Skip to main content
Journal of Virology logoLink to Journal of Virology
. 1987 May;61(5):1342–1349. doi: 10.1128/jvi.61.5.1342-1349.1987

Nucleotide sequence of a cDNA clone carrying the glycoprotein gene of infectious hematopoietic necrosis virus, a fish rhabdovirus.

J F Koener, C W Passavant, G Kurath, J Leong
PMCID: PMC254108  PMID: 3033264

Abstract

The nucleotide sequence of the mRNA encoding the glycoprotein of infectious hematopoietic necrosis virus was determined from a cDNA clone containing the entire coding region. The G-protein cDNA is 1,609 nucleotides long (excluding the polyadenylic acid) and encodes a protein of 508 amino acids. The predicted amino acid sequence was compared with that of the glycoprotein of the Indiana and New Jersey serotypes of vesicular stomatitis virus and with the glycoprotein of rabies virus, using a computer program which determined optimal alignment. An amino acid identity of approximately 20% was found between infectious hematopoietic necrosis virus and the two vesicular stomatitis virus serotypes and between infectious hematopoietic necrosis virus and rabies virus. The positions and sizes of the signal sequence and transmembrane domain and the possible glycosylation sites were determined.

Full text

PDF
1342

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amend D. F. Detection and transmission of infectious hematopoietic necrosis virus in rainbow trout. J Wildl Dis. 1975 Oct;11(4):471–478. doi: 10.7589/0090-3558-11.4.471. [DOI] [PubMed] [Google Scholar]
  2. Anilionis A., Wunner W. H., Curtis P. J. Structure of the glycoprotein gene in rabies virus. Nature. 1981 Nov 19;294(5838):275–278. doi: 10.1038/294275a0. [DOI] [PubMed] [Google Scholar]
  3. Appleyard R K. Segregation of New Lysogenic Types during Growth of a Doubly Lysogenic Strain Derived from Escherichia Coli K12. Genetics. 1954 Jul;39(4):440–452. doi: 10.1093/genetics/39.4.440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bergmann J. E., Tokuyasu K. T., Singer S. J. Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus en route to the plasma membrane. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1746–1750. doi: 10.1073/pnas.78.3.1746. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  7. Collins P. L., Huang Y. T., Wertz G. W. Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus. Proc Natl Acad Sci U S A. 1984 Dec;81(24):7683–7687. doi: 10.1073/pnas.81.24.7683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Doolittle R. F. Similar amino acid sequences: chance or common ancestry? Science. 1981 Oct 9;214(4517):149–159. doi: 10.1126/science.7280687. [DOI] [PubMed] [Google Scholar]
  9. Feng D. F., Johnson M. S., Doolittle R. F. Aligning amino acid sequences: comparison of commonly used methods. J Mol Evol. 1984;21(2):112–125. doi: 10.1007/BF02100085. [DOI] [PubMed] [Google Scholar]
  10. Gallione C. J., Rose J. K. Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus. J Virol. 1983 Apr;46(1):162–169. doi: 10.1128/jvi.46.1.162-169.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  12. Heindell H. C., Liu A., Paddock G. V., Studnicka G. M., Salser W. A. The primary sequence of rabbit alpha-globin mRNA. Cell. 1978 Sep;15(1):43–54. doi: 10.1016/0092-8674(78)90081-8. [DOI] [PubMed] [Google Scholar]
  13. Hill B. J. Physico-chemical and serological characterization of five rhabdoviruses infecting fish. J Gen Virol. 1975 Jun;27(3):369–378. doi: 10.1099/0022-1317-27-3-369. [DOI] [PubMed] [Google Scholar]
  14. Holmes D. S., Quigley M. A rapid boiling method for the preparation of bacterial plasmids. Anal Biochem. 1981 Jun;114(1):193–197. doi: 10.1016/0003-2697(81)90473-5. [DOI] [PubMed] [Google Scholar]
  15. Hsu Y. L., Engelking H. M., Leong J. C. Occurrence of different types of infectious hematopoietic necrosis virus in fish. Appl Environ Microbiol. 1986 Dec;52(6):1353–1361. doi: 10.1128/aem.52.6.1353-1361.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hubbard S. C., Ivatt R. J. Synthesis and processing of asparagine-linked oligosaccharides. Annu Rev Biochem. 1981;50:555–583. doi: 10.1146/annurev.bi.50.070181.003011. [DOI] [PubMed] [Google Scholar]
