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. 1980 Jan;33(1):52–58. doi: 10.1128/jvi.33.1.52-58.1980

Heterogeneity of vesicular stomatitis virus particles: implications for virion assembly.

H F Lodish, M Porter
PMCID: PMC288522  PMID: 6245248

Abstract

Vesicular stomatitis virus (VSV) particles formed at early times after infection contain only one-third the amount of viral glycoportein (G protein), relative to the major internal structural proteins M and N, as is found in particles released later. These "early" particles also have a lower density in equilibrium sucrose gradients than do those formed later; however, the sedimentation velocity and specific infectivity of these two classes of particles are the same. VSV-infected cells also release virus-like particles which sediment considerably faster than authentic virions and contain a higher-than-normal proportion of the VSV G protein relative to internal VSV proteins. These particles have a reduced specific infectivity but a normal density in sucrose gradients. All classes of VSV virions contain a constant proportion of M and N polypeptides. The ratio of G protein to M or N protein, in contrast, can vary over a sixfold range; this implies that an interaction between a precise number of surface G proteins with either of the underlying M and N proteins is not a prerequisite for budding of infectious viral particles from the cell surface.

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Selected References

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

  1. Dubovi E. J., Wagner R. R. Spatial relationships of the proteins of vesicular stomatitis virus: induction of reversible oligomers by cleavable protein cross-linkers and oxidation. J Virol. 1977 May;22(2):500–509. doi: 10.1128/jvi.22.2.500-509.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Eger R., Compans R. W., Rifkin D. B. The organization of the proteins of vesicular stomatitis virions: labeling with pyridoxal phosphate. Virology. 1975 Aug;66(2):610–615. doi: 10.1016/0042-6822(75)90233-0. [DOI] [PubMed] [Google Scholar]
  3. Emerson S. U. Vesicular stomatitis virus: structure and function of virion components. Curr Top Microbiol Immunol. 1976;73:1–34. doi: 10.1007/978-3-642-66306-2_1. [DOI] [PubMed] [Google Scholar]
  4. Hecht T. T., Summers D. F. Interactions of vesicular stomatitis virus with murine cell surface antigens. J Virol. 1976 Sep;19(3):833–845. doi: 10.1128/jvi.19.3.833-845.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Katz F. N., Lodish H. F. Transmembrane biogenesis of the vesicular stomatitis virus glycoprotein. J Cell Biol. 1979 Feb;80(2):416–426. doi: 10.1083/jcb.80.2.416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Katz F. N., Rothman J. E., Lingappa V. R., Blobel G., Lodish H. F. Membrane assembly in vitro: synthesis, glycosylation, and asymmetric insertion of a transmembrane protein. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3278–3282. doi: 10.1073/pnas.74.8.3278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kelley J. M., Emerson S. U., Wagner R. R. The glycoprotein of vesicular stomatitis virus is the antigen that gives rise to and reacts with neutralizing antibody. J Virol. 1972 Dec;10(6):1231–1235. doi: 10.1128/jvi.10.6.1231-1235.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Knipe D. M., Baltimore D., Lodish H. F. Separate pathways of maturation of the major structural proteins of vesicular stomatitis virus. J Virol. 1977 Mar;21(3):1128–1139. doi: 10.1128/jvi.21.3.1128-1139.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Knipe D. M., Lodish H. F., Baltimore D. Localization of two cellular forms of the vesicular stomatitis viral glycoprotein. J Virol. 1977 Mar;21(3):1121–1127. doi: 10.1128/jvi.21.3.1121-1127.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Lenard J., Compans R. W. The membrane structure of lipid-containing viruses. Biochim Biophys Acta. 1974 Apr 8;344(1):51–94. doi: 10.1016/0304-4157(74)90008-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lenard J. Virus envelopes and plasma membranes. Annu Rev Biophys Bioeng. 1978;7:139–165. doi: 10.1146/annurev.bb.07.060178.001035. [DOI] [PubMed] [Google Scholar]
  13. Lingappa V. R., Katz F. N., Lodish H. F., Blobel G. A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function. J Biol Chem. 1978 Dec 25;253(24):8667–8670. [PubMed] [Google Scholar]
  14. Lodish H. F., Weiss R. A. Selective isolation of mutants of vesicular stomatitis virus defective in production of the viral glycoprotein. J Virol. 1979 Apr;30(1):177–189. doi: 10.1128/jvi.30.1.177-189.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McSharry J. J., Compans R. W., Choppin P. W. Proteins of vesicular stomatitis virus and of phenotypically mixed vesicular stomatitis virus-simian virus 5 virions. J Virol. 1971 Nov;8(5):722–729. doi: 10.1128/jvi.8.5.722-729.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Morrison T. G., McQuain C. O. Assembly of viral membranes: nature of the association of vesicular stomatitis virus proteins to membranes. J Virol. 1978 Apr;26(1):115–125. doi: 10.1128/jvi.26.1.115-125.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Nakai T., Howatson A. F. The fine structure of vesicular stomatitis virus. Virology. 1968 Jun;35(2):268–281. doi: 10.1016/0042-6822(68)90267-5. [DOI] [PubMed] [Google Scholar]
  18. Schnitzer T. J., Dickson C., Weiss R. A. Morphological and biochemical characterization of viral particles produced by the tsO45 mutant of vesicular stomatitis virus at restrictive temperature. J Virol. 1979 Jan;29(1):185–195. doi: 10.1128/jvi.29.1.185-195.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Toneguzzo F., Ghosh H. P. In vitro synthesis of vesicular stomatitis virus membrane glycoprotein and insertion into membranes. Proc Natl Acad Sci U S A. 1978 Feb;75(2):715–719. doi: 10.1073/pnas.75.2.715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wagner R. R., Prevec L., Brown F., Summers D. F., Sokol F., MacLeod R. Classification of rhabdovirus proteins: a proposal. J Virol. 1972 Dec;10(6):1228–1230. doi: 10.1128/jvi.10.6.1228-1230.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Weiss R. A., Boettiger D., Murphy H. M. Pseudotypes of avian sarcoma viruses with the envelope properties of vesicular stomatitis virus. Virology. 1977 Feb;76(2):808–825. doi: 10.1016/0042-6822(77)90261-6. [DOI] [PubMed] [Google Scholar]
  22. Závada J., Závodská E. Complementation and phenotypic stabilization of vesicular stomatitis virus temperature-sensitive and thermolabile mutants by avian myeloblastosis virus. Intervirology. 1974;2(1):25–32. doi: 10.1159/000149401. [DOI] [PubMed] [Google Scholar]

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