1887

Abstract

The nucleotide sequence of the bovine ephemeral fever virus (BEFV) genome has been determined from the 3′ terminus to the end of the nucleoprotein (N) gene. The 3′ leader sequence comprises 50 nucleotides and shares a common terminal three nucleotides (3′-UGC-) and a downstream U-rich domain with vesicular stomatitis virus (VSV) and rabies virus. The N gene comprises 1328 nucleotides from the transcription initiation consensus sequence (AACAGG) to the conserved transcription termination-poly(A) sequence [CATG(A)] and encodes a polypeptide of 431 amino acids with an estimated of 49159 and a pI of 5·4. The deduced amino acid sequence of the BEFV N protein is similar to those of other mammalian rhabdoviruses and is more closely related in sequence to vesiculoviruses (VSV Indiana and New Jersey, Piry, Chandipura) than to lyssaviruses (rabies and Mokola). An almost full-length clone, 1301 bp in length, of the BEFV N gene and clones derived from 5′-terminal (559 bp) and 3′-terminal (742 bp) fragments were expressed in as glutathione--transferase fusion proteins. A panel of 12 BEFV N protein-specific monoclonal antibodies was shown to react in immunoblots with fusion proteins containing the almost full-length N protein and the C-terminal fragment, but not the N-terminal fragment. Two of these antibodies also reacted with baculovirus-expressed rabies virus N protein. Polyclonal mouse ascitic fluids derived from BEFV, rabies virus and several other related viruses were also shown to cross-react in immunoblots with purified preparations of rabies virus and BEFV N proteins.

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1994-08-01
2022-05-19
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References

  1. Barabino S. M. L., Sproat B. S., Lamond A. I. 1992; Antisense probes targeted to an internal domain in U2 SnRNP specifically inhibit the second step of pre-mRNA splicing. Nucleic Acids Research 20:4457–4464
    [Google Scholar]
  2. Barik S., Banerjee A. K. 1992; Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P. Proceedings of the National Academy of Sciences, U.S.A 89:6570–6574
    [Google Scholar]
  3. Barr J., Chambers P., Pringle C. R., Easton A. J. 1991; Sequence of the major nucleocapsid protein gene of pneumonia virus of mice: sequence comparisons suggest structural homology between nucleocapsid proteins of pneumoviruses, paramyxoviruses, rhabdo-viruses and filoviruses. Journal of General Virology 72:677–685
    [Google Scholar]
  4. Blumberg B. M., Leppert M., Kolakofsky D. 1981; Interaction of VSV leader RNA and nucleocapsid protein may control VSV genome replication. Cell 23:837–845
    [Google Scholar]
  5. Bourhy H., Kissi B., Tordo N. 1993; Molecular diversity of the Lyssavirus genus. Virology 194:70–81
    [Google Scholar]
  6. Boyd K. R., Whitaker-Dowling P. 1988; Flanders virus replication and protein synthesis. Virology 163:349–358
    [Google Scholar]
  7. Calisher C. H., Karabatsos N., Zeller H., Digoutte J. -P., Tesh R. B., Shope R. E., Travassos da Rosa A. P. A., St George T. D. 1989; Antigenic relationships among rhabdoviruses from vertebrates and haematophagous arthropods. Intervirology 50:241–257
    [Google Scholar]
  8. Crysler J. G., Lee P., Reinders M., Prevec L. 1990; The sequence of the nucleocapsid protein (N) gene of Piry virus: possible domains in the N protein of vesiculoviruses. Journal of General Virology 71:2191–2194
    [Google Scholar]
  9. Cybinski D. H., St George T. D. 1993; Antigenic variation in the bovine ephemeral fever virus glycoprotein. In Bovine Ephemeral Fever and Related Rhabdoviruses ACIAR Proceedings 44 pp. 131–137 St George T. D., Uren M. F., Young P. L., Hoffman D. Edited by Canberra: ACIAR;
    [Google Scholar]
  10. Cybinski D. H., Walker P. J., Byrne K. A., Zakrzewski H. 1990; Mapping of antigenic sites on the bovine ephemeral fever virus glycoprotein using monoclonal antibodies. Journal of General Virology 71:2065–2072
    [Google Scholar]