  17. Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984 Jan 25;12(2):857–872. doi: 10.1093/nar/12.2.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 1986 Jan 31;44(2):283–292. doi: 10.1016/0092-8674(86)90762-2. [DOI] [PubMed] [Google Scholar]
  19. Kozak M. Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Res. 1981 Oct 24;9(20):5233–5252. doi: 10.1093/nar/9.20.5233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kurath G., Ahern K. G., Pearson G. D., Leong J. C. Molecular cloning of the six mRNA species of infectious hematopoietic necrosis virus, a fish rhabdovirus, and gene order determination by R-loop mapping. J Virol. 1985 Feb;53(2):469–476. doi: 10.1128/jvi.53.2.469-476.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Kurath G., Leong J. C. Characterization of infectious hematopoietic necrosis virus mRNA species reveals a nonvirion rhabdovirus protein. J Virol. 1985 Feb;53(2):462–468. doi: 10.1128/jvi.53.2.462-468.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  23. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  24. McAllister P. E., Wagner R. R. Structural proteins of two salmonid rhabdoviruses. J Virol. 1975 Apr;15(4):733–738. doi: 10.1128/jvi.15.4.733-738.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. McCain B. B., Fryer J. L., Pilcher K. S. Physicochemical properties of RNA of salmonid hematopoietic necrosis virus (Oregon strain). Proc Soc Exp Biol Med. 1974 Jun;146(2):630–634. doi: 10.3181/00379727-146-38161. [DOI] [PubMed] [Google Scholar]
  26. Moore N. F., Barenholz Y., McAllister P. E., Wagner R. R. Comparative membrane microviscosity of fish and mammalian rhabdoviruses studied by fluorescence depolarization. J Virol. 1976 Jul;19(1):275–278. doi: 10.1128/jvi.19.1.275-278.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Mulcahy D., Pascho R., Jenes C. K. Comparison of in vitro growth characteristics of ten isolates of infectious haematopoietic necrosis virus. J Gen Virol. 1984 Dec;65(Pt 12):2199–2207. doi: 10.1099/0022-1317-65-12-2199. [DOI] [PubMed] [Google Scholar]
  28. Perlman D., Halvorson H. O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol. 1983 Jun 25;167(2):391–409. doi: 10.1016/s0022-2836(83)80341-6. [DOI] [PubMed] [Google Scholar]
  29. Rose J. K. Complete intergenic and flanking gene sequences from the genome of vesicular stomatitis virus. Cell. 1980 Feb;19(2):415–421. doi: 10.1016/0092-8674(80)90515-2. [DOI] [PubMed] [Google Scholar]
  30. Rose J. K., Doolittle R. F., Anilionis A., Curtis P. J., Wunner W. H. Homology between the glycoproteins of vesicular stomatitis virus and rabies virus. J Virol. 1982 Jul;43(1):361–364. doi: 10.1128/jvi.43.1.361-364.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Rose J. K., Gallione C. J. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. J Virol. 1981 Aug;39(2):519–528. doi: 10.1128/jvi.39.2.519-528.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. SWARTZ M. N., TRAUTNER T. A., KORNBERG A. Enzymatic synthesis of deoxyribonucleic acid. XI. Further studies on nearest neighbor base sequences in deoxyribonucleic acids. J Biol Chem. 1962 Jun;237:1961–1967. [PubMed] [Google Scholar]
  33. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  35. Taub F., Thompson E. B. An improved method for preparing large arrays of bacterial colonies containing plasmids for hybridization: in situ purification and stable binding of DNA on paper filters. Anal Biochem. 1982 Oct;126(1):222–230. doi: 10.1016/0003-2697(82)90133-6. [DOI] [PubMed] [Google Scholar]
  36. Wunner W. H., Dietzschold B., Smith C. L., Lafon M., Golub E. Antigenic variants of CVS rabies virus with altered glycosylation sites. Virology. 1985 Jan 15;140(1):1–12. doi: 10.1016/0042-6822(85)90440-4. [DOI] [PubMed] [Google Scholar]
  37. Zilberstein A., Snider M. D., Porter M., Lodish H. F. Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein. Cell. 1980 Sep;21(2):417–427. doi: 10.1016/0092-8674(80)90478-x. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES