1887

Abstract

The biological properties of an Indian isolate (GP78) of Japanese encephalitis virus (JEV) were characterized in tissue-cultured cells and mice and these were compared with the JaOArS982 strain from Japan. The GP78 strain had a markedly extended lag phase during its growth in porcine stable kidney (PS) cells. There were no obvious defects in the penetration of GP78 into PS cells. However, viral RNA and protein synthesis were significantly delayed in GP78-infected PS cells. Fusion-from-within assays carried out in C6/36 cells indicated that GP78 was less fusogenic than the JaOArS982 strain of JEV. Moreover, maximum fusion in GP78-infected cells occurred at pH 5.5, whereas JaOArS982-infected cells showed maximum fusion at pH 6.0. These results suggested that there may be a lesion in the virus-cell fusion process. The GP78 strain also showed delayed growth in brains of 1-week-old BALB/c mice. Although JEV GP78 was as virulent as the JaOArS982 strain in these mice, the appearance of clinical symptoms of JEV infection was delayed by a day in mice infected with the GP78 strain and these animals showed an increased average survival time. Comparison of the nucleotide sequences of the GP78 and the JaOArS982 strains of JEV identified a number of amino acid substitutions in structural proteins. Of these, a Thr→> Met substitution at residue 76 of the envelope protein is predicted to be causally associated with the altered biology of the GP78 strain during growth.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-80-7-1665
1999-07-01
2024-04-23
Loading full text...

Full text loading...

/deliver/fulltext/jgv/80/7/0801665a.html?itemId=/content/journal/jgv/10.1099/0022-1317-80-7-1665&mimeType=html&fmt=ahah

