Single Amino Acid Codon Changes Detected in Louping Ill Virus Antibody-Resistant Mutants with Reduced Neurovirulence

References

1. Arbiza J., Taylor G., López J. A., Furze J., Wyld S., Whyte P., Stott E. J., Wertz G., Sullender W., Trudel M., Melero J. A. 1992; Characterization of two antigenic sites recognized by neutralizing monoclonal antibodies directed against the fusion glycoprotein of human respiratory syncytial virus. Journal of General Virology 73:2225–2234
   [Google Scholar]
2. Calisher C. H., Karabatsos N., Dalrymple J. M., Shope R. E., Porterfield J. S., Westaway E. G., Brandt W. E. 1989; Antigenic relationships between flaviviruses as determined by crossneutralization tests with polyclonal antisera. Journal of General Virology 70:37–13
   [Google Scholar]
3. 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]
4. Chomczynski P., Sacchi N. 1987; Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry 162:156–159
   [Google Scholar]
5. Clarke D. H., Casals J. 1958; Techniques for hemagglutination and hemagglutination-inhibition with arthropod-borne viruses. American Journal of Tropical Medicine and Hygiene 7:561–573
   [Google Scholar]
6. De Madrid A. T., Porterfield J. S. 1974; The flaviviruses (group B arboviruses): a cross-neutralization study. Journal of General Virology 23:91–96
   [Google Scholar]
7. Dietzschold B., Wunner W. H., Wiktor T. J., Lopes A. D., Lafon M., Smith C. L., Koprowski H. L. 1983; Characterization of an antigenic determinant of the glycoprotein that correlates with pathogenicity of rabies virus. Proceedings of the National Academy of Sciences, U.S.A. 80:70–74
   [Google Scholar]
8. Gould E. A., Buckley A., Cammack N., Barrett A. D. T., Clegg J. C. S., Ishak R., Varma M. G. R. 1985; Examination of the immunological relationships between flaviviruses using yellow fever virus monoclonal antibodies. Journal of General Virology 66:1369–1382
   [Google Scholar]
9. Gould E. A., Buckley A., Higgs S., Gaidamovich S. 1990; Antigenicity of flaviviruses. Archives of Virology Supplementum 1:137–152
   [Google Scholar]
10. Gritsun T. S., Lashkevich V. A., Gould E. A. 1993; Nucleotide and deduced amino acid sequence of the envelope glycoprotein of Omsk haemorrhagic fever virus; comparison with other flaviviruses. Journal of General Virology 74:287–291
    [Google Scholar]
11. Hahn C. S., Dalrymple J. M., Strauss J. H., Rice C. M. 1987; Comparison of the virulent Asibi strain of yellow fever virus with the 17D vaccine strain derived from it. Proceedings of the National Academy of Sciences, U.S.A. 84:2019–2023
    [Google Scholar]
12. Hahn C. S., Galler R., Hunkapiller T., Dalrymple J. M., Strauss J. H., Strauss E. G. 1988; Nucleotide sequence of dengue 2 RNA and comparison of the encoded proteins with those of the other flaviviruses. Virology 162:167–180
    [Google Scholar]
13. Heinz F. X. 1986; Epitope mapping of flavivirus glycoproteins. Advances in Virus Research 31:103–167
    [Google Scholar]
14. Heinz F. X., Mandl C. W., Guirakhoo F., Holzmann H., Tuma W., Kunz C. 1990; The envelope protein E of tick-borne encephalitis virus and other flaviviruses: structure, function and evolutionary relationships. Archives of Virology Supplementum 1:125–135
    [Google Scholar]
15. Holzmann H., Heinz F. X., Mandl C. W., Guirakhoo F., Kunz C. 1990; A single amino acid substitution in envelope protein E of tick-borne encephalitis virus leads to attenuation in the mouse model. Journal of Virology 64:5156–5159
    [Google Scholar]
16. Lobigs M., Usha R., Nestorowicz A., Marshall I. D., Weir R. C., Dalgarno L. 1990; Host cell selection of the Murray Valley encephalitis virus variants altered at an RGD sequence in the envelope protein and in mouse virulence. Virology 176:587–595
    [Google Scholar]
17. Porterfield J. S. 1980 Antigenic characteristics and classification of Togaviridae. In The Togaviruses pp. 13–16 Edited by Schlesinger R. W. New York & London: Academic Press;
    [Google Scholar]
18. Reid H. W. 1987 Louping ill. In The Arboviruses: Epidemiology and Ecology vol. 3 pp. 117–135 Edited by Monath T. P. Boca Raton: CRC Press;
    [Google Scholar]
19. Russell D. L., Dalrymple J. M., Johnston R. E. 1989; Sindbis virus mutations which coordinately affect glycoprotein processing, penetration and virulence in mice. Journal of Virology 63:1619–1629
    [Google Scholar]
20. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences, U.S.A. 74:5463–5467
    [Google Scholar]
21. Shiu S. Y. W., Ayres M. D., Gould E. A. 1991; Genomic sequence of the structural proteins of louping ill virus: comparative analysis with tick-borne encephalitis virus. Virology 180:411–415
    [Google Scholar]
22. Venugopal K., Buckley A., Reid H. W., Gould E. A. 1992; Nucleotide sequence of the envelope glycoprotein of Negishi virus shows very close homology to louping ill virus. Virology 190:515–521
    [Google Scholar]
23. Westaway E. G., Brinton M. A., Gaidamovich S. Ya., Horzinek M. C., Igarashi A., Kääriänen L., Lvov D. K., Porterfield J. S., Russell P. K., Trent D. W. 1985; Flaviviridae. Intervirology 24:183–192
    [Google Scholar]