  11. Dayhoff M. O., Schwartz R. M., Orcutt B. C. 1978 In Atlas of Protein Sequence and Structure, 5 supplement 3 p. 345 Dayhoff M. O. Edited by Washington: NBRF;
    [Google Scholar]
  12. Della-Porta A. J., Brown F. 1979; The physico-chemical characterization of bovine ephemeral fever virus as a member of the family Rhabdoviridae. Journal of General Virology 44:99–112
    [Google Scholar]
  13. Dietzschold B., Lafon M., Wang H., Otvos L., Celis E., Wunner W. H., Koprowski H. 1987; Localization and immunological characterization of antigenic domains of the rabies virus internal N and NS proteins. Virus Research 8:103–125
    [Google Scholar]
  14. Dietzschold B., Rupprecht C. E., Tollis M., Lafon M., Mattei J., Wiktor T. J., Koprowski H. 1988; Antigenic diversity of the glycoprotein and nucleocapsid proteins of rabies and rabies-related viruses: implications for epidemiology and control of rabies. Reviews of Infectious Diseases 10: supplement 4 785–798
    [Google Scholar]
  15. Doherty R. L., Standfast H. A., Clarke I. A. 1969; Adaptation to mice of the causative virus of ephemeral fever of cattle from an epizootic in Queensland, 1968. Australian Journal of Science 31:365–366
    [Google Scholar]
  16. Dumas J. B., Edwards M., Delort J., Mallet J. 1991; Oligodeoxynucleotide ligation of single-stranded cDNAs: a new tool for cloning 5′ ends of mRNAs and for constructing cDNA libraries by in vitro amplification. Nucleic Acids Research 19:5227–5232
    [Google Scholar]
  17. Geliebter J., Zeff R. A., Melvold R. W., Nathenson S. G. 1986; Mitotic recombination in germ cells generated two major histocompatibility complex mutant genes shown to be identical by RNA sequence analysis: Kbm9 and Kbm6. Proceedings of the National Academy of Sciences, U.S.A 83:3371–3375
    [Google Scholar]
  18. Georgi C., Blumberg B., Kolakofsky D. 1983; Sequence determination of the ( + ) leader RNA regions of the vesicular stomatitis virus, Chandipura, Cocal, and Piry serotype genomes. Journal of Virology 46:125–130
    [Google Scholar]
  19. Geysen H. M., Meloen R. H., Barteling S. J. 1984; Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proceedings of the National Academy of Sciences, U.S.A 81:3998–4002
    [Google Scholar]
  20. Gubler U., Hoffman B. J. 1983; A simple and very efficient method for generating cDNA libraries. Gene 25:263–269
    [Google Scholar]
  21. Higgins D. G., Sharp P. M. 1989; Fast and sensitive multiple sequence alignments on a microcomputer. Computer Applications in the Biosciences 5:151–153
    [Google Scholar]
  22. Kyte J., Doolittle R. F. 1982; A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 157:105–132
    [Google Scholar]
  23. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
  24. Lafon M., Wiktor T. J. 1985; Antigenic sites on the ERA rabies virus nucleoprotein and non-structural protein. Journal of General Virology 66:2125–2133
    [Google Scholar]
  25. Marston F. A. O., Lowe P. A., Doel M. T., Schoemaker J. M., White S., Angal S. 1984; Purification of calf prochymosin (prorennin) synthesized in Escherichia coli. Bio/Technology 2:800–804
    [Google Scholar]
  26. Masters P. S., Banerjee A. K. 1987; Sequences of Chandipura virus N and NS genes: evidence for high mutability of the NS gene within vesiculoviruses. Virology 157:298–306
    [Google Scholar]
  27. Moyer S. A., Smallwood-Kentro S., Haddad A., Prevec L. 1991; Assembly and transcription of synthetic vesicular stomatitis virus nucleocapsids. Journal of Virology 65:2170–2178
    [Google Scholar]
  28. Murphy F. A., Taylor W. P., Mims C. A., Whitfield S. G. 1972; Bovine ephemeral fever in cell culture and mice. Archiv für die gesamte Virusforschung 38:234–249
    [Google Scholar]
  29. Nichol S. T., Holland J. J. 1987; Genome RNA terminus conservation and diversity among vesiculoviruses. Journal of Virology 61:200–205
    [Google Scholar]
  30. Pattniak A.K, LeGrone A. W., Wertz G. W. 1992; Infectious defective interfering particles of VSV from transcripts of a cDNA clone. Cell 69:1011–1020
    [Google Scholar]