References

  1. Burke D. S., Leake C. J. 1988; Japanese encephalitis. In The Arboviruses:Epidemiology and Ecology vol 3 pp 63–92 Edited by Monath T. Boca Raton: CRC Press;
    [Google Scholar]
  2. Cecilia D., Gould E. A. 1991; Nucleotide changes responsible for loss of neuroinvasiveness in Japanese encephalitis virus neutralization-resistant mutants. Virology 181:70–77
    [Google Scholar]
  3. Chambers T. J., Hahn C. S., Galler R., Rice C. M. 1990; Flavivirus genome organization, expression, and replication. Annual Review of Microbiology 44:649–688
    [Google Scholar]
  4. Gage P. J., Levine M., Glorioso J. C. 1993; Syncytium-inducing mutations localize to two discrete regions within the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B. Journal of Virology 67:2191–2201
    [Google Scholar]
  5. Hasegawa H., Yoshida M., Shiosaka T., Fujita S., Kobayashi Y. 1992; Mutations in the envelope protein of Japanese encephalitis virus affect entry into cultured cells and virulence in mice. Virology 191:158–165
    [Google Scholar]
  6. Heinz F. X., Roehrig J. T. 1990; The basis for serodiagnosis and vaccines. In Immunochemistry of Viruses vol 2 pp 289–305 Edited by van Regenmortel V. M. H., Neurath A. R. Amsterdam: Elsevier Science;
    [Google Scholar]
  7. Huong V. T. Q., Ha D. Q., Deubel V. 1993; Genetic study of Japanese encephalitis viruses from Vietnam. American Journal of Tropical Medicine and Hygiene 49:538–544
    [Google Scholar]
  8. Ito M., Matsuo Y., Nishikawa K. 1997; Prediction of protein secondary structure using the 3D-1D compatibility algorithm. Computer Applications in the Biosciences 13:415–424
    [Google Scholar]
  9. Konishi E., Yamaoka M., Khin-Sane-Win Kurane I., Mason P. W. 1998; Induction of protective immunity against Japanese encephalitis in mice by immunization with a plasmid encoding Japanese encephalitis virus premembrane and envelope genes. Journal of Virology 72:4925–4930
    [Google Scholar]
  10. McMinn P.C. 1997; The molecular basis of virulence of the encephalitogenic flaviviruses. Journal of General Virology 78:2711–2722
    [Google Scholar]
  11. McMinn P. C., Weir R. C., Dalgarno L. 1996; A mouse-attenuated envelope protein variant of Murray Valley encephalitis virus with altered fusion activity. Journal of General Virology 77:2085–2088
    [Google Scholar]
  12. Mandl C. W., Guirakhoo F., Holzmann H., Heinz F. X., Kunz C. 1989; Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. Journal of Virology 63:564–571
    [Google Scholar]
  13. Mason P. W., Pincus S., Fournier M. J., Mason T. L., Shope R. E., Paoletti E. 1991; Japanese encephalitis virus-vaccinia recombinants produce particulate forms of the structural membrane proteins and induce high levels of protection against lethal JEV infection. Virology 180:294–305
    [Google Scholar]
  14. Mathur A., Chaturvedi U. C., Tandon H. O., Agarwal A. K., Mathur G. P., Nag D., Prasad A., Mittal V. P. 1982; Japanese encephalitis epidemic in Uttar Pradesh, India during 1978. Indian Journal of Medical Research 75:161–169
    [Google Scholar]
  15. Monath T. P., Heinz F. X. 1996; Flaviviruses. In Fields Virology 3rd edn, pp 961–1034 Edited by Fields B. N., Knipe D. M., Howley P. M. Philadelphia: Lippincott–Raven;
    [Google Scholar]
  16. Olmsted R. A., Meyer W. J., Johnston R. E. 1986; Characterization of Sindbis virus epitopes important for penetration in cell culture and pathogenesis in animals. Virology 148:245–254
    [Google Scholar]
  17. Randolph V. B., Stollar V. 1990; Low pH-induced cell fusion in flavivirus-infected Aedes albopictus cell cultures. Journal of General Virology 71:1845–1850
    [Google Scholar]
  18. Reed L. J., Muench H. 1938; A simple method of estimating fifty percent endpoints. American Journal of Hygiene 27:493–497
    [Google Scholar]
  19. Rey F. A., Heinz F. X., Mandl C., Kunz C., Harrison S. C. 1995; The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375:291–298
    [Google Scholar]
  20. Rice C. M. 1996; Flaviviridae: the viruses and their replication. In Fields Virology 3rd edn, pp 931–959 Edited by Fields B. N., Knipe D. M., Howley P. M. Philadelphia: Lippincott–Raven;
    [Google Scholar]
  21. Roehrig J. T., Hunt A. R., Johnson A. J., Hawkes R. A. 1989; Synthetic peptides derived from the deduced amino acid sequence of the E-glycoprotein of Murray Valley encephalitis virus elicit antiviral antibody. Virology 171:49–60
    [Google Scholar]
  22. Seif S. A., Morita K., Matsuo S., Hasebe F., Igarashi A. 1995; Finer mapping of neutralizing epitope(s) on the C-terminal of Japanese encephalitis virus E-protein expressed in recombinant Escherichia coli system. Vaccine 13:1515–1521
    [Google Scholar]
  23. Sumiyoshi H., Mori C., Fuke I., Morita K., Kuhara S., Kondou J., Kikuchi Y., Nagamatu H., Igarashi A. 1987; Complete nucleotide sequence of the Japanese encephalitis virus genome RNA. Virology 161:497–510
    [Google Scholar]
  24. Vaughn D. W., Hoke C. H. Jr 1992; The epidemiology of Japanese encephalitis: prospects for prevention. Epidemiologic Reviews 14:197–221
    [Google Scholar]
  25. Vrati S., Kerr P. J., Weir R. C., Dalgarno L. 1996; Entry kinetics and mouse virulence of Ross River virus mutants altered in neutralization epitopes. Journal of Virology 70:1745–1750
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-80-7-1665
Loading
/content/journal/jgv/10.1099/0022-1317-80-7-1665
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