S. 1976; Polypeptides of mumps virus. Journal of Virology 17:363–373
    [Google Scholar]
  7. Kingsbury D. W., Bratt M. A., Choppin P. W., Hansen R. P., Hosaka Y., Ter Meulen V., Norrby E., Plowright W., Rott R., Wunner W. H. 1978; Paramyxoviridae. Intervirology 10:137–152
    [Google Scholar]
  8. Klenk H.-D., Rott R., Orlich M., Blödorn J. 1975; Activation of influenza A viruses by trypsin treatment. Virology 68:426–439
    [Google Scholar]
  9. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  10. Lamb R. A., Mahy B. W. J., Choppin P. W. 1976; The synthesis of Sendai virus polypeptides in infected cells. Virology 69:116–131
    [Google Scholar]
  11. Luukkonen A., Gahmberg C. G., Renkonen O. 1977; Surface labelling of Semliki Forest virus glyco-proteins using galactose oxidase. Virology 76:55–59
    [Google Scholar]
  12. Maizel J. V. 1971; Polyacrylamide gel electrophoresis of viral proteins. Methods in Virology 5179–246 Maramorosch K., Koprowski H. London and New York: Academic Press;
    [Google Scholar]
  13. Mountcastle W. E., Compans R. W., Caliguiri L. A., Choppin P. W. 1970; Nucleocapsid protein sub-unit of Simian virus 5, Newcastle disease virus, and Sendai virus. Journal of Virology 6:677–684
    [Google Scholar]
  14. Mountcastle W. E., Choppin P. W. 1977; A comparison of the polypeptides of four measles virus strains. Virology 78:463–474
    [Google Scholar]
  15. Örvell C. 1976; Identification of paramyxovirus-specific haemolysis-inhibiting antibodies separate from haemagglutinating inhibiting and neuraminidase-inhibiting antibodies. Acta Pathologica et Microbiologica Scandinavica Section B 84:441–457
    [Google Scholar]
  16. Scheid A., Caliguiri L. A., Compans R. W., Choppin P. W. 1972; Isolation of paramyxovirus glyco-proteins. Association of both hemagglutinating and neuraminidase activities with the larger SV5 glycoprotein. Virology 50:640–652
    [Google Scholar]
  17. Scheid A., Choppin P. W. 1973; Isolation and purification of the envelope proteins of Newcastle disease virus. Journal of Virology 11:263–271
    [Google Scholar]
  18. Scheid A., Choppin P. W. 1974; Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57:475–490
    [Google Scholar]
  19. Studier F. W. 1973; Analysis of bacteriophage T7 early RNAs and proteins on slab gels. Journal of Molecular Biology 79:237–248
    [Google Scholar]
  20. Tyrrell D. L. J., Norrby E. 1978; Structural polypeptides of measles virus. Journal of General Virology 39:219–229
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-41-3-527
Loading
/content/journal/jgv/10.1099/0022-1317-41-3-527
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