  31. Poch O., Blumberg B. M., Bougueleret L., Tordo N. 1990; Sequence comparison of five polymerases (L proteins) of unsegmented negative-strand RNA viruses: theoretical assignment of functional domains. Journal of General Virology 71:1153–1162
    [Google Scholar]
  32. Pustell J., Kafatos F. C. 1984; A convenient and adaptable package of computer programs for DNA and protein sequence management, analysis, and homology determination. Nucleic Acids Research 12:643–655
    [Google Scholar]
  33. Riding G. A., Wang Y., Walker P. J. 1993; A strategy for purification and peptide sequence analysis of bovine ephemeral fever virus structural proteins. In Bovine Ephemeral Fever and Related Rhabdoviruses ACIAR Proceedings 44 pp. 98–102 St George T. D., Uren M. F., Young P. L., Hoffman D. Edited by Canberra: ACIAR;
    [Google Scholar]
  34. Roy P., Gupta K. C., Kiuchi A. 1984; Characterization of spring viremia of carp virus mRNA species and the 3′ sequence of the viral RNA. Virus Research 1:189–202
    [Google Scholar]
  35. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: A Laboratory Manual,, 2nd edn. New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
  36. Sanchez A., Kiley M. P., Klenk H.-D., Feldmann H. 1992; Sequence analysis of the Marburg virus nucleoprotein gene: comparison to Ebola virus and other non-segmented negative-strand RNA viruses. Journal of General Virology 73:347–357
    [Google Scholar]
  37. Smallwood S., Moyer S. A. 1993; Promoter analysis of the vesicular stomatitis virus RNA polymerase. Virology 192:254–263
    [Google Scholar]
  38. Smith D. B., Johnson K. S. 1988; Single step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67:31–40
    [Google Scholar]
  39. Sokol F., Clark H. F. 1973; Phosphoproteins, structural components of rhabdoviruses. Virology 52:246–263
    [Google Scholar]
  40. Sokol F., Clark H. F., Wiktor T. J., Mcfalls M. L. 1974; Structural phosphoproteins associated with ten rhabdoviruses. Journal of General Virology 24:433–445
    [Google Scholar]
  41. Soria M., Little S. P., Huang A. S. 1974; Characterization of vesicular stomatitis virus nucleocapsids. I. Complementary 40S RNA molecules in nucleocapsids. Virology 61:270–280
    [Google Scholar]
  42. Thomas D., Newcomb W. W., Brown J. C., Wall J. S., Hainfeld J. F., Trus B. S., Steven A. C. 1985; Mass and molecular composition of vesicular stomatitis virus: a scanning transmission electron microscopy analysis. Journal of Virology 54:598–607
    [Google Scholar]
  43. Tordo N., Poch O., Ermine A., Keith G. 1986a; Primary structure of leader RNA and nucleoprotein genes of the rabies genome: segmented homology with VSV. Nucleic Acids Research 14:2671–2683
    [Google Scholar]
  44. Tordo N., Poch O., Ermine A., Keith G., Rougeon F. 1986b; Walking along the rabies genome: is the large G-L intergenic region a remnant gene?. Proceedings of the National Academy of Sciences, U.S.A 83:3914–3918
    [Google Scholar]
  45. Uren M. F., Walker P. J., Zakrzewski FI., St George T. D., Byrne K. A. 1993; Effective vaccination of cattle using the virion G protein of bovine ephemeral fever virus as an antigen. Vaccine in press
    [Google Scholar]
  46. Walker P. J., Byrne K. A., Cybinski D. H., Doolan D. L., Wang Y. 1991; Proteins of bovine ephemeral fever virus. Journal of General Virology 72:67–74
    [Google Scholar]
  47. Walker P. J., Byrne K. A., Riding G. A., Cowley J. A., Wang Y., Mcwilliam S. 1992; The genome of bovine ephemeral fever rhabdovirus contains two related glycoprotein genes. Virology 191:49–61
    [Google Scholar]
  48. Wang Y., Walker P. J. 1993; Adelaide River rhabdovirus expresses consecutive glycoprotein genes as polycistronic mRNA: new evidence of gene duplication as an evolutionary process. Virology 195:719–731
    [Google Scholar]
  49. Wunner W. H., Calisher C. H., Dietzgen R. G., Jackson A. O., Kitajima E. W., Lafon M., Leong J. C., Nichol S. T., Peters D., Smith J. S., Walker P. J. 1994; Rhabdoviridae. In Classification and Nomenclature of Viruses Wien & New York: Springer-Verlag; in press
    [Google Scholar]
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