Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1975 Aug;16(2):259–262. doi: 10.1128/jvi.16.2.259-262.1975

Fish rhabdoviruses: comparative study of protein structure.

G Lenoir, P de Kinkelin
PMCID: PMC354662  PMID: 1171263

Abstract

Proteins from four fish rhabdoviruses have been studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The viruses were: trout viral hemorrhagic septicemia (VHS), infectious hematopoietic necrosis virus (IHN), spring viremia virus of carp (SVC), and the pike fry rhabdovirus (PFR). For the two salmonid viruses (VHS-IHN), gel electrophoresis indicated the proteins, with molecular weights estimated to be 190,000, 80,000, 38,000, 25,000, and 19,000, respectively. The electrophoretic profile of the two other viruses (SVC-PFR) revealed four major proteins with molecular weights of 190,000 80,000 42,000 and 21,000, respectively. In this case a minor component with 50,000 daltons was found. For each virus only one protein was found to be glycosylated, i.e., the one with a molecular weight of 80,000. A major protein (molecular weight between 38,000 and 42,000) was found to be associated with the nucleocapsid. All these results revealed marked similarities in protein structure between the four fish rhabdoviruses and the previously well-characterized members of rhabdovirus group. However, one can distinguish two groups of viruses: the first one is composed of salmonid viruses (VHS and IHN) with a protein structure comparable to that of rabies virus and potato yellow dwarf virus; the second one is composed of carp and pike viruses, having a protein structure very similar to that of vesicular stomatitis virus.

Full text

PDF
259

Selected References

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

  1. Darlington R. W., Trafford R., Wolf K. Fish rhabdoviruses: morphology and ultrastructure of North American salmonid isolates. Arch Gesamte Virusforsch. 1972;39(1):257–264. doi: 10.1007/BF01241548. [DOI] [PubMed] [Google Scholar]
  2. Gravell M., Malsberger R. G. A permanent cell line from the fathead minnow (Pimephales promelas). Ann N Y Acad Sci. 1965 Aug 10;126(1):555–565. doi: 10.1111/j.1749-6632.1965.tb14302.x. [DOI] [PubMed] [Google Scholar]
  3. Knudson D. L., MacLeod R. The proteins of potato yellow dwarf virus. Virology. 1972 Feb;47(2):285–295. doi: 10.1016/0042-6822(72)90264-4. [DOI] [PubMed] [Google Scholar]
  4. Laporte J., Lenoir G. Structural proteins of foot-and-mouth disease virus. J Gen Virol. 1973 Aug;20(2):161–168. doi: 10.1099/0022-1317-20-2-161. [DOI] [PubMed] [Google Scholar]
  5. Lenoir G. Structural proteins of spring viremia virus of carp. Biochem Biophys Res Commun. 1973 Apr 16;51(4):895–899. doi: 10.1016/0006-291x(73)90011-9. [DOI] [PubMed] [Google Scholar]
  6. McCain B. B., Fryer J. L., Pilcher K. S. Antigenic relationships in a group of three viruses of salmonid fish by cross neutralization. Proc Soc Exp Biol Med. 1971 Jul;137(3):1042–1046. doi: 10.3181/00379727-137-35724. [DOI] [PubMed] [Google Scholar]
  7. Obijeski J. F., Marchenko A. T., Bishop D. H., Cann B. W., Murphy F. A. Comparative electrophoretic analysis of the virus proteins of four rhabdoviruses. J Gen Virol. 1974 Jan;22(1):21–33. doi: 10.1099/0022-1317-22-1-21. [DOI] [PubMed] [Google Scholar]
  8. Roy P., Clark H. F., Madore H. P., Bishop D. H. RNA polymerase associated with virions of pike fry rhabdovirus. J Virol. 1975 Feb;15(2):338–347. doi: 10.1128/jvi.15.2.338-347.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  10. Sokol F., Stancek D., Koprowski H. Structural proteins of rabies virus. J Virol. 1971 Feb;7(2):241–249. doi: 10.1128/jvi.7.2.241-249.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Stampfer M., Baltimore D. Identification of the vesicular stomatitis virus large protein as a unique viral protein. J Virol. 1973 Apr;11(4):520–526. doi: 10.1128/jvi.11.4.520-526.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Wagner R. R., Prevec L., Brown F., Summers D. F., Sokol F., MacLeod R. Classification of rhabdovirus proteins: a proposal. J Virol. 1972 Dec;10(6):1228–1230. doi: 10.1128/jvi.10.6.1228-1230.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wagner R. R., Schnaitman T. C., Snyder R. M., Schnaitman C. A. Protein composition of the structural components of vesicular stomatitis virus. J Virol. 1969 Jun;3(6):611–618. doi: 10.1128/jvi.3.6.611-618.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. de Kinkelin P., Le Berre M., Lenoir G. Rhabdovirus des poissons. I. Propriétés in vitro du virus de la maladie rouge de l'alevin de brochet. Ann Microbiol (Paris) 1974 Jan;125A(1):93–111. [PubMed] [Google Scholar]

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

RESOURCES