1887

Abstract

A cDNA encoding the spike (S) protein of the neurovirulent murine coronavirus JHMV variant c1-2 was isolated and sequenced. Analysis of the cDNA revealed that the S protein consists of 1376 amino acids, as does the S protein of mouse hepatitis virus 4. We inserted the cDNA into the genome of vaccinia virus to obtain a recombinant vaccinia virus (rVV). The S protein expressed in RK13 cells infected by the rVV was shown to be electrophoretically and immunologically indistinguishable from the S protein produced in DBT cells infected with c1-2 virus. RVV infection of rats and mice induced S protein-specific antibody production detectable by immunofluorescence and neutralization. Moreover, the S protein expressed by the rVV induced syncytium formation not only in mouse DBT and L cells, which are susceptible to c1-2 virus infection, but also in rabbit RK13 cells, which are not susceptible to c1-2 virus infection. This result suggests the possibility that RK13 cells have binding sites for the c1-2 virus S protein.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-73-5-1065
1992-05-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/jgv/73/5/JV0730051065.html?itemId=/content/journal/jgv/10.1099/0022-1317-73-5-1065&mimeType=html&fmt=ahah

References

  1. Banner L. R., Keck J. G., Lai M. M. C. 1990; A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus. Virology 175:548–555
    [Google Scholar]
  2. Boyle J. F., Weismeller D. G., Holmes K. V. 1987; Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues. Journal of Virology 61:185–189
    [Google Scholar]
  3. Collins A. R., Knobler R. L., Powell H., Buchmeier M. J. 1982; Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell fusion. Virology 119:358–371
    [Google Scholar]
  4. Dalziel R. G., Lampert P. W., Talbot J., Buchmeier M. J. 1986; Site-specific alteration of murine hepatitis virus type 4 peplomer glycoprotein E2 results in reduced neurovirulence. Journal of Virology 59:463–471
    [Google Scholar]
  5. Daya M., Wong F., Cervin M., Evans G., Vennema H., Spaan W., Anderson R. 1989; Mutation of host cell determinants which discriminate between lytic and persistent mouse hepatitis virus infection results in a fusion-resistant phenotype. Journal of General Virology 70:3335–3346
    [Google Scholar]
  6. De Groot R. J., Luytjes W., Horzinek M. C., van der Zeijst B. A. M., Spaan W. J. M., Wiley D. C. 1987; Evidence for a coiled-coil structure in the spike proteins of coronaviruses. Journal of Molecular Biology 196:963–966
    [Google Scholar]
  7. De Groot R. J., Vanleen R. W., Dalderup M. J. M., Vennema H., Horzinek M. C., Spaan W. J. M. 1989; Stably expressed FIPV peplomer protein induces cell fusion and elicits neutralizing antibodies in mice. Virology 171:493–502
    [Google Scholar]
  8. Fleming J. O., Trousdale M. D., El-Zaatari F. A. K., Stohlman S. A., Weiner L. P. 1986; Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies. Journal of Virology 58:869–875
    [Google Scholar]
  9. Frana M. F., Behnke J. N., Sturman L. S., Holmes K. V. 1985; Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: host-dependent differences in proteolytic cleavage and cell fusion. Journal of Virology 56:912–920
    [Google Scholar]
  10. Funahashi S., Sato T., Shida H. 1988; Cloning and characterization of the gene encoding the major protein of the A-type inclusion body of cowpox virus. Journal of General Virology 69:35–47
    [Google Scholar]
  11. Funahashi S., Itamura S., Iinuma H., Nerome K., Sugimoto M., Shida H. 1991; Increased expression in vivo and in vitro of foreign genes directed by A-type inclusion body hybrid promoters in recombinant vaccinia viruses. Journal of Virology 65:5584–5588
    [Google Scholar]
  12. Holmes K. V., Doller E. W., Behnke J. N. 1981; Analysis of the function of coronavirus glycoproteins by differential inhibition of synthesis with tunicamycin. Advances in Experimental Medicine and Biology 142:131–142
    [Google Scholar]
  13. Kyuwa S., Stohlman S. A. 1990; Pathogenesis of a neurotropic murine coronavirus strain JHM in central nervous system of mice. Seminars in Virology 1:273–280
    [Google Scholar]
  14. Lee H., Shieh C., Gorbalenya A., Koonin E., Monica N. A., Tuler J., Bagdzhadzhyan A., Lai M. M. C. 1991; The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase. Virology 180:567–582
    [Google Scholar]
