1887

Abstract

We investigated unusual structures produced in BHK-21 cells infected with rabies virus (HEP-Flury strain). Sellers’ staining of the cells revealed, in addition to Negri body-like structures (inclusion bodies), production of a fuchsin-stained cytoplasmic structure (FCPS) which encircled the nucleus. The frequency of the FCPS-forming cells increased as replication progressed. The FCPS was different from the inclusion body because the former contained the viral glycoprotein (G) and matrix protein (M2) antigens, while the latter contained nucleocapsid antigens. In the early phase of infection, we observed accumulation of viral envelope antigens in a cytoplasmic structure that was considered to be expanded rough endoplasmic reticulum (rER) because of its concomitant increase in BiP content. Time-course studies suggested that the envelope antigen-containing structure, which was not stained with basic fuchsin, translocated to the perinuclear region to form the FCPS. FCPS formation was dependent on incubation temperature and was decreased at 30°C, while the development of virus-induced cytopathic effect (CPE) was delayed. When the incubation temperature was shifted up to 37°C, FCPS formation was induced again and progression of CPE was accelerated in approximate proportion to the increasing number of FCPS-positive cells. From these studies, we conclude that viral G proteins gradually accumulate in the rER with M2 protein and the expanded rER converts eventually into the FCPS, which may be closely related to accelerated host cell death.

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1996-09-01
2024-03-28
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References

  1. Blondel D., Harmison G. G., Schubert M. 1990; Role of matrix protein in cytopathogenesis of vesicular stomatitis virus. ]oumal of Virology 64:1716–1725
    [Google Scholar]
  2. Coulon P., Deutsch V., Lafay F., Martinet-Edelist C., Wyers F., Herman R. C., Flamand A. 1990; Genetic evidence for multiple functions of the matrix protein of vesicular stomatitis virus. Journal of General Virology 71:991–996
    [Google Scholar]
  3. Dietzschold B., Rupprecht C. E., Tollis M., Lafon M., Mattel J., Wiktor T. J., Koprowski H. 1988; Antigenic diversity of the glycoprotein and nucleocapsid protein of rabies and rabies-related viruses: implications for epidemiology and control of rabies. Reviews of Infectious Diseases 10: Suppl 4785–798
    [Google Scholar]
  4. Gaudin Y., Tuffereau C., Durrer P., Flamand A., Ruigrok R. W. H. 1995; Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformation. Journal of Virology 69:5528–5534
    [Google Scholar]
  5. Hummeler K., Koprowski H., Wiktor T. J. 1967; Structure and development of rabies virus in tissue culture. Journal of Virology 1:152–170
    [Google Scholar]
  6. Hummeler K., Tomassini N., Sokol F., Kuwert E., Koprowski H. 1968; Morphology of the nucleoprotein component of rabies virus. Journal of Virology 2:1191–1199
    [Google Scholar]
  7. Kawai A., Matsumoto S. 1977; Interfering and noninterfering defective particles generated by a rabies small plaque variant virus. Virology 76:60–71
    [Google Scholar]
  8. Kawai A., Takeuchi K. 1992; Temperature-sensitivity of the replication of rabies virus (HEP–Flury strain) in BHK-21 cells. I. Alteration of viral RNA synthesis at the elevated temperature. Virology 186:524–532
    [Google Scholar]
  9. Kawai A., Matsumoto S., Tanabe K. 1975; Characterization of rabies viruses recovered from persistently infected BHK cells. Virology 67:520–533
    [Google Scholar]
  10. Lafon M., Wiktor T. J., Macfarlan R. I. 1983; Antigenic sites on the CVS rabies virus glycoprotein: analysis with monoclonal antibodies. Journal of General Virology 64:843–851
    [Google Scholar]
  11. Matsumoto S. 1970; Rabies virus. Advances in Virus Research 16:257–301
    [Google Scholar]
  12. Matsumoto S., Kawai A. 1969; Comparative studies on development of rabies virus in different host cells. Virology 39:449–459
    [Google Scholar]
  13. Matsumoto S., Schneider L. G., Kawai A., Yonezawa T. 1974; Further studies on the replication of rabies and rabies-like viruses in organized cultures of mammalian neural tissues. Journal of Virology 14:981–996
    [Google Scholar]
  14. Melki R., Gaudin Y., Blondel D. 1994; Interaction between tubulin and the viral matrix protein of vesicular stomatitis virus: possible implications in the viral cytopathic effect. Virology 202:339–347
    [Google Scholar]
  15. Miyamoto K., Matsumoto S. 1967; Comparative studies between pathogenesis of street and fixed rabies infection. Journal of Experimental Medicine 125:447–456
    [Google Scholar]
  16. Morimoto K., Kawai A., Mifune K. 1992; Comparison of rabies virus G proteins produced by cDNA-transfected animal cells that display either inducible or constitutive expression of the gene. Journal of General Virology 72:335–345
    [Google Scholar]
  17. Ni Y., Tominaga Y., Honda Y., Morimoto K., Sakamoto S., Kawai A. 1995; Mapping and characterization of a sequential epitope on the rabies virus glycoprotein which is recognized by a neutralizing monoclonal antibody, RG719. Microbiology and Immunology 39:693–702
    [Google Scholar]
  18. Sagara J., Tsukita Sa., Yonemura S., Tsukita Sh., Kawai A. 1995; Cellular actin-binding ezrin-radixin-moesin (ERM) family proteins are incorporated into the rabies virion and closely associated with viral envelope proteins in the cell. Virology 206:485–494
    [Google Scholar]
  19. Sellers T. F. 1927; A new method for staining Negri bodies of rabies. American Journal of Public Health 17:1080–1081
    [Google Scholar]
  20. Whitt M. A., Buonocore L., Prehaud C., Rose J. K. 1991; Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 185:681–688
    [Google Scholar]
  21. Ye Z., Sun W., Suryanarayana K., Justice P., Robinson D., Wagner R. R. 1994; Membrane-binding domains and cytopathogenesis of the matrix protein of vesicular stomatitis virus. Journal of Virology 68:7386–7396
    [Google Scholar]
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