  15. Maniatis T., Fritsch E. F., Sambrook J. 1982 Molecular Cloning: A Laboratory Manual New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  16. Matsubara Y., Watanabe R., Taguchi F. 1991; Neurovirulence of six different murine coronavirus JHMV variants for rats. Virus Research 20:45–58
    [Google Scholar]
  17. Morris V. L., Tieszer C., Mackinnon J., Percy D. 1989; Characterization of coronavirus JHM variants isolated from Wistar Furth rats with a viral-induced demyelinating disease. Virology 169:127–136
    [Google Scholar]
  18. Parker S. E., Gallagher T. M., Buchmeier M. J. 1989; Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus. Virology 173:664–673
    [Google Scholar]
  19. Patel D. D., Ray C. A., Drucker R. P., Pickup D. J. 1988; A poxvirus derived vector that directs high levels of expression cloned genes in mammalian cells. Proceedings of the National Academy of Sciences, U.S.A. 85:9431–9435
    [Google Scholar]
  20. Schmidt I., Skinner M., Siddell S. 1987; Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM. Journal of General Virology 68:47–56
    [Google Scholar]
  21. Shida H. 1986; Nucleotide sequence of the vaccinia virus hemagglutinin gene. Virology 150:451–462
    [Google Scholar]
  22. Shida H., Matsumoto S. 1983; Analysis of the hemagglutinin glycoprotein from mutants of vaccinia virus that accumulates on the nuclear envelope. Cell 33:423–434
    [Google Scholar]
  23. Siddell S., Wege H., Barthel A., ter Meulen V. 1981; Coronavirus JHM: intracellular protein synthesis. Journal of General Virology 53:145–155
    [Google Scholar]
  24. Siddell S., Wege H., ter Meulen V. 1983; The biology of coronaviruses. Journal of General Virology 64:761–776
    [Google Scholar]
  25. Skinner M. A., Siddell S. G. 1985; Coding sequence of coronavirus MHV-JHM mRNA4. Journal of General Virology 66:593–596
    [Google Scholar]
  26. Spaan W., Cavanagh D., Horzinek M. C. 1988; Coronaviruses: structure and genome expression. Journal of General Virology 69:2939–2952
    [Google Scholar]
  27. Sturman L. S., Ricard C. S., Holmes K. V. 1985; Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments. Journal of Virology 56:904–911
    [Google Scholar]
  28. Taguchi F., Fleming J. O. 1989; Comparison of six different murine coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein. Virology 169:232–235
    [Google Scholar]
  29. Taguchi F., Yamada A., Fujiwara K. 1980; Resistance to highly virulent mouse hepatitis virus acquired by mice after low-virulence infection: enhanced antiviral activity of macrophages. Infection and Immunity 29:42–49
    [Google Scholar]
  30. Taguchi F., Siddell S., Wege H., ter Meulen V. 1985; Characterization of a variant virus selected in rat brains after infection by coronavirus mouse hepatitis virus JHM. Journal of Virology 54:429–435
    [Google Scholar]
  31. Taguchi F., Massa P., ter Meulen V. 1986; Characterization of a variant virus isolated from neural cell culture after infection of mouse coronavirus JHMV. Virology 155:267–270
    [Google Scholar]
  32. Takase-Yoden S., Kikuchi T., Siddell S., Taguchi F. 1990; Localization of neutralizing epitopes on the S1 polypeptide of the murine coronavirus peplomer glycoprotein. Virus Research 18:99–108
    [Google Scholar]
  33. Tyrrell D. A. J., Almeida J. D., Berry D. M., Cunningham C. H., Hamre K., Hofstad M. S., Malluci L., Macintosh K. 1968; Coronaviruses. Nature, London 220:650
    [Google Scholar]
  34. Vennema H., Hejnen L., Zijderfeld A., Horzinek M. C., Spaan W. J. M. 1990; Intracellular transport of recombinant coronavirus spike proteins: implication for virus assembly. Journal of Virology 64:339–346
    [Google Scholar]
  35. Wege H., Siddell S., ter Meulen V. 1982; The biology and pathogenesis of coronaviruses. Current Topics in Microbiology and Immunology 99:131–163
    [Google Scholar]
  36. Wege H., Dorries R., Wege H. 1984; Hybridoma antibodies to the murine coronavirus JHM: characterization of epitopes on the peplomer protein (E2). Journal of General Virology 65:1931–1942
    [Google Scholar]
  37. Wege H., Winter J., Meyermann R. 1988; The peplomer protein E2 of coronavirus JHM as a determinant of neurovirulence: definition of critical epitopes by variant analysis. Journal of General Virology 69:87–98
    [Google Scholar]
  38. Yoden S., Kikuchi T., Siddell S., Taguchi F. 1989; Expression of the peplomer glycoprotein of murine coronavirus JHM using a baculovirus vector. Virology 173:615–623
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-73-5-1065
Loading
/content/journal/jgv/10.1099/0022-1317-73-5-1